EC 2.3.1.1 to EC 2.3.1.50
EC 2.3.1.51 to EC 2.3.1.100
EC 2.3.1.101 to EC 2.3.1.150
EC 2.3.1.151 to EC 2.3.1.200
Accepted name: UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase
Reaction: acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate = CoA + UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate
For diagram of reaction, click here
Other name(s): WbpD; WlbB
Systematic name: acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate N-acetyltransferase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854-11862. [PMID: 19282284]
2. Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446-5455. [PMID: 19348502]
Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
Reaction: acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine = CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose
Other name(s): PseH
Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
Comments: Isolated from Helicobacter pylori. The enzyme is involved in the biosynthesis of pseudaminic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C-14C. [PMID: 16751642]
Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase
Reaction: acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine = CoA + UDP-N,N'-diacetylbacillosamine
For diagram of reaction click here.
Glossary: UDP-N,N'-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose
Other name(s): PglD
Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase
Comments: The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-aspargine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659-13669. [PMID: 17087520]
2. Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827-1836. [PMID: 18198901]
3. Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine. Biochemistry 50 (2011) 4936-4948. [PMID: 21542610]
Accepted name: octanoyl-[GcvH]:protein N-octanoyltransferase
Reaction: [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
Glossary: GcvH = glycine cleavage system H]
Other name(s): LipL; octanoyl-[GcvH]:E2 amidotransferase; ywfL (gene name)
Systematic name: [glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase
Comments: In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Christensen, Q.H., Martin, N., Mansilla, M.C., de Mendoza, D. and Cronan, J.E. A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol. Microbiol. 80 (2011) 350-363. [PMID: 21338421]
2. Martin, N., Christensen, Q.H., Mansilla, M.C., Cronan, J.E. and de Mendoza, D. A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol. Microbiol. 80 (2011) 335-349. [PMID: 21338420]
Accepted name: fumigaclavine B O-acetyltransferase
Reaction: acetyl-CoA + fumigaclavine B = CoA + fumigaclavine A
For diagram of reaction click here.
Glossary: fumigaclavine B = 6,8β-dimethylergolin-9-ol
fumigaclavine A = 6,8β-dimethylergolin-9β-yl acetate
Other name(s): FgaAT
Systematic name: acetyl-CoA:fumigaclavine B O-acetyltransferase
Comments: The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Liu, X., Wang, L., Steffan, N., Yin, W.B. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: FgaAT catalyses the acetylation of fumigaclavine B. ChemBioChem. 10 (2009) 2325-2328. [PMID: 19672909]
Accepted name: 3,5,7-trioxododecanoyl-CoA synthase
Reaction: 3 malonyl-CoA + hexanoyl-CoA = 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2
For diagram of reaction click here.
Other name(s): TKS (ambiguous); olivetol synthase (incorrect)
Systematic name: malonyl-CoA:hexanoyl-CoA malonyltransferase (3,5,7-trioxododecanoyl-CoA-forming)
Comments: A polyketide synthase catalysing the first committed step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme was previously thought to also function as a cyclase, but the cyclization is now known to be catalysed by EC 4.4.1.26, olivetolic acid cyclase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Taura, F., Tanaka, S., Taguchi, C., Fukamizu, T., Tanaka, H., Shoyama, Y. and Morimoto, S. Characterization of olivetol synthase, a polyketide synthase putatively involved in cannabinoid biosynthetic pathway. FEBS Lett 583 (2009) 2061-2066. [PMID: 19454282]
2. Gagne, S.J., Stout, J.M., Liu, E., Boubakir, Z., Clark, S.M. and Page, J.E. Identification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketides. Proc. Natl. Acad. Sci. USA 109 (2012) 12811-12816. [PMID: 22802619]
Accepted name: β-ketodecanoyl-[acyl-carrier-protein] synthase
Reaction: octanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: [acyl-carrier protein] = [acp]
Systematic name: octanoyl-CoA:malonyl-[acyl-carrier protein] C-heptanoylltransferase (decarboxylating, CoA-forming)
Comments: This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via β-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for β-oxidation degradation intermediates into de novo fatty acid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yuan, Y., Leeds, J.A. and Meredith, T.C. Pseudomonas aeruginosa directly shunts β-oxidation degradation intermediates into de novo fatty acid biosynthesis. J. Bacteriol. (2012) . [PMID: 22753057]
Accepted name: 4-hydroxycoumarin synthase
Reaction: malonyl-CoA + 2-hydroxybenzoyl-CoA = 2 CoA + 4-hydroxycoumarin + CO2
For diagram of reaction click here.
Glossary: 2-hydroxybenzoyl-CoA = salicyloyl-CoA
Other name(s): BIS2; BIS3
Systematic name: malonyl-CoA:2-hydroxybenzoyl-CoA malonyltransferase
Comments: The enzyme, a polyketide synthase, can also accept benzoyl-CoA as substrate, which it condenses with 3 malonyl-CoA molecules to form 3,5-dihydroxybiphenyl (cf. EC 2.3.1.177, biphenyl synthase) [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Liu, B., Raeth, T., Beuerle, T. and Beerhues, L. A novel 4-hydroxycoumarin biosynthetic pathway. Plant Mol. Biol. 72 (2010) 17-25. [PMID: 19757094]
Accepted name: dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
Reaction: acetyl-CoA + dTDP-4-amino-4,6-dideoxy-α-D-glucose = CoA + dTDP-4-acetamido-4,6-dideoxy-α-D-glucose
Other name(s): VioB
Systematic name: acetyl-CoA:dTDP-4-amino-4,6-dideoxy-α-D-glucose N-acetyltransferase
Comments: The non-activated product, 4-acetamido-4,6-dideoxy-α-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wang, Y., Xu, Y., Perepelov, A.V., Qi, Y., Knirel, Y.A., Wang, L. and Feng, L. Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7. J. Bacteriol. 189 (2007) 8626-8635. [PMID: 17905981]
Accepted name: dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
Reaction: acetyl-CoA + dTDP-4-amino-4,6-dideoxy-α-D-galactose = CoA + dTDP-4-acetamido-4,6-dideoxy-α-D-galactose
For diagram of reaction click here.
Glossary: dTDP-4-amino-4,6-dideoxy-α-D-galactose = dTDP-α-D-fucosamine
Other name(s): TDP-fucosamine acetyltransferase; WecD; RffC
Systematic name: acetyl-CoA:dTDP-4-amino-4,6-dideoxy-α-D-galactose N-acetyltransferase
Comments: The product, TDP-4-acetamido-4,6-dideoxy-D-galactose, is utilized in the biosynthesis of enterobacterial common antigen (ECA).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hung, M.N., Rangarajan, E., Munger, C., Nadeau, G., Sulea, T. and Matte, A. Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis. J. Bacteriol. 188 (2006) 5606-5617. [PMID: 16855251]
Accepted name: bisdemethoxycurcumin synthase
Reaction: 2 4-coumaroyl-CoA + malonyl-CoA + H2O = 3 CoA + bisdemethoxycurcumin + 2 CO2
For diagram of reaction click here.
Glossary: bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
Other name(s): CUS; curcuminoid synthase (ambiguous)
Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (bisdemethoxycurcumin-forming)
Comments: A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyses the formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin. Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes (EC 2.3.1.218, phenylpropanoyl-diketide CoA synthase and EC 2.3.1.217, curcumin synthase), the diketide intermediate formed by this enzyme remains within the enzyme's cavity and is not released to the environment.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Morita, H., Wanibuchi, K., Nii, H., Kato, R., Sugio, S. and Abe, I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc. Natl. Acad. Sci. USA 107 (2010) 19778-19783. [PMID: 21041675]
Accepted name: benzalacetone synthase
Reaction: 4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2
For diagram of reaction click here.
Glossary: 4-hydroxybenzalacetone = 4-(4-hydroxyphenyl)but-3-en-2-one
Other name(s): BAS
Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (4-hydroxybenzalacetone-forming)
Comments: A polyketide synthase that catalyses the C6-C4 skeleton of phenylbutanoids in higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Borejsza-Wysocki, W. and Hrazdina, G. Aromatic polyketide synthases (purification, characterization, and antibody development to benzalacetone synthase from raspberry fruits). Plant Physiol. 110 (1996) 791-799. [PMID: 12226219]
2. Abe, I., Takahashi, Y., Morita, H. and Noguchi, H. Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum. Eur. J. Biochem. 268 (2001) 3354-3359. [PMID: 11389739]
3. Zheng, D. and Hrazdina, G. Molecular and biochemical characterization of benzalacetone synthase and chalcone synthase genes and their proteins from raspberry (Rubus idaeus L.). Arch. Biochem. Biophys. 470 (2008) 139-145. [PMID: 18068110]
4. Morita, H., Shimokawa, Y., Tanio, M., Kato, R., Noguchi, H., Sugio, S., Kohno, T. and Abe, I. A structure-based mechanism for benzalacetone synthase from Rheum palmatum. Proc. Natl. Acad. Sci. USA 107 (2010) 669-673. [PMID: 20080733]
Accepted name: cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6'''-O-hydroxycinnamoyltransferase
Reaction: 1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside]
For diagram of reaction click here.
Glossary: 1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3',4',5,7-pentahydroxyflavylium
Other name(s): 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6'''-O-(4-hydroxycinnamoyl)transferase
Systematic name: 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6'''-O-(4-hydroxycinnamoyl)transferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582-585.
Accepted name: pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4'''-malonyltransferase
Reaction: malonyl-CoA + 4'''-demalonylsalvianin = CoA + salvianin
For diagram of reaction click here.
Glossary: salvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(4,6-di-O-malonyl-β-D-glucoside)
4'''-demalonylsalvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(6-O-malonyl-β-D-glucoside)
Other name(s): malonyl-CoA:anthocyanin 5-glucoside 4'''-O-malonyltransferase; Ss5MaT2
Systematic name: malonyl-CoA:4'''-demalonylsalvianin 4'''-O-malonyltransferase
Comments: Isolated from the plant Salvia splendens (scarlet sage).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Suzuki, H., Sawada, S., Watanabe, K., Nagae, S., Yamaguchi, M.A., Nakayama, T. and Nishino, T. Identification and characterization of a novel anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers: an enzyme that is phylogenetically separated from other anthocyanin acyltransferases. Plant J. 38 (2004) 994-1003. [PMID: 15165190]
Accepted name: anthocyanidin 3-O-glucoside 6''-O-acyltransferase
Reaction: 4-hydroxycinnamoyl-CoA + an anthocyanidin 3-O-β-D-glucoside = CoA + an anthocyanidin 3-O-[6-O-(4-hydroxycinnamoyl)-β-D-glucoside]
For diagram of reaction click here.
Glossary: 4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA
3,4-dihydroxycinnamoyl-CoA = caffeoyl-CoA
cyanidin = 3,3',4',5,7-pentahydroxyflavylium
delphinidin = 3,3',4',5,5',7-hexahydroxyflavylium
Systematic name: 4-hydroxycinnamoyl-CoA:anthocyanin-3-O-glucoside 6''-O-acyltransferase
Comments: Isolated from the plants Perilla frutescens and Gentiana triflora (clustered gentian). Acts on a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside. It did not act on delphinidin 3,3',7-tri-O-glucoside. Recombinant Perilla frutescens enzyme could utilize caffeoyl-CoA but not malonyl-CoA as alternative acyl donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fujiwara, H., Tanaka, Y., Fukui, Y., Ashikari, T., Yamaguchi, M. and Kusumi, T. Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens. Plant Sci. 137 (1998) 87-94.
2. Yonekura-Sakakibara, K., Tanaka, Y., Fukuchi-Mizutani, M., Fujiwara, H., Fukui, Y., Ashikari, T., Murakami, Y., Yamaguchi, M. and Kusumi, T. Molecular and biochemical characterization of a novel hydroxycinnamoyl-CoA: anthocyanin 3-O-glucoside-6"-O-acyltransferase from Perilla frutescens. Plant Cell Physiol 41 (2000) 495-502. [PMID: 10845463]
Accepted name: 5,7-dihydroxy-2-methylchromone synthase
Reaction: 5 malonyl-CoA = 5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O
For diagram of reaction click here.
Other name(s): pentaketide chromone synthase
Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (5,7-dihydroxy-2-methyl-4H-chromen-4-one-forming)
Comments: A polyketide synthase from the plant Aloe arborescens (aloe).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Abe, I., Utsumi, Y., Oguro, S., Morita, H., Sano, Y. and Noguchi, H. A plant type III polyketide synthase that produces pentaketide chromone. J. Am. Chem. Soc. 127 (2005) 1362-1363. [PMID: 15686354]
Accepted name: curcumin synthase
Reaction: feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2
For diagram of reaction click here.
Glossary: curcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
Other name(s): CURS; CURS1 (gene name); CURS2 (gene name); CURS3 (gene name)
Systematic name: feruloyl-CoA:feruloylacetyl-CoA feruloyltransferase (curcumin-forming)
Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well [2] (see EC 2.3.1.219, demethoxycurcumin synthase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160-11170. [PMID: 19258320]
2. Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett 583 (2009) 2799-2803. [PMID: 19622354]
3. Katsuyama, Y., Miyazono, K., Tanokura, M., Ohnishi, Y. and Horinouchi, S. Structural and biochemical elucidation of mechanism for decarboxylative condensation of β-keto acid by curcumin synthase. J. Biol. Chem. 286 (2011) 6659-6668. [PMID: 21148316]
Accepted name: phenylpropanoylacetyl-CoA synthase
Reaction: (1) feruloyl-CoA + malonyl-CoA = feruloylacetyl-CoA + CO2 + CoA
(2) 4-coumaroyl-CoA + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO2 + CoA
For diagram of reaction click here.
Glossary: feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
phenylpropanoylacetyl-CoA = phenylpropanoyl-diketide-CoA
Other name(s): phenylpropanoyl-diketide-CoA synthase; DCS
Systematic name: phenylpropanoyl-CoA:malonyl-CoA phenylpropanoyl-transferase (decarboxylating)
Comments: The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160-11170. [PMID: 19258320]
Accepted name: demethoxycurcumin synthase
Reaction: (1) 4-coumaroyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + demethoxycurcumin + CO2
(2) 4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O = 2 CoA + bisdemethoxycurcumin + CO2
For diagram of reaction click here.
Glossary: demethoxycurcumin = (1E,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
Other name(s): CURS3
Systematic name: 4-coumaroyl-CoA:feruloylacetyl-CoA feruloyltransferase (demethoxycurcumin-forming)
Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett 583 (2009) 2799-2803. [PMID: 19622354]
Accepted name: 2,4,6-trihydroxybenzophenone synthase
Reaction: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
For diagram of reaction click here.
Other name(s): benzophenone synthase (ambiguous); BPS (ambiguous)
Systematic name: malonyl-CoA:benzoyl-CoA malonyltransferase (2,4,6-trihydroxybenzophenone-forming)
Comments: Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3',4,6-tetrahydroxybenzophenone synthase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Schmidt, W. and Beerhues, L. Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum L. FEBS Lett 420 (1997) 143-146. [PMID: 9459298]
2. Nualkaew, N., Morita, H., Shimokawa, Y., Kinjo, K., Kushiro, T., De-Eknamkul, W., Ebizuka, Y. and Abe, I. Benzophenone synthase from Garcinia mangostana L. pericarps. Phytochemistry 77 (2012) 60-69. [PMID: 22390826]
Accepted name: noranthrone synthase
Reaction: 7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
For diagram of reaction click here.
Glossary: norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
Other name(s): polyketide synthase A (ambiguous); PksA (ambiguous); norsolorinic acid anthrone synthase
Systematic name: malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Crawford, J.M., Thomas, P.M., Scheerer, J.R., Vagstad, A.L., Kelleher, N.L. and Townsend, C.A. Deconstruction of iterative multidomain polyketide synthase function. Science 320 (2008) 243-246. [PMID: 18403714]
2. Crawford, J.M., Korman, T.P., Labonte, J.W., Vagstad, A.L., Hill, E.A., Kamari-Bidkorpeh, O., Tsai, S.C. and Townsend, C.A. Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461 (2009) 1139-1143. [PMID: 19847268]
3. Korman, T.P., Crawford, J.M., Labonte, J.W., Newman, A.G., Wong, J., Townsend, C.A. and Tsai, S.C. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 6246-6251. [PMID: 20332208]
Accepted name: phosphate propanoyltransferase
Reaction: propanoyl-CoA + phosphate = CoA + propanoyl phosphate
Other name(s): PduL
Systematic name: propanoyl-CoA:phosphate propanoyltransferase
Comments: Part of the degradation pathway for propane-1,2-diol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Liu, Y., Leal, N.A., Sampson, E.M., Johnson, C.L., Havemann, G.D. and Bobik, T.A. PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 189 (2007) 1589-1596. [PMID: 17158662]
Accepted name: 3-oxo-5,6-didehydrosuberyl-CoA thiolase
Reaction: 2,3-didehydroadipoyl-CoA + acetyl-CoA = CoA + 3-oxo-5,6-didehydrosuberoyl-CoA
Glossary: 2,3-didehydroadipoyl-CoA = 5-carboxypent-2-enoyl-CoA
3-oxo-5,6-didehydrosuberoyl-CoA = 7-carboxy-3-oxohept-5-enoyl-CoA
Other name(s): paaJ (gene name)
Systematic name: 2,3-didehydroadipoyl-CoA:acetyl-CoA C-didehydroadipoyltransferase (double bond migration)
Comments: The enzyme acts in the opposite direction. The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174 (3-oxoadipyl-CoA thiolase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Teufel, R., Mascaraque, V., Ismail, W., Voss, M., Perera, J., Eisenreich, W., Haehnel, W. and Fuchs, G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. USA 107 (2010) 14390-14395. [PMID: 20660314]
Accepted name: acetyl-CoA-benzylalcohol acetyltransferase
Reaction: (1) acetyl-CoA + benzyl alcohol = CoA + benzyl acetate
(2) acetyl-CoA + cinnamyl alcohol = CoA + cinnamyl acetate
Other name(s): BEAT
Systematic name: acetyl-CoA:benzylalcohol O-acetyltransferase
Comments: The enzyme is found in flowers like Clarkia breweri, where it is important for floral scent production. Unlike EC 2.3.1.84, alcohol O-acetyltransferase, this enzyme is active with alcohols that contain a benzyl ring.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Dudareva, N., D'Auria, J.C., Nam, K.H., Raguso, R.A. and Pichersky, E. Acetyl-CoA:benzylalcohol acetyltransferase - an enzyme involved in floral scent production in Clarkia breweri. Plant J. 14 (1998) 297-304. [PMID: 9628024]
Accepted name: protein S-acyltransferase
Reaction: palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
Other name(s): DHHC palmitoyl transferase; S-protein acyltransferase; G-protein palmitoyltransferase
Systematic name: palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase
Comments: The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Dunphy, J.T., Greentree, W.K., Manahan, C.L. and Linder, M.E. G-protein palmitoyltransferase activity is enriched in plasma membranes. J. Biol. Chem. 271 (1996) 7154-7159. [PMID: 8636152]
2. Veit, M., Dietrich, L.E. and Ungermann, C. Biochemical characterization of the vacuolar palmitoyl acyltransferase. FEBS Lett 540 (2003) 101-105. [PMID: 12681491]
3. Batistic, O. Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family. Plant Physiol. 160 (2012) 1597-1612. [PMID: 22968831]
4. Jennings, B.C. and Linder, M.E. DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities. J. Biol. Chem. 287 (2012) 7236-7245. [PMID: 22247542]
5. Zhou, L.Z., Li, S., Feng, Q.N., Zhang, Y.L., Zhao, X., Zeng, Y.L., Wang, H., Jiang, L. and Zhang, Y. Protein S-acyl transferase10 is critical for development and salt tolerance in Arabidopsis. Plant Cell 25 (2013) 1093-1107. [PMID: 23482856]
Accepted name: carboxymethylproline synthase
Reaction: malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2
Other name(s): CarB (ambiguous)
Systematic name: malonyl-CoA:(S)-1-pyrroline-5-carboxylate malonyltransferase (cyclizing)
Comments: The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, PDB, CAS registry number:
References:
1. Sleeman, M.C. and Schofield, C.J. Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis. J. Biol. Chem. 279 (2004) 6730-6736. [PMID: 14625287]
2. Gerratana, B., Arnett, S.O., Stapon, A. and Townsend, C.A. Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase superfamily. Biochemistry 43 (2004) 15936-15945. [PMID: 15595850]
3. Sorensen, J.L., Sleeman, M.C. and Schofield, C.J. Synthesis of deuterium labelled L- and D-glutamate semialdehydes and their evaluation as substrates for carboxymethylproline synthase (CarB)—implications for carbapenem biosynthesis. Chem. Commun. (Camb.) (2005) 1155-1157. [PMID: 15726176]
4. Sleeman, M.C., Sorensen, J.L., Batchelar, E.T., McDonough, M.A. and Schofield, C.J. Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis. J. Biol. Chem. 280 (2005) 34956-34965. [PMID: 16096274]
5. Batchelar, E.T., Hamed, R.B., Ducho, C., Claridge, T.D., Edelmann, M.J., Kessler, B. and Schofield, C.J. Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily. Angew. Chem. Int. Ed. Engl. 47 (2008) 9322-9325. [PMID: 18972478]
6. Hamed, R.B., Gomez-Castellanos, J.R., Thalhammer, A., Harding, D., Ducho, C., Claridge, T.D. and Schofield, C.J. Stereoselective C-C bond formation catalysed by engineered carboxymethylproline synthases. Nat. Chem. 3 (2011) 365-371. [PMID: 21505494]
Accepted name: GDP-perosamine N-acetyltransferase
Reaction: acetyl-CoA + GDP-4-amino-4,6-dideoxy-α-D-mannose = CoA + GDP-4-acetamido-4,6-dideoxy-α-D-mannose
Glossary: GDP-4-amino-4,6-dideoxy-α-D-mannose = GDP-α-D-perosamine
GDP-4-acetamido-4,6-dideoxy-α-D-mannose = GDP-N-acetyl-α-D-perosamine
Other name(s): perB (gene name); GDP-α-D-perosamine N-acetyltransferase
Systematic name: acetyl-CoA:GDP-4-amino-4,6-dideoxy-α-D-mannose N-acetyltransferase
Comments: D-Perosamine is one of several dideoxy sugars found in the O-antigen component of the outer membrane lipopolysaccharides of Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Albermann, C. and Beuttler, H. Identification of the GDP-N-acetyl-D-perosamine producing enzymes from Escherichia coli O157:H7. FEBS Lett 582 (2008) 479-484. [PMID: 18201574]
Accepted name: isovaleryl-homoserine lactone synthase
Reaction: isovaleryl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5'-thioadenosine + N-isovaleryl-L-homoserine lactone
Glossary: S -methyl-5'-thioadenosine = 5'-deoxy-5'-(methylsulfanyl)adenosine
Other name(s): IV-HSL synthase; BjaI
Systematic name: isovaleryl-CoA:S-adenosyl-L-methionine isovaleryltranserase (lactone-forming, methylthioadenosine-releasing)
Comments: The enzyme, found in the bacterium Bradyrhizobium japonicum, does not accept isovaleryl-[acyl-carrier protein] as acyl donor (cf. EC 2.3.1.184, acyl-homoserine-lactone synthase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lindemann, A., Pessi, G., Schaefer, A.L., Mattmann, M.E., Christensen, Q.H., Kessler, A., Hennecke, H., Blackwell, H.E., Greenberg, E.P. and Harwood, C.S. Isovaleryl-homoserine lactone, an unusual branched-chain quorum-sensing signal from the soybean symbiont Bradyrhizobium japonicum. Proc. Natl. Acad. Sci. USA 108 (2011) 16765-16770. [PMID: 21949379]
Accepted name: 4-coumaroyl-homoserine lactone synthase
Reaction: 4-coumaroyl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
Glossary: S -methyl-5'-thioadenosine = 5'-deoxy-5'-(methylsulfanyl)adenosine
Other name(s): p-coumaryl-homoserine lactone synthase; RpaI
Systematic name: 4-coumaroyl-CoA:S-adenosyl-L-methionine trans-4-coumaroyltranserase (lactone-forming, methylthioadenosine-releasing)
Comments: The enzyme is found in the bacterium Rhodopseudomonas palustris, which produces N-(4-coumaroyl)-L-homoserine lactone as a quorum-sensing signal.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Schaefer, A.L., Greenberg, E.P., Oliver, C.M., Oda, Y., Huang, J.J., Bittan-Banin, G., Peres, C.M., Schmidt, S., Juhaszova, K., Sufrin, J.R. and Harwood, C.S. A new class of homoserine lactone quorum-sensing signals. Nature 454 (2008) 595-599. [PMID: 18563084]
Accepted name: 2-heptyl-4(1H)-quinolone synthase
Reaction: octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O (overall reaction)
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O
Glossary: 2-heptyl-4(1H)-quinolone = 2-heptyl-4-hydroxyquinoline
Other name(s): pqsBC (gene names); malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating)
Systematic name: octanoyl-CoA:(2-aminobenzoyl)acetate octanoyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the Pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481-1491. [PMID: 24239007]
2. Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. and Fetzner, S. PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone Signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291 (2016) 6610-6624. [PMID: 26811339]
Accepted name: tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase
Reaction: S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe + CO2 = S-adenosyl-L-homocysteine + wybutosine37 in tRNAPhe
For diagram of reaction, click here
Glossary: wyosine = 4,6-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
wybutosine = yW = 7-{(3S)-3-(methoxycarbonyl)-3-(methoxycarbonylamino)propyl}-4,5-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
Other name(s): TYW4 (ambiguous); tRNA-yW synthesizing enzyme-4 (ambiguous)
Systematic name: S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methyltransferase (carbon dioxide-adding)
Comments: The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-[2-hydroxy-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.1.1.290, tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Noma, A., Kirino, Y., Ikeuchi, Y. and Suzuki, T. Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J. 25 (2006) 2142-2154. [PMID: 16642040]
2. Suzuki, Y., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4. Nucleic Acids Res. 37 (2009) 2910-2925. [PMID: 19287006]
3. Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and Nureki, O. Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification. Nucleic Acids Res. 39 (2011) 1576-1585. [PMID: 20972222]
Accepted name: methanol O-anthraniloyltransferase
Reaction: anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate
Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA
Other name(s): AMAT; anthraniloyl-coenzyme A (CoA):methanol acyltransferase
Systematic name: anthraniloyl-coenzyme A:methanol O-anthraniloyltransferase
Comments: The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes. Also catalyses EC 2.3.1.196, benzyl alcohol O-benzoyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wang, J. and De Luca, V. The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate. Plant J. 44 (2005) 606-619. [PMID: 16262710]
Accepted name: 1,3,6,8-tetrahydroxynaphthalene synthase
Reaction: 5 malonyl-CoA = 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
For diagram of reaction click here.
Other name(s): PKS1; THNS; SCO1206; RppA
Systematic name: malonyl-CoA C-acyl transferase (1,3,6,8-tetrahydroxynaphthalene forming)
Comments: Isolated from the fungus Colletotrichum lagenarium [1], and the bacteria Streptomyces coelicolor [2,3] and Streptomyces peucetius [4]. It only uses malonyl-CoA, without invovement of acetyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Fujii, I., Mori, Y., Watanabe, A., Kubo, Y., Tsuji, G. and Ebizuka, Y. Enzymatic synthesis of 1,3,6,8-tetrahydroxynaphthalene solely from malonyl coenzyme A by a fungal iterative type I polyketide synthase PKS1. Biochemistry 39 (2000) 8853-8858. [PMID: 10913297]
2. Izumikawa, M., Shipley, P.R., Hopke, J.N., O'Hare, T., Xiang, L., Noel, J.P. and Moore, B.S. Expression and characterization of the type III polyketide synthase 1,3,6,8-tetrahydroxynaphthalene synthase from Streptomyces coelicolor A3(2). J Ind Microbiol Biotechnol 30 (2003) 510-515. [PMID: 12905073]
3. Austin, M.B., Izumikawa, M., Bowman, M.E., Udwary, D.W., Ferrer, J.L., Moore, B.S. and Noel, J.P. Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates. J. Biol. Chem. 279 (2004) 45162-45174. [PMID: 15265863]
4. Ghimire, G.P., Oh, T.J., Liou, K. and Sohng, J.K. Identification of a cryptic type III polyketide synthase (1,3,6,8-tetrahydroxynaphthalene synthase) from Streptomyces peucetius ATCC 27952. Mol. Cells 26 (2008) 362-367. [PMID: 18612244]
Accepted name: N6-L-threonylcarbamoyladenine synthase
Reaction: L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N6-L-threonylcarbamoyladenine37 in tRNA
For diagram of reaction click here.
Glossary: N6-L-threonylcarbamoyladenine37 = t6A37
Other name(s): t6A synthase; Kae1; ygjD (gene name); Qri7
Systematic name: L-threonylcarbamoyladenylate:adenine37 in tRNA N6-L-threonylcarbamoyltransferase
Comments: The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Lauhon, C.T. Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Biochemistry 51 (2012) 8950-8963. [PMID: 23072323]
2. Deutsch, C., El Yacoubi, B., de Crecy-Lagard, V. and Iwata-Reuyl, D. Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside. J. Biol. Chem. 287 (2012) 13666-13673. [PMID: 22378793]
3. Perrochia, L., Crozat, E., Hecker, A., Zhang, W., Bareille, J., Collinet, B., van Tilbeurgh, H., Forterre, P. and Basta, T. In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya. Nucleic Acids Res. 41 (2013) 1953-1964. [PMID: 23258706]
4. Wan, L.C.K., Mao, D.Y.L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R.K., Lissina, E., Nislow, C., Caudy, A.A., Durocher, D. and Sicheri, F. Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. 41 (2013) 6332-6346. [PMID: 23620299]
Accepted name: tetracenomycin F2 synthase
Reaction: 10 malonyl-CoA = tetracenomycin F2 + 10 CoA + 10 CO2 + 2 H2O
For diagram of reaction click here.
Glossary: tetracenomycin F2 = 4-(3-acetyl-4,5,7,10-tetrahydroxyanthracen-2-yl)-3-oxobutanoic acid
Other name(s): TCM PKS
Systematic name: malonyl-CoA:acetate malonyltransferase (tetracenomycin F2 forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of tetracenomycin in the bacterium Streptomyces glaucescens. It involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN). A malonyl-CoA molecule is initially bound to the acyl carrier protein and decarboxylated to form an acetyl starter unit. Additional two-carbon units are added from nine more malonyl-CoA molecules.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bao, W., Wendt-Pienkowski, E. and Hutchinson, C.R. Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry 37 (1998) 8132-8138. [PMID: 9609708]
Accepted name: 5-methylnaphthoic acid synthase
Reaction: acetyl-CoA + 5 malonyl-CoA + 3 NADPH + 3 H+ = 5-methyl-1-naphthoate + 6 CoA + 5 CO2 + 4 H2O + 3 NADP+
For diagram of reaction click here.
Other name(s): AziB
Systematic name: malonyl-CoA:acetyl-CoA malonyltransferase (5-methyl-1-naphthoic acid forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of azinomycin B in the bacterium Streptomyces griseofuscus.
References:
1. Zhao, Q., He, Q., Ding, W., Tang, M., Kang, Q., Yu, Y., Deng, W., Zhang, Q., Fang, J., Tang, G. and Liu, W. Characterization of the azinomycin B biosynthetic gene cluster revealing a different iterative type I polyketide synthase for naphthoate biosynthesis. Chem. Biol. 15 (2008) 693-705. [PMID: 18635006]
Accepted name: neocarzinostatin naphthoate synthase
Reaction: acetyl-CoA + 5 malonyl-CoA + 2 NADPH + 2 H+ = 2-hydroxy-5-methyl-1-naphthoate + 6 CoA + 5 CO2 + 3 H2O + 2 NADP+
For diagram of reaction click here.
Other name(s): naphthoic acid synthase; NNS; ncsB (gene name)
Systematic name: malonyl-CoA:acetyl-CoA malonyltransferase (2-hydroxy-5-methyl-1-naphthoic acid forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sthapit, B., Oh, T.J., Lamichhane, R., Liou, K., Lee, H.C., Kim, C.G. and Sohng, J.K. Neocarzinostatin naphthoate synthase: an unique iterative type I PKS from neocarzinostatin producer Streptomyces carzinostaticus. FEBS Lett 566 (2004) 201-206. [PMID: 15147895]
Accepted name: monacolin J acid methylbutanoate transferase
Reaction: monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] = lovastatin acid + [2-methylbutanoate polyketide synthase]
For diagram of reaction click here.
Glossary: monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
lovastatin acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-{[(2S)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovD
Systematic name: monacolin J acid:(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] (S)-2-methylbutanoate transferase
Comments: The enzyme catalyses the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368-1372. [PMID: 10334994]
2. Xie, X., Watanabe, K., Wojcicki, W.A., Wang, C.C. and Tang, Y. Biosynthesis of lovastatin analogs with a broadly specific acyltransferase. Chem. Biol. 13 (2006) 1161-1169. [PMID: 17113998]
3. Xie, X., Meehan, M.J., Xu, W., Dorrestein, P.C. and Tang, Y. Acyltransferase mediated polyketide release from a fungal megasynthase. J. Am. Chem. Soc. 131 (2009) 8388-8389. [PMID: 19530726]
Accepted name: 10-deoxymethynolide synthase
Reaction: malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O
For diagram of reaction click here.
Other name(s): pikromycin PKS
Systematic name: (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (10-deoxymethynolide forming)
Comments: The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae. The enzyme also produces narbonolide (see EC 2.3.1.240, narbonolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Lu, H., Tsai, S.C., Khosla, C. and Cane, D.E. Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. Biochemistry 41 (2002) 12590-12597. [PMID: 12379101]
2. Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W. and Sherman, D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944-954. [PMID: 17719493]
3. Yan, J., Gupta, S., Sherman, D.H. and Reynolds, K.A. Functional dissection of a multimodular polypeptide of the pikromycin polyketide synthase into monomodules by using a matched pair of heterologous docking domains. Chembiochem 10 (2009) 1537-1543. [PMID: 19437523]
4. Whicher, J.R., Dutta, S., Hansen, D.A., Hale, W.A., Chemler, J.A., Dosey, A.M., Narayan, A.R., Hakansson, K., Sherman, D.H., Smith, J.L. and Skiniotis, G. Structural rearrangements of a polyketide synthase module during its catalytic cycle. Nature 510 (2014) 560-564. [PMID: 24965656]
Accepted name: narbonolide synthase
Reaction: malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O
For diagram of reaction click here.
Other name(s): pikromycin PKS
Systematic name: (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (narbonolide forming)
Comments: The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae. The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239, 10-deoxymethynolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Lu, H., Tsai, S.C., Khosla, C. and Cane, D.E. Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. Biochemistry 41 (2002) 12590-12597. [PMID: 12379101]
2. Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W. and Sherman, D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944-954. [PMID: 17719493]
3. Yan, J., Gupta, S., Sherman, D.H. and Reynolds, K.A. Functional dissection of a multimodular polypeptide of the pikromycin polyketide synthase into monomodules by using a matched pair of heterologous docking domains. Chembiochem 10 (2009) 1537-1543. [PMID: 19437523]
4. Whicher, J.R., Dutta, S., Hansen, D.A., Hale, W.A., Chemler, J.A., Dosey, A.M., Narayan, A.R., Hakansson, K., Sherman, D.H., Smith, J.L. and Skiniotis, G. Structural rearrangements of a polyketide synthase module during its catalytic cycle. Nature 510 (2014) 560-564. [PMID: 24965656]
Accepted name: Kdo2-lipid IVA acyltransferase
Reaction: a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] + an [acyl-carrier protein]
For diagram of reaction, click here
Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose
Other name(s): LpxL; htrB (gene name); dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-dodecanoyltransferase; lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase; (Kdo)2-lipid IVA lauroyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA lauroyltransferase; dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase; Kdo2-lipid IVA lauroyltransferase
Systematic name: fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] O-acyltransferase
Comments: The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Clementz, T., Bednarski, J.J. and Raetz, C.R. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271 (1996) 12095-12102. [PMID: 8662613]
2. van der Ley, P., Steeghs, L., Hamstra, H.J., ten Hove, J., Zomer, B. and van Alphen, L. Modification of lipid A biosynthesis in Neisseria meningitidis lpxL mutants: influence on lipopolysaccharide structure, toxicity, and adjuvant activity. Infect. Immun. 69 (2001) 5981-5990. [PMID: 11553534]
3. McLendon, M.K., Schilling, B., Hunt, J.R., Apicella, M.A. and Gibson, B.W. Identification of LpxL, a late acyltransferase of Francisella tularensis, Infect. Immun. 75 (2007) 5518-5531. [PMID: 17724076]
4. Six, D.A., Carty, S.M., Guan, Z. and Raetz, C.R. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47 (2008) 8623-8637. [PMID: 18656959]
5. Fathy Mohamed, Y., Hamad, M., Ortega, X.P. and Valvano, M.A. The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia, Mol. Microbiol. 104 (2017) 144-162. [PMID: 28085228]
Accepted name: Kdo2-lipid IVA palmitoleoyltransferase
Reaction: a (9Z)-hexadec-9-enoyl-[acyl-carrier protein] + Kdo2-lipid IVA = (9Z)-hexadec-9-enoyl-Kdo2-lipid IVA + an [acyl-carrier protein]
For diagram of reaction click here.
Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA
(9Z)-hexadec-9-enoyl = palmitoleoyl
(9Z)-hexadec-9-enoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-{(3R)-3-[(9Z)-hexadec-9-enoyloxy]tetradecanamido}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Other name(s): LpxP; palmitoleoyl-acyl carrier protein-dependent acyltransferase; cold-induced palmitoleoyl transferase; palmitoleoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase; (Kdo)2-lipid IVA palmitoleoyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA palmitoleoyltransferase
Systematic name: (9Z)-hexadec-9-enoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-palmitoleoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Carty, S.M., Sreekumar, K.R. and Raetz, C.R. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274 (1999) 9677-9685. [PMID: 10092655]
2. Vorachek-Warren, M.K., Carty, S.M., Lin, S., Cotter, R.J. and Raetz, C.R. An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C. J. Biol. Chem. 277 (2002) 14186-14193. [PMID: 11830594]
Accepted name: acyl-Kdo2-lipid IVA acyltransferase
Reaction: a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)2-[lipid IVA] + an [acyl-carrier protein]
For diagram of reaction click here
Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)2-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-(acyloxy)acyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
Other name(s): lpxM (gene name); MsbB acyltransferase; myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase; tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase; lauroyl-Kdo2-lipid IVA myristoyltransferase
Systematic name: fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] O-acyltransferase
Comments: The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Clementz, T., Zhou, Z. and Raetz, C.R. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB. J. Biol. Chem. 272 (1997) 10353-10360. [PMID: 9099672]
2. Dovala, D., Rath, C.M., Hu, Q., Sawyer, W.S., Shia, S., Elling, R.A., Knapp, M.S. and Metzger, L.E., 4th. Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism. Proc. Natl. Acad. Sci. USA 113 (2016) E6064-E6071. [PMID: 27681620]
Accepted name: 2-methylbutanoate polyketide synthase
Reaction: acetyl-CoA + malonyl-CoA + [2-methylbutanoate polyketide synthase] + 2 NADPH + 2 H+ + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CoA + CO2 + 2 NADP+ + S-adenosyl-L-homocysteine + H2O
For diagram of reaction click here.
Other name(s): LovF
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (2-methylbutanoate-forming)
Comments: This polyketide synthase enzyme forms the (S)-2-methylbutanoate side chain during lovastatin biosynthesis by the filamentous fungus Aspergillus terreus. The overall reaction comprises a single condensation reaction followed by α-methylation, β-ketoreduction, dehydration, and α,β enoyl reduction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368-1372. [PMID: 10334994]
2. Meehan, M.J., Xie, X., Zhao, X., Xu, W., Tang, Y. and Dorrestein, P.C. FT-ICR-MS characterization of intermediates in the biosynthesis of the α-methylbutyrate side chain of lovastatin by the 277 kDa polyketide synthase LovF. Biochemistry 50 (2011) 287-299. [PMID: 21069965]
Accepted name: 3-hydroxy-5-phosphooxypentane-2,4-dione thiolase
Reaction: glycerone phosphate + acetyl-CoA = 3-hydroxy-2,4-dioxopentyl phosphate + CoA
Glossary: (4S)-4,5-dihydroxypentane-2,3-dione = autoinducer 2 = AI-2
Other name(s): lsrF (gene name); 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
Systematic name: acetyl-CoA:glycerone phosphate C-acetyltransferase
Comments: The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Diaz, Z., Xavier, K.B. and Miller, S.T. The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF. PLoS One 4 (2009) e6820. [PMID: 19714241]
2. Marques, J.C., Oh, I.K., Ly, D.C., Lamosa, P., Ventura, M.R., Miller, S.T. and Xavier, K.B. LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2. Proc. Natl. Acad. Sci. USA 111 (2014) 14235-14240. [PMID: 25225400]
Accepted name: 3,5-dihydroxyphenylacetyl-CoA synthase
Reaction: 4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
Other name(s): DpgA
Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (3,5-dihydroxyphenylacetyl-CoA-forming)
Comments: The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the nonproteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Pfeifer, V., Nicholson, G.J., Ries, J., Recktenwald, J., Schefer, A.B., Shawky, R.M., Schroder, J., Wohlleben, W. and Pelzer, S. A polyketide synthase in glycopeptide biosynthesis: the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine. J. Biol. Chem. 276 (2001) 38370-38377. [PMID: 11495926]
2. Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901-14906. [PMID: 11752437]
3. Tseng, C.C., McLoughlin, S.M., Kelleher, N.L. and Walsh, C.T. Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase. Biochemistry 43 (2004) 970-980. [PMID: 14744141]
4. Wu, H.C., Li, Y.S., Liu, Y.C., Lyu, S.Y., Wu, C.J. and Li, T.L. Chain elongation and cyclization in type III PKS DpgA. Chembiochem 13 (2012) 862-871. [PMID: 22492619]
Accepted name: (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase
Reaction: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = acetoacetate + L-3-aminobutanoyl-CoA
For diagram of reaction, click here
Glossary: L-3-aminobutyryl-CoA = (3S)-3-aminobutanoyl-CoA
Other name(s): kce (gene name); 3-keto-5-aminohexanoate cleavage enzyme
Systematic name: (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase
Comments: Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, belongs to a class of enzymes known as β-keto acid cleavage enzymes (BKACE). It is involved in the anaerobic fermentation of lysine. cf. EC 2.3.1.317, 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase, EC 2.3.1.318, 3-oxoadipate:acetyl-CoA acetyltransferase, and EC 2.3.1.319, 3,5-dioxohexanoate:acetyl-CoA acetone transferase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Barker, H.A., Kahn, J.M. and Hedrick, L. Pathway of lysine degradation in Fusobacterium nucleatum. J. Bacteriol. 152 (1982) 201-207. [PMID: 6811551]
2. Kreimeyer, A., Perret, A., Lechaplais, C., Vallenet, D., Medigue, C., Salanoubat, M. and Weissenbach, J. Identification of the last unknown genes in the fermentation pathway of lysine. J. Biol. Chem. 282 (2007) 7191-7197. [PMID: 17166837]
3. Bellinzoni, M., Bastard, K., Perret, A., Zaparucha, A., Perchat, N., Vergne, C., Wagner, T., de Melo-Minardi, R.C., Artiguenave, F., Cohen, G.N., Weissenbach, J., Salanoubat, M. and Alzari, P.M. 3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon Claisen-type condensation. J. Biol. Chem. 286 (2011) 27399-27405. [PMID: 21632536]
Accepted name: spermidine disinapoyl transferase
Reaction: 2 sinapoyl-CoA + spermidine = 2 CoA + N1,N8-bis(sinapoyl)-spermidine
Other name(s): SDT
Systematic name: sinapoyl-CoA:spermidine N-(hydroxycinnamoyl)transferase
Comments: The enzyme from the plant Arabidopsis thaliana has no activity with 4-coumaroyl-CoA (cf. EC 2.3.1.249, spermidine dicoumaroyl transferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Luo, J., Fuell, C., Parr, A., Hill, L., Bailey, P., Elliott, K., Fairhurst, S.A., Martin, C. and Michael, A.J. A novel polyamine acyltransferase responsible for the accumulation of spermidine conjugates in Arabidopsis seed. Plant Cell 21 (2009) 318-333. [PMID: 19168716]
Accepted name: spermidine dicoumaroyl transferase
Reaction: 2 4-coumaroyl-CoA + spermidine = 2 CoA + N1,N8-bis(4-coumaroyl)-spermidine
Other name(s): SCT
Systematic name: 4-coumaroyl-CoA:spermidine N-(hydroxycinnamoyl)transferase
Comments: The enzyme from the plant Arabidopsis thaliana has no activity with sinapoyl-CoA (cf. EC 2.3.1.248, spermidine disinapoyl transferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Luo, J., Fuell, C., Parr, A., Hill, L., Bailey, P., Elliott, K., Fairhurst, S.A., Martin, C. and Michael, A.J. A novel polyamine acyltransferase responsible for the accumulation of spermidine conjugates in Arabidopsis seed. Plant Cell 21 (2009) 318-333. [PMID: 19168716]
Accepted name: [Wnt protein] O-palmitoleoyl transferase
Reaction: (9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
Glossary: (9Z)-hexadec-9-enoate = palmitoleoate
Other name(s): porcupine; PORCN (gene name)
Systematic name: (9Z)-hexadec-9-enoyl-CoA:[Wnt]-L-serine O-hexadecenoyltransferase
Comments: The enzyme, found in animals, modifies a specific serine residue in Wnt proteins, e.g. Ser209 in human Wnt3a and Ser224 in chicken WNT1 [2,3]. The enzyme can accept C13 to C16 fatty acids in vitro, but only (9Z)-hexadecenoate modification is observed in vivo [1]. cf. EC 3.1.1.98, [Wnt protein]-O-palmitoleoyl-L-serine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Takada, R., Satomi, Y., Kurata, T., Ueno, N., Norioka, S., Kondoh, H., Takao, T. and Takada, S. Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion. Dev Cell 11 (2006) 791-801. [PMID: 17141155]
2. Gao, X. and Hannoush, R.N. Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine. Nat. Chem. Biol. 10 (2014) 61-68. [PMID: 24292069]
3. Miranda, M., Galli, L.M., Enriquez, M., Szabo, L.A., Gao, X., Hannoush, R.N. and Burrus, L.W. Identification of the WNT1 residues required for palmitoylation by Porcupine. FEBS Lett. 588 (2014) 4815-4824. [PMID: 25451226]
Accepted name: lipid IVA palmitoyltransferase
Reaction: (1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
(2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = 2-acyl-sn-glycero-3-phosphocholine + lipid IIB
(3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA = 2-acyl-sn-glycero-3-phosphocholine + lipid IVB
For diagram of reaction click here.
Glossary: palmitoyl = hexadecanoyl
hexa-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
hepta-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IIB = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IVB = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
Other name(s): PagP; crcA (gene name)
Systematic name: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase
Comments: Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2→4)-Kdo-(2→6)-lipid IVA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I. and Raetz, C.R. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19 (2000) 5071-5080. [PMID: 11013210]
2. Cuesta-Seijo, J.A., Neale, C., Khan, M.A., Moktar, J., Tran, C.D., Bishop, R.E., Pomes, R. and Prive, G.G. PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure 18 (2010) 1210-1219. [PMID: 20826347]
Accepted name: mycolipanoate synthase
Reaction: a long-chain acyl-CoA + 3 (S)-methylmalonyl-CoA + 6 NADPH + 6 H+ + holo-[mycolipanoate synthase] = mycolipanoyl-[mycolipanoate synthase] + 4 CoA + 3 CO2 + 6 NADP+ + 3 H2O
Glossary: mycolipanoic acid = (2S,4S,6S)-2,4,6-trimethyl-very-long-chain fatty acid
Other name(s): msl3 (gene name); Pks3/4; mycolipanoic acid synthase; long-chain acyl-CoA:methylmalonyl-CoA C-acyltransferase (mycolipanoate-forming)
Systematic name: long-chain acyl-CoA:(S)-methylmalonyl-CoA C-acyltransferase (mycolipanoate-forming)
Comments: This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyltetracosanoate (C27-mycolipanoate). Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1. Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem 276 (2001) 16833-16839. [PMID: 11278910]
2. Dubey, V.S., Sirakova, T.D. and Kolattukudy, P.E. Disruption of msl3 abolishes the synthesis of mycolipanoic and mycolipenic acids required for polyacyltrehalose synthesis in Mycobacterium tuberculosis H37Rv and causes cell aggregation. Mol. Microbiol. 45 (2002) 1451-1459. [PMID: 12207710]
Accepted name: phloroglucinol synthase
Reaction: 3 malonyl-CoA = phloroglucinol + 3 CO2 + 3 CoA
For diagram of reaction click here.
Glossary: phloroglucinol = 1,3,5-trihydroxybenzene
Other name(s): phlD (gene name)
Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (decarboxylating, phloroglucinol-forming)
Comments: The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a type III polyketide synthase. The mechanism involves the cyclization of an activated 3,5-dioxoheptanedioate intermediate. The enzyme exhibits broad substrate specificity, and can accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoA as the starter molecules, forming 6-(polyoxoalkylated)-α-pyrones by sequential condensation with malonyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Achkar, J., Xian, M., Zhao, H. and Frost, J.W. Biosynthesis of phloroglucinol. J. Am. Chem. Soc. 127 (2005) 5332-5333.
2. Zha, W., Rubin-Pitel, S.B. and Zhao, H. Characterization of the substrate specificity of PhlD, a type III polyketide synthase from Pseudomonas fluorescens. J. Biol. Chem. 281 (2006) 32036-32047. [PMID: 16931521]
Accepted name: N-terminal methionine Nα-acetyltransferase NatB
Reaction: (1) acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Other name(s): NAA20 (gene name); NAA25 (gene name)
Systematic name: acetyl-CoA:N-terminal Met-Asn/Gln/Asp/Glu-[protein] Met-Nα-acetyltransferase
Comments: N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Starheim, K.K., Arnesen, T., Gromyko, D., Ryningen, A., Varhaug, J.E. and Lillehaug, J.R. Identification of the human Nα-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression. Biochem. J. 415 (2008) 325-331. [PMID: 18570629]
2. Ferrandez-Ayela, A., Micol-Ponce, R., Sanchez-Garcia, A.B., Alonso-Peral, M.M., Micol, J.L. and Ponce, M.R. Mutation of an Arabidopsis NatB N-α-terminal acetylation complex component causes pleiotropic developmental defects. PLoS One 8 (2013) e80697. [PMID: 24244708]
3. Lee, K.E., Ahn, J.Y., Kim, J.M. and Hwang, C.S. Synthetic lethal screen of NAA20, a catalytic subunit gene of NatB N-terminal acetylase in Saccharomyces cerevisiae. J Microbiol 52 (2014) 842-848. [PMID: 25163837]
Accepted name: N-terminal amino-acid Nα-acetyltransferase NatA
Reaction: (1) acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-Nα-acetyl-glycyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-Nα-acetyl-L-alanyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-Nα-acetyl-L-seryl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal-Nα-acetyl-L-valyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal-Nα-acetyl-L-cysteinyl-[protein] + CoA
(6) acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal-Nα-acetyl-L-threonyl-[protein] + CoA
Other name(s): NAA10 (gene name); NAA15 (gene name); ARD1 (gene name)
Systematic name: acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mullen, J.R., Kayne, P.S., Moerschell, R.P., Tsunasawa, S., Gribskov, M., Colavito-Shepanski, M., Grunstein, M., Sherman, F. and Sternglanz, R. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J. 8 (1989) 2067-2075. [PMID: 2551674]
2. Park, E.C. and Szostak, J.W. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 11 (1992) 2087-2093. [PMID: 1600941]
3. Sugiura, N., Adams, S.M. and Corriveau, R.A. An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development. J. Biol. Chem. 278 (2003) 40113-40120. [PMID: 12888564]
4. Gautschi, M., Just, S., Mun, A., Ross, S., Rucknagel, P., Dubaquie, Y., Ehrenhofer-Murray, A. and Rospert, S. The yeast Nα-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell Biol. 23 (2003) 7403-7414. [PMID: 14517307]
5. Xu, F., Huang, Y., Li, L., Gannon, P., Linster, E., Huber, M., Kapos, P., Bienvenut, W., Polevoda, B., Meinnel, T., Hell, R., Giglione, C., Zhang, Y., Wirtz, M., Chen, S. and Li, X. Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis. Plant Cell 27 (2015) 1547-1562. [PMID: 25966763]
6. Dorfel, M.J. and Lyon, G.J. The biological functions of Naa10 - From amino-terminal acetylation to human disease. Gene 567 (2015) 103-131. [PMID: 25987439]
Accepted name: N-terminal methionine Nα-acetyltransferase NatC
Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
Other name(s): NAA30 (gene name); NAA35 (gene name); NAA38 (gene name); MAK3 (gene name); MAK10 (gene name); MAK31 (gene name)
Systematic name: acetyl-CoA:N-terminal-Met-Leu/Ile/Phe/Trp/Tyr-[protein] Met Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Polevoda, B. and Sherman, F. NatC Nα-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p. J. Biol. Chem. 276 (2001) 20154-20159. [PMID: 11274203]
2. Polevoda, B. and Sherman, F. Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 308 (2003) 1-11. [PMID: 12890471]
3. Pesaresi, P., Gardner, N.A., Masiero, S., Dietzmann, A., Eichacker, L., Wickner, R., Salamini, F. and Leister, D. Cytoplasmic N-terminal protein acetylation is required for efficient photosynthesis in Arabidopsis. Plant Cell 15 (2003) 1817-1832. [PMID: 12897255]
4. Wenzlau, J.M., Garl, P.J., Simpson, P., Stenmark, K.R., West, J., Artinger, K.B., Nemenoff, R.A. and Weiser-Evans, M.C. Embryonic growth-associated protein is one subunit of a novel N-terminal acetyltransferase complex essential for embryonic vascular development. Circ. Res. 98 (2006) 846-855. [PMID: 16484612]
5. Starheim, K.K., Gromyko, D., Evjenth, R., Ryningen, A., Varhaug, J.E., Lillehaug, J.R. and Arnesen, T. Knockdown of human Nα-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell Biol. 29 (2009) 3569-3581. [PMID: 19398576]
Accepted name: N-terminal L-serine Nα-acetyltransferase NatD
Reaction: (1) acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nα-acetyl-L-seryl-[histone H4] + CoA
(2) acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nα-acetyl-L-seryl-[histone H2A] + CoA
Other name(s): NAA40 (gene name)
Systematic name: acetyl-CoA:N-terminal-L-seryl-[histone 4/2A] L-serine Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4. Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Song, O.K., Wang, X., Waterborg, J.H. and Sternglanz, R. An Nα-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J. Biol. Chem. 278 (2003) 38109-38112. [PMID: 12915400]
2. Polevoda, B., Hoskins, J. and Sherman, F. Properties of Nat4, an Nα-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4. Mol. Cell Biol. 29 (2009) 2913-2924. [PMID: 19332560]
3. Magin, R.S., Liszczak, G.P. and Marmorstein, R. The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD. Structure 23 (2015) 332-341. [PMID: 25619998]
Accepted name: N-terminal methionine Nα-acetyltransferase NatE
Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-alanyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-seryl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-valyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-threonyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-lysyl-[protein] + CoA
(6) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(7) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
(8) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
Other name(s): NAA50 (gene name); NAT5; SAN
Systematic name: acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nα-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase.The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hou, F., Chu, C.W., Kong, X., Yokomori, K. and Zou, H. The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner. J. Cell Biol. 177 (2007) 587-597. [PMID: 17502424]
2. Pimenta-Marques, A., Tostoes, R., Marty, T., Barbosa, V., Lehmann, R. and Martinho, R.G. Differential requirements of a mitotic acetyltransferase in somatic and germ line cells. Dev. Biol. 323 (2008) 197-206. [PMID: 18801358]
3. Evjenth, R., Hole, K., Karlsen, O.A., Ziegler, M., Arnesen, T. and Lillehaug, J.R. Human Naa50p (Nat5/San) displays both protein Nα- and Nε-acetyltransferase activity. J. Biol. Chem. 284 (2009) 31122-31129. [PMID: 19744929]
4. Van Damme, P., Hole, K., Gevaert, K. and Arnesen, T. N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases. Proteomics 15 (2015) 2436-2446. [PMID: 25886145]
Accepted name: N-terminal methionine Nα-acetyltransferase NatF
Reaction: acetyl-CoA + an N-terminal-L-methionyl-[transmembrane protein] = an N-terminal-Nα-acetyl-L-methionyl-[transmembrane protein] + CoA
Other name(s): NAA60 (gene name)
Systematic name: acetyl-CoA:N-terminal-Met-Lys/Ser/Val/Leu/Gln/Ile/Tyr/Thr-[transmembrane protein] Met-Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. NatF is found only in higher eukaryotes, and is absent from yeast. Unlike other Nat systems the enzyme is located in the Golgi apparatus. It faces the cytosolic side of intracellular membranes, and specifically acetylates transmembrane proteins whose N termini face the cytosol. NatF targets N-terminal L-methionine residues attached to Lys, Ser, Val, Leu, Gln, Ile, Tyr and Thr residues.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Van Damme, P., Hole, K., Pimenta-Marques, A., Helsens, K., Vandekerckhove, J., Martinho, R.G., Gevaert, K. and Arnesen, T. NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet 7 (2011) e1002169. [PMID: 21750686]
2. Aksnes, H., Van Damme, P., Goris, M., Starheim, K.K., Marie, M., Støve, S.I., Hoel, C., Kalvik, T.V., Hole, K., Glomnes, N., Furnes, C., Ljostveit, S., Ziegler, M., Niere, M., Gevaert, K. and Arnesen, T. An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. Cell Rep 10 (2015) 1362-1374. [PMID: 25732826]
Accepted name: tetracycline polyketide synthase
Reaction: malonamoyl-[OxyC acyl-carrier protein] + 8 malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC acyl-carrier protein] + 8 CO2 + 8 CoA
For diagram of reaction click here.
Systematic name: malonyl-CoA:malonamoyl-[OxyC acyl-carrier protein] malonyltransferase
Comments: The synthesis, in the bacterium Streptomyces rimosus, of the tetracycline antibiotics core skeleton requires a minimal polyketide synthase (PKS) consisting of a ketosynthase (KS), a chain length factor (CLF), and an acyl-carrier protein (ACP). Initiation involves an amide-containing starter unit that becomes the C-2 amide that is present in the tetracycline compounds. Following the initiation, the PKS catalyses the iterative condensation of 8 malonyl-CoA molecules to yield the polyketide backbone of tetracycline. Throughout the proccess, the nascent chain is attached to the OxyC acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Thomas, R. and Williams, D.J. Oxytetracycline biosynthesis: origin of the carboxamide substituent. J. Chem. Soc., Chem. Commun. (1983) 677-679.
2. Zhang, W., Ames, B.D., Tsai, S.C. and Tang, Y. Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase. Appl. Environ. Microbiol. 72 (2006) 2573-2580. [PMID: 16597959]
3. Yu, L., Cao, N., Wang, L., Xiao, C., Guo, M., Chu, J., Zhuang, Y. and Zhang, S. Oxytetracycline biosynthesis improvement in Streptomyces rimosus following duplication of minimal PKS genes. Enzyme Microb. Technol. 50 (2012) 318-324. [PMID: 22500899]
Accepted name: (4-hydroxyphenyl)alkanoate synthase
Reaction: (1) 4-hydroxybenzoyl-[(4-hydroxyphenyl)alkanoate synthase] + 8 malonyl-CoA + 16 NADPH + 16 H+ = 17-(4-hydroxyphenyl)heptadecanoyl-[(4-hydroxyphenyl)alkanoate synthase] + 8 CO2 + 8 CoA + 16 NADP+ + 8 H2O
(2) 4-hydroxybenzoyl-[(4-hydroxyphenyl)alkanoate synthase] + 9 malonyl-CoA + 18 NADPH + 18 H+ + holo-[(4-hydroxyphenyl)alkanoate synthase] = 19-(4-hydroxyphenyl)nonadecanoyl-[(4-hydroxyphenyl)alkanoate synthase] + 9 CO2 + 9 CoA + 18 NADP+ + 9 H2O
Other name(s): msl7 (gene name); Pks15/1
Systematic name: malonyl-CoA:4-hydroxybenzoyl-[(4-hydroxyphenyl)alkanoate synthase] malonyltransferase [(4-hydroxyphenyl)alkanoate-forming]
Comments: The enzyme is part of the biosynthetic pathway of phenolphthiocerol, a lipid that serves as a virulence factor of pathogenic mycobacteria. It catalyses the elongation of 4-hydroxybenzoate that is loaded on its acyl-carrier domain to form (4-hydroxyphenyl)alkanoate intermediates. The enzyme adds either 8 or 9 malonyl-CoA units, resulting in formation of 17-(4-hydroxyphenyl)heptadecanoate or 19-(4-hydroxyphenyl)nonadecanoate, respectively. As the enzyme lacks a thioesterase domain [1], the product remains loaded on the acyl-carrier domain at the end of catalysis, and has to be hydrolysed by an as-yet unknown mechanism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem. 276 (2001) 16833-16839. [PMID: 11278910]
2. Constant, P., Perez, E., Malaga, W., Laneelle, M.A., Saurel, O., Daffe, M. and Guilhot, C. Role of the pks15/1 gene in the biosynthesis of phenolglycolipids in the Mycobacterium tuberculosis complex. Evidence that all strains synthesize glycosylated p-hydroxybenzoic methyl esters and that strains devoid of phenolglycolipids harbor a frameshift mutation in the pks15/1 gene. J. Biol. Chem. 277 (2002) 38148-38158. [PMID: 12138124]
3. Simeone, R., Leger, M., Constant, P., Malaga, W., Marrakchi, H., Daffe, M., Guilhot, C. and Chalut, C. Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis. FEBS J. 277 (2010) 2715-2725. [PMID: 20553505]
Accepted name: anthraniloyl-CoA anthraniloyltransferase
Reaction: anthraniloyl-CoA + malonyl-CoA = 2-(aminobenzoyl)acetyl-CoA + CoA + CO2 (overall reaction)
(1a) anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
(1b) S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = 2-(aminobenzoyl)acetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]
Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA
Other name(s): pqsD (gene name)
Systematic name: anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thiesterase, is present, it removes the CoA moiety from the product, forming the stable 2-aminobenzoylacetate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Bera, A.K., Atanasova, V., Robinson, H., Eisenstein, E., Coleman, J.P., Pesci, E.C. and Parsons, J.F. Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate. Biochemistry 48 (2009) 8644-8655. [PMID: 19694421]
2. Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the Pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481-1491. [PMID: 24239007]
3. Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611-618. [PMID: 25960261]
Accepted name: 2-amino-4-oxopentanoate thiolase
Reaction: acetyl-CoA + D-alanine = CoA + (2R)-2-amino-4-oxopentanoate
Other name(s): AKPT; AKP thiolase; 2-amino-4-ketopentanoate thiolase
Systematic name: acetyl-CoA:D-alanine acetyltransferase
Comments: A pyridoxal 5'-phosphate enzyme. The enzyme, characterized from the bacterium Clostridium sticklandii, is part of a degradation pathway of ornithine. It is specific for acetyl-CoA and D-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Jeng, I.M., Somack, R. and Barker, H.A. Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl coenzyme A. Biochemistry 13 (1974) 2898-2903. [PMID: 4407783]
2. Fonknechten, N., Perret, A., Perchat, N., Tricot, S., Lechaplais, C., Vallenet, D., Vergne, C., Zaparucha, A., Le Paslier, D., Weissenbach, J. and Salanoubat, M. A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine. J. Bacteriol. 191 (2009) 3162-3167. [PMID: 19251850]
Accepted name: β-lysine N6-acetyltransferase
Reaction: acetyl-CoA + (3S)-3,6-diaminohexanoate = CoA + (3S)-6-acetamido-3-aminohexanoate
Glossary: (3S)-3,6-diaminohexanoate = β-L-lysine
(3S)-6-acetamido-3-aminohexanoate = N6-acetyl-β-L-lysine
Other name(s): ablB (gene name)
Systematic name: acetyl-CoA:(3S)-3,6-diaminohexanoate N6-acetyltransferase
Comments: This entry describes enzymes that catalyse a single methylation of the L-lysine4 residue of histone H3 (H3K4), generating a monomethylated form. This modifications influence the binding of chromatin-associated proteins and result in gene activation or suppression. Some enzymes that catalyse this reaction continue to generate a dimethyated form, these enzymes are classified under EC 2.1.1.370, [histone H3]-lysine4 N-dimethyltransferase. Other enzymes continue to catalyse a third methylation, those are classified under EC 2.1.1.354, [histone H3]-lysine4 N-trimethyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Pfluger, K., Baumann, S., Gottschalk, G., Lin, W., Santos, H. and Muller, V. Lysine-2,3-aminomutase and β-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nε-acetyl-β-lysine and growth at high salinity. Appl. Environ. Microbiol. 69 (2003) 6047-6055. [PMID: 14532061]
2. Muller, S., Hoffmann, T., Santos, H., Saum, S.H., Bremer, E. and Muller, V. Bacterial abl-like genes: production of the archaeal osmolyte N(ε)-acetyl-β-lysine by homologous overexpression of the yodP-kamA genes in Bacillus subtilis. Appl. Microbiol. Biotechnol. 91 (2011) 689-697. [PMID: 21538109]
Accepted name: phosphatidylinositol dimannoside acyltransferase
Reaction: (1) an acyl-CoA + 2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-α-D-mannosyl)-6-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2) an acyl-CoA + 2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Other name(s): PIM2 acyltransferase; ptfP1 (gene name)
Systematic name: acyl-CoA:2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol acyltransferase
Comments: The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Svetlikova, Z., Barath, P., Jackson, M., Kordulakova, J. and Mikusova, K. Purification and characterization of the acyltransferase involved in biosynthesis of the major mycobacterial cell envelope glycolipid —monoacylated phosphatidylinositol dimannoside. Protein Expr. Purif. 100 (2014) 33-39. [PMID: 24810911]
Accepted name: [ribosomal protein bS18]-alanine N-acetyltransferase
Reaction: acetyl-CoA + an N-terminal L-alanyl-[bS18 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[bS18 protein of 30S ribosome]
Other name(s): rimI (gene name)
Systematic name: acetyl-CoA:N-terminal L-alanyl-[bS18 protein of 30S ribosome] N-acetyltransferase
Comments: The enzyme, characterized from bacteria, is specific for protein bS18, a component of the 30S ribosomal subunit. cf. EC 2.3.1.267, [ribosomal protein uS5]-alanine N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Isono, K. and Isono, S. Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18. Mol. Gen. Genet. 177 (1980) 645-651. [PMID: 6991870]
2. Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481-488. [PMID: 2828880]
Accepted name: [ribosomal protein uS5]-alanine N-acetyltransferase
Reaction: acetyl-CoA + an N-terminal L-alanyl-[uS5 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[uS5 protein of 30S ribosome]
Other name(s): rimJ (gene name)
Systematic name: acetyl-CoA:N-terminal L-alanyl-[uS5 protein of 30S ribosome] N-acetyltransferase
Comments: The enzyme, characterized from bacteria, is specific for protein uS5, a component of the 30S ribosomal subunit. It also plays a role in maturation of the 30S ribosomal subunit. cf. EC 2.3.1.266, [ribosomal protein bS18]-alanine N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481-488. [PMID: 2828880]
2. Roy-Chaudhuri, B., Kirthi, N., Kelley, T. and Culver, G.M. Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis. Mol. Microbiol. 68 (2008) 1547-1559. [PMID: 18466225]
3. Roy-Chaudhuri, B., Kirthi, N. and Culver, G.M. Appropriate maturation and folding of 16S rRNA during 30S subunit biogenesis are critical for translational fidelity. Proc. Natl. Acad. Sci. USA 107 (2010) 4567-4572. [PMID: 20176963]
Accepted name: ethanol O-acetyltransferase
Reaction: ethanol + acetyl-CoA = ethyl acetate + CoA
Other name(s): eat1 (gene name); ethanol acetyltransferase
Systematic name: acetyl-CoA:ethanol O-acetyltransferase
Comments: The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts. It is only distantly related to enzymes classified as EC 2.3.1.84, alcohol O-acetyltransferase. The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kruis, A.J., Levisson, M., Mars, A.E., van der Ploeg, M., Garces Daza, F., Ellena, V., Kengen, S.WM., van der Oost, J. and Weusthuis, R.A. Ethyl acetate production by the elusive alcohol acetyltransferase from yeast. Metab. Eng. 41 (2017) 92-101. [PMID: 28356220]
Accepted name: apolipoprotein N-acyltransferase
Reaction: a phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Other name(s): lnt (gene name); Lnt
Systematic name: phosphoglyceride:[apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine N-acyltransferase
Comments: This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Gupta, S.D. and Wu, H.C. Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli. FEMS Microbiol. Lett. 62 (1991) 37-41. [PMID: 2032623]
2. Robichon, C., Vidal-Ingigliardi, D. and Pugsley, A.P. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J. Biol. Chem. 280 (2005) 974-983. [PMID: 15513925]
3. Hillmann, F., Argentini, M. and Buddelmeijer, N. Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. J. Biol. Chem. 286 (2011) 27936-27946. [PMID: 21676878]
Accepted name: lyso-ornithine lipid O-acyltransferase
Reaction: a lyso-ornithine lipid + an acyl-[acyl-carrier protein] = an ornithine lipid + a holo-[acyl-carrier protein]
Glossary: a lyso-ornithine lipid = an Nα-[(3R)-3-hydroxyacyl]-L-ornithine
an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine
Other name(s): olsA (gene name)
Systematic name: Nα-[(3R)-hydroxy-acyl]-L-ornithine O-acyltransferase
Comments: This bacterial enzyme catalyses the second step in the formation of ornithine lipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Weissenmayer, B., Gao, J.L., Lopez-Lara, I.M. and Geiger, O. Identification of a gene required for the biosynthesis of ornithine-derived lipids. Mol. Microbiol. 45 (2002) 721-733. [PMID: 12139618]
2. Aygun-Sunar, S., Bilaloglu, R., Goldfine, H. and Daldal, F. Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both ornithine lipid and phosphatidic acid biosynthesis. J. Bacteriol. 189 (2007) 8564-8574. [PMID: 17921310]
3. Lewenza, S., Falsafi, R., Bains, M., Rohs, P., Stupak, J., Sprott, G.D. and Hancock, R.E. The olsA gene mediates the synthesis of an ornithine lipid in Pseudomonas aeruginosa during growth under phosphate-limiting conditions, but is not involved in antimicrobial peptide susceptibility. FEMS Microbiol. Lett. 320 (2011) 95-102. [PMID: 21535098]
Accepted name: L-glutamate-5-semialdehyde N-acetyltransferase
Reaction: acetyl-CoA + L-glutamate 5-semialdehyde = CoA + N-acetyl-L-glutamate 5-semialdehyde
Other name(s): MPR1 (gene name); MPR2 (gene name)
Systematic name: acetyl-CoA:L-glutamate-5-semialdehyde N-acetyltransferase
Comments: The enzyme, characterized from the yeast Saccharomyces cerevisiae Σ1278b, N-acetylates L-glutamate 5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions. Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress. The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Shichiri, M., Hoshikawa, C., Nakamori, S. and Takagi, H. A novel acetyltransferase found in Saccharomyces cerevisiae Σ1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid. J. Biol. Chem. 276 (2001) 41998-42002. [PMID: 11555637]
2. Nomura, M. and Takagi, H. Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate. Proc. Natl Acad. Sci. USA 101 (2004) 12616-12621. [PMID: 15308773]
3. Nishimura, A., Kotani, T., Sasano, Y. and Takagi, H. An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1: oxidative stress-induced arginine synthesis and its physiological role. FEMS Yeast Res. 10 (2010) 687-698. [PMID: 20550582]
4. Nishimura, A., Nasuno, R. and Takagi, H. The proline metabolism intermediate Δ1-pyrroline-5-carboxylate directly inhibits the mitochondrial respiration in budding yeast. FEBS Lett. 586 (2012) 2411-2416. [PMID: 22698729]
5. Nasuno, R., Hirano, Y., Itoh, T., Hakoshima, T., Hibi, T. and Takagi, H. Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism. Proc. Natl Acad. Sci. USA 110 (2013) 11821-11826. [PMID: 23818613]
Accepted name: 2-acetylphloroglucinol acetyltransferase
Reaction: 2 2-acetylphloroglucinol = 2,4-diacetylphloroglucinol + phloroglucinol
Glossary: phloroglucinol = benzene-1,3,5-triol
Other name(s): MAPG ATase
Systematic name: 2-acetylphloroglucinol C-acetyltransferase
Comments: The enzyme from the bacterium Pseudomonas sp YGJ3 is composed of three subunits named PhlA, PhlB and PhlC. Production of 2,4-diacetylphloroglucinol, which has antibiotic activity, is strongly inhibited by chloride ions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hayashi, A., Saitou, H., Mori, T., Matano, I., Sugisaki, H. and Maruyama, K. Molecular and catalytic properties of monoacetylphloroglucinol acetyltransferase from Pseudomonas sp. YGJ3. Biosci. Biotechnol. Biochem. 76 (2012) 559-566. [PMID: 22451400]
Accepted name: diglucosylglycerate octanoyltransferase
Reaction: octanoyl-CoA + 2-O-[α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate = 2-O-[6-O-octanoyl-α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate. + CoA
Other name(s): octT (gene name); DGG octanoyltransferase
Systematic name: octanoyl-CoA:2-O-[α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate octanoyltransferase
Comments: The enzyme, characterized from mycobacteria, is involved in the biosynthesis of methylglucose lipopolysaccharide (MGLP). The enzyme can also act on 2-O-(α-D-glucopyranosyl)-D-glycerate, but with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Maranha, A., Moynihan, P.J., Miranda, V., Correia Lourenco, E., Nunes-Costa, D., Fraga, J.S., Jose Barbosa Pereira, P., Macedo-Ribeiro, S., Ventura, M.R., Clarke, A.J. and Empadinhas, N. Octanoylation of early intermediates of mycobacterial methylglucose lipopolysaccharides. Sci Rep 5 (2015) 13610. [PMID: 26324178]
Accepted name: phosphate acyltransferase
Reaction: an acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein]
Other name(s): plsX (gene name); acyl-ACP phosphotransacylase; acyl-[acyl-carrier-protein]—phosphate acyltransferase; phosphate-acyl-ACP acyltransferase
Systematic name: an acyl-[acyl-carrier protein]:phosphate acyltransferase
Comments: The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765-772. [PMID: 16949372]
2. Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7 (2007) 69. [PMID: 17645809]
3. Kim, Y., Li, H., Binkowski, T.A., Holzle, D. and Joachimiak, A. Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis. J Struct Funct Genomics 10 (2009) 157-163. [PMID: 19058030]
4. Kaczmarzyk, D., Cengic, I., Yao, L. and Hudson, E.P. Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX. Metab. Eng. 45 (2018) 59-66. [PMID: 29199103]
Accepted name: acyl phosphate:glycerol-3-phosphate acyltransferase
Reaction: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate
Other name(s): plsY (gene name); G3P acyltransferase; GPAT; lysophosphatidic acid synthase; LPA synthase
Systematic name: acyl phosphoate:sn-glycerol 3-phosphate acyltransferase
Comments: The enzyme, found in bacteria, catalyses a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. The enzyme is membrane-bound.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765-772. [PMID: 16949372]
2. Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7 (2007) 69. [PMID: 17645809]
3. Lu, Y.J., Zhang, F., Grimes, K.D., Lee, R.E. and Rock, C.O. Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase. J. Biol. Chem 282 (2007) 11339-11346. [PMID: 17308305]
4. Hara, Y., Seki, M., Matsuoka, S., Hara, H., Yamashita, A. and Matsumoto, K. Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-phosphate acyltransferase PlsY in the initial stage of glycerolipid synthesis in Bacillus subtilis. Genes Genet. Syst. 83 (2008) 433-442. [PMID: 19282621]
Accepted name: galactosamine-1-phosphate N-acetyltransferase
Reaction: acetyl-CoA + α-D-galactosamine 1-phosphate = CoA + N-acetyl-α-D-galactosamine 1-phosphate
Other name(s): ST0452 (locus name)
Systematic name: acetyl-CoA:α-D-galactosamine-1-phosphate N-acetyltransferase
Comments: The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward α-D-glucosamine 1-phosphate (cf. EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase). In addition, that enzyme contains a second domain that catalyses the activities of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase, and EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Zhang, Z., Tsujimura, M., Akutsu, J., Sasaki, M., Tajima, H. and Kawarabayasi, Y. Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7. J. Biol. Chem 280 (2005) 9698-9705. [PMID: 15598657]
2. Zhang, Z., Akutsu, J. and Kawarabayasi, Y. Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7. J. Bacteriol. 192 (2010) 3287-3293. [PMID: 20400541]
3. Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]
Accepted name: 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase
Reaction: a medium-chain 3-oxoacyl-[acyl-carrier protein] + glycerone phosphate = 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate + a holo-[acyl-carrier protein]
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): afsA (gene name); scbA (gene name); barX (gene name)
Systematic name: 3-oxoacyl-[acyl-carrier protein]:glycerone phosphate 3-oxonacylltransferase
Comments: The enzyme catalyses the first committed step in the biosynthesis of γ-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Horinouchi, S., Suzuki, H., Nishiyama, M. and Beppu, T. Nucleotide sequence and transcriptional analysis of the Streptomyces griseus gene (afsA) responsible for A-factor biosynthesis. J. Bacteriol. 171 (1989) 1206-1210. [PMID: 2492509]
2. Kato, J.Y., Funa, N., Watanabe, H., Ohnishi, Y. and Horinouchi, S. Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces. Proc. Natl Acad. Sci. USA 104 (2007) 2378-2383. [PMID: 17277085]
3. Hsiao, N.H., Soding, J., Linke, D., Lange, C., Hertweck, C., Wohlleben, W. and Takano, E. ScbA from Streptomyces coelicolor A3(2) has homology to fatty acid synthases and is able to synthesize γ-butyrolactones. Microbiology 153 (2007) 1394-1404. [PMID: 17464053]
4. Lee, Y.J., Kitani, S. and Nihira, T. Null mutation analysis of an afsA-family gene, barX, that is involved in biosynthesis of the γ-butyrolactone autoregulator in Streptomyces virginiae. Microbiology 156 (2010) 206-210. [PMID: 19778967]
Accepted name: mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase
Reaction: a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose = a 2-(long-chain fatty acyl)-3-mycolipenoyl-trehalose + CoA
Glossary: a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA
polyacyltrehalose = PAT = a 2-(long-chain fatty acyl)-2',3,4',6-tetramycolipenoyl-trehalose
Other name(s): papA3 (gene name)
Systematic name: mycolipenoyl-CoA:2-(long-chain-fatty acyl)-trehalose 3-mycolipenoyltransferase
Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279, long-chain-acyl-CoA—trehalose acyltransferase), followed by the transfer of a mycolipenyl group to position 3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 284 (2009) 12745-12751. [PMID: 19276083]
Accepted name: long-chain-acyl-CoA—trehalose acyltransferase
Reaction: a long-chain fatty acyl-CoA + α,α-trehalose = a 2-(long-chain-fatty acyl)-trehalose + CoA
Glossary: polyacyltrehalose = PAT = a 2-(long-chain fatty acyl)-2',3,4',6-tetramycolipenoyl-trehalose
a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA
Other name(s): papA3 (gene name)
Systematic name: long-chain fatty acyl-CoA:α,α-trehalose 2-acyltransferase
Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278, mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 284 (2009) 12745-12751. [PMID: 19276083]
Accepted name: (aminoalkyl)phosphonate N-acetyltransferase
Reaction: acetyl-CoA + (aminomethyl)phosphonate = CoA + (acetamidomethyl)phosphonate
Other name(s): phnO (gene name)
Systematic name: acetyl-CoA:(aminomethyl)phosphonate N-acetyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is able to acetylate a range of (aminoalkyl)phosphonic acids. Requires a divalent metal ion for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Errey, J.C. and Blanchard, J.S. Functional annotation and kinetic characterization of PhnO from Salmonella enterica. Biochemistry 45 (2006) 3033-3039. [PMID: 16503658]
2. Hove-Jensen, B., McSorley, F.R. and Zechel, D.L. Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-acetylation by the phnO gene product. PLoS One 7 (2012) e46416. [PMID: 23056305]
Accepted name: 5-hydroxydodecatetraenal polyketide synthase
Reaction: 6 malonyl-CoA + 5 NADPH + NADH + 6 H+ = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O
For diagram of reaction click here.
Glossary: coelimycin P1 = N-[(3R)-8-[(2E)-but-2-enoyl]-6-[(2E)-5,6-dihydropyridin-2(1H)-ylidene]-2-oxo-3,4-dihydro-2H,6H-1,5-oxathiocin-3-yl]acetamide
Other name(s): cpkABC (gene names)
Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase ((2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal-forming)
Comments: This polyketide synthase enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), catalyses the first reaction in the biosynthesis of coelimycin P1. The enzyme is made of three proteins which together comprise six modules that contain a total of 28 domains. An NADH-dependent terminal reductase domain at the C-terminus of the enzyme catalyses the reductive release of the product.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Pawlik, K., Kotowska, M., Chater, K.F., Kuczek, K. and Takano, E. A cryptic type I polyketide synthase (cpk) gene cluster in Streptomyces coelicolor A3(2). Arch. Microbiol. 187 (2007) 87-99. [PMID: 17009021]
2. Awodi, U.R., Ronan, J.L., Masschelein, J., Santos, E.LC. and Challis, G.L. Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis. Chem. Sci. 8 (2017) 411-415. [PMID: 28451186]
Accepted name: phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
Reaction: (1) 2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol = a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
(2) 2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
(3) 2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
Glossary: a mycocerosate = 2,4,6-trimethyl- and 2,4,6,8-tetramethyl-2-alkanoic acids present in many pathogenic mycobacteria. The chiral centers bearing the methyl groups have an L (levorotatory) stereo configuration.
a phthiocerol = a linear carbohydrate molecule to which one methoxyl group, one methyl group, and two secondary hydroxyl groups are attached.
a phthiodiolone = an intermediate in phthiocerol biosynthesis, containing an oxo group where phthiocerols contain a methoxyl group
a phenolphthiocerol = a compound related to phthiocerol that contains a phenol group at the ω end of the molecule
Other name(s): papA5 (gene name)
Systematic name: mycocerosyl-[mycocerosic acid synthase]:phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
Comments: The enzyme, present in certain pathogenic species of mycobacteria, catalyses the transfer of mycocerosic acids to the two hydroxyl groups at the common lipid core of phthiocerol, phthiodiolone, and phenolphthiocerol, forming dimycocerosate esters. The fatty acid precursors of mycocerosic acids are activated by EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28, which loads them onto EC 2.3.1.111, mycocerosate synthase. That enzyme extends the precursors to form mycocerosic acids that remain attached until transferred by EC 2.3.1.282.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Onwueme, K.C., Ferreras, J.A., Buglino, J., Lima, C.D. and Quadri, L.E. Mycobacterial polyketide-associated proteins are acyltransferases: proof of principle with Mycobacterium tuberculosis PapA5. Proc. Natl Acad. Sci. USA 101 (2004) 4608-4613. [PMID: 15070765]
2. Buglino, J., Onwueme, K.C., Ferreras, J.A., Quadri, L.E. and Lima, C.D. Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis. J. Biol. Chem 279 (2004) 30634-30642. [PMID: 15123643]
3. Chavadi, S.S., Onwueme, K.C., Edupuganti, U.R., Jerome, J., Chatterjee, D., Soll, C.E. and Quadri, L.E. The mycobacterial acyltransferase PapA5 is required for biosynthesis of cell wall-associated phenolic glycolipids. Microbiology 158 (2012) 1379-1387. [PMID: 22361940]
4. Touchette, M.H., Bommineni, G.R., Delle Bovi, R.J., Gadbery, J.E., Nicora, C.D., Shukla, A.K., Kyle, J.E., Metz, T.O., Martin, D.W., Sampson, N.S., Miller, W.T., Tonge, P.J. and Seeliger, J.C. Diacyltransferase activity and chain length specificity of Mycobacterium tuberculosis PapA5 in the synthesis of alkyl β-diol lipids. Biochemistry 54 (2015) 5457-5468. [PMID: 26271001]
Accepted name: 2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
Reaction: a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose = a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
Other name(s): papA1 (gene name)
Systematic name: (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase]:2'-acyl-2-O-sulfo-α,α-trehalose 3'-(hydroxy)phthioceranyltransferase
Comments: This mycobacterial enzyme catalyses the acylation of 2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose at the 3' position by a (hydroxy)phthioceranoyl group during the biosynthesis of mycobacterial sulfolipids.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Bhatt, K., Gurcha, S.S., Bhatt, A., Besra, G.S. and Jacobs, W.R., Jr. Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153 (2007) 513-520. [PMID: 17259623]
2. Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl Acad. Sci. USA 104 (2007) 11221-11226. [PMID: 17592143]
Accepted name: 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
Reaction: 3 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose = 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-α-alpha-trehalose + 2 2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose
Glossary: 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-α-alpha-trehalose = a mycobacterial sulfolipid
Other name(s): chp1 (gene name)
Systematic name: 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose:3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose 6,6'-di(hydroxy)phthioceranyltransferase
Comments: The enzyme, present in mycobacteria, catalyses the ultimate step in the biosynthesis of mycobacterial sulfolipids. It catalyses two successive transfers of a (hydroxy)phthioceranyl group from two diacylated intermediates to third diacylated intermediate, generating the tetraacylated sulfolipid.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 287 (2012) 7990-8000. [PMID: 22194604]
Accepted name: (13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase
Reaction: acetyl-CoA + (13S,14R)-1,13-dihydroxy-N-methylcanadine = (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + CoA
For diagram of reaction click here.
Other name(s): AT1 (gene name)
Systematic name: acetyl-CoA:(13S,14R)-1,13-dihydroxy-N-methylcanadine O-acetyltransferase
Comments: The enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Dang, T.T., Chen, X. and Facchini, P.J. Acetylation serves as a protective group in noscapine biosynthesis in opium poppy. Nat. Chem. Biol. 11 (2015) 104-106. [PMID: 25485687]
2. Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl Acad. Sci. USA 115 (2018) E3922-E3931. [PMID: 29610307]
Accepted name: protein acetyllysine N-acetyltransferase
Reaction: [protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2"-O-acetyl-ADP-D-ribose + nicotinamide (overall reaction)
(1a) [protein]-N6-acetyl-L-lysine + NAD+ = [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
(1b) [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O = [protein]-L-lysine + 2"-O-acetyl-ADP-D-ribose
Other name(s): Sir2; protein lysine deacetylase; NAD+-dependent protein deacetylase
Systematic name: [protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2"-O-acetyl-ADP-D-ribose-forming)
Comments: The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2"-O-acetyl-ADP-D-ribose converts non-enzymically to 3"-O-acetyl-ADP-D-ribose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Landry, J., Slama, J.T. and Sternglanz, R. Role of NAD+ in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun. 278 (2000) 685-690. [PMID: 11095969]
2. Sauve, A.A., Celic, I., Avalos, J., Deng, H., Boeke, J.D. and Schramm, V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40 (2001) 15456-15463. [PMID: 11747420]
3. Min, J., Landry, J., Sternglanz, R. and Xu, R.M. Crystal structure of a SIR2 homolog-NAD complex. Cell 105 (2001) 269-279. [PMID: 11336676]
4. Jackson, M.D., Schmidt, M.T., Oppenheimer, N.J. and Denu, J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 278 (2003) 50985-50998. [PMID: 14522996]
5. Sauve, A.A., Wolberger, C., Schramm, V.L. and Boeke, J.D. The biochemistry of sirtuins. Annu. Rev. Biochem. 75 (2006) 435-465. [PMID: 16756498]
Accepted name: phthioceranic/hydroxyphthioceranic acid synthase
Reaction: (1) 8 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 16 NADPH + 16 H+ = 8 CoA + C40-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 16 NADP+ + 8 CO2 + 8 H2O
(2) 7 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 14 NADPH + 14 H+ = 7 CO2 + C37-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 14 NADP+ + 7 CoA + 7 H2O
Other name(s): msl2 (gene name); PKS2
Systematic name: (S)-methylmalonyl-CoA:palmitoyl-[(hydroxy)phthioceranic acid synthase] methylmalonyltransferase (phthioceranyl-[(hydroxy)phthioceranic acid synthase]-forming)
Comments: This mycobacterial polyketide enzyme produces the hepta- and octa-methylated fatty acids known as phthioceranic acids, and presumably their hydroxylated versions. Formation of hepta- and octamethylated products depends on whether the enzyme incorporates seven or eight methylmalonyl-CoA extender units, respectively. Formation of hydroxylated products may result from the enzyme skipping the dehydratase (DH) and enoylreductase (ER) domains during the first cycle of condensation [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem 276 (2001) 16833-16839. [PMID: 11278910]
2. Gokhale, R.S., Saxena, P., Chopra, T. and Mohanty, D. Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat. Prod. Rep. 24 (2007) 267-277. [PMID: 17389997]
3. Passemar, C., Arbues, A., Malaga, W., Mercier, I., Moreau, F., Lepourry, L., Neyrolles, O., Guilhot, C. and Astarie-Dequeker, C. Multiple deletions in the polyketide synthase gene repertoire of Mycobacterium tuberculosis reveal functional overlap of cell envelope lipids in host-pathogen interactions. Cell Microbiol 16 (2014) 195-213. [PMID: 24028583]
Accepted name: 2-O-sulfo trehalose long-chain-acyltransferase
Reaction: (1) stearoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2'-stearoyl-α,α-trehalose + CoA
(2) palmitoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2'-palmitoyl-α,α-trehalose + CoA
Other name(s): papA2 (gene name)
Systematic name: acyl-CoA:2-O-sulfo-α,α-trehalose 2'-long-chain-acyltransferase
Comments: This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-α,α-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl Acad. Sci. USA 104 (2007) 11221-11226. [PMID: 17592143]
2. Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 287 (2012) 7990-8000. [PMID: 22194604]
Accepted name: aureothin polyketide synthase system
Reaction: 4-nitrobenzoyl-CoA + malonyl-CoA + 4 (S)-methylmalonyl-CoA + 4 NADPH + 4 H+ = demethylluteothin + 5 CO2 + 6 CoA + 4 NADP+ + 3 H2O
For diagram of reaction, click here
Glossary: demethylluteothin = nordeoxyaureothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-hydroxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
Other name(s): aurABC (gene names); aureothin polyketide synthase complex
Systematic name: malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethylluteothin-forming)
Comments: This polyketide synthase, characterized from the bacterium Streptomyces thioluteus, generates the backbone of the antibiotic aureothin. It is composed of 4 modules that total 18 domains and is encoded by three genes. The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 4 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module (encoded by aurA) is used twice in an iterative fashion, so that the five Claisen condensation reactions are catalysed by only four modules. The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. He, J. and Hertweck, C. Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster. Chem. Biol. 10 (2003) 1225-1232. [PMID: 14700630]
2. He, J. and Hertweck, C. Functional analysis of the aureothin iterative type I polyketide synthase. Chembiochem 6 (2005) 908-912. [PMID: 15812854]
3. Busch, B., Ueberschaar, N., Sugimoto, Y. and Hertweck, C. Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module. J. Am. Chem. Soc. 134 (2012) 12382-12385. [PMID: 22799266]
Accepted name: spectinabilin polyketide synthase system
Reaction: 4-nitrobenzoyl-CoA + malonyl-CoA + 6 (S)-methylmalonyl-CoA + 6 NADPH + 4 H+ = demethyldeoxyspectinabilin + 7 CO2 + 8 CoA + 6 NADP+ + 5 H2O
For diagram of reaction, click here
Glossary: demethyldeoxyspectinabilin = 2-hydroxy-3,5-dimethyl-6-[(3E,5E,7E,9E)-3,5,7,9-tetramethyl-10-(4-nitrophenyl)deca-3,5,7,9-tetraen-1-yl]pyran-4-one
spectinabilin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]pyran-4-one
Other name(s): norAA’BC (gene names); spectinabilin polyketide synthase complex
Systematic name: malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethyldeoxyspectinabilin-forming)
Comments: This polyketide synthase, characterized from the bacteria Streptomyces orinoci and Streptomyces spectabilis, generates the backbone of the antibiotic spectinabilin. It is composed of 6 modules that total 28 domains and is encoded by four genes. The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module (encoded by norA) is used twice in an iterative fashion, so that the seven Claisen condensation reactions are catalysed by only six modules. The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Traitcheva, N., Jenke-Kodama, H., He, J., Dittmann, E. and Hertweck, C. Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective. Chembiochem 8 (2007) 1841-1849. [PMID: 17763486]
2. Choi, Y.S., Johannes, T.W., Simurdiak, M., Shao, Z., Lu, H. and Zhao, H. Cloning and heterologous expression of the spectinabilin biosynthetic gene cluster from Streptomyces spectabilis. Mol. Biosyst. 6 (2010) 336-338. [PMID: 20094652]
Accepted name: sphingoid base N-palmitoyltransferase
Reaction: palmitoyl-CoA + a sphingoid base = an N-(palmitoyl)-sphingoid base + CoA
Other name(s): mammalian ceramide synthase 5; CERS5 (gene name); LASS5 (gene name)
Systematic name: palmitoyl-CoA:sphingoid base N-palmitoyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 5 (CERS5) is specific for palmitoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Lahiri, S. and Futerman, A.H. LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor. J. Biol. Chem 280 (2005) 33735-33738. [PMID: 16100120]
2. Xu, Z., Zhou, J., McCoy, D.M. and Mallampalli, R.K. LASS5 is the predominant ceramide synthase isoform involved in de novo sphingolipid synthesis in lung epithelia. J. Lipid Res. 46 (2005) 1229-1238. [PMID: 15772421]
3. Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263-271. [PMID: 15823095]
Accepted name: (phenol)carboxyphthiodiolenone synthase
Reaction: (1) 3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + icosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O
(2) 3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + docosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O
(3) 3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)-nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C37-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O
(4) 3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C35-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O
Glossary: C32-carboxyphthiodiolenone = (4E,9R,11R)-9,11-dihydroxy-2,4-dimethyl-3-oxotriacont-4-enoate
C34-carboxyphthiodiolenone = (4E,9R,11R)-9,11-dihydroxy-2,4-dimethyl-3-oxodotriacont-4-enoate
C35-phenolcarboxyphthiodiolenone = (4E)-9,11-dihydroxy-27-(4-hydroxyphenyl)-2,4-dimethyl-3-oxoheptacos-4-enoate
C37-phenolcarboxyphthiodiolenone = (4E,9R,11R)-9,11-dihydroxy-29-(4-hydroxyphenyl)-2,4-dimethyl-3-oxononacos-4-enoate
phthiocerols = linear carbohydrates containing one methoxyl group, one methyl group, and two secondary hydroxyl groups that serve as a backbone for certain lipids and glycolipids found in many species of Mycobacteriaceae
Other name(s): ppsABCDE (gene names)
Systematic name: (methyl)malonyl-CoA:long-chain acyl-[(phenol)carboxyphthiodiolenone synthase] (methyl)malonyltransferase {carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase]-forming}
Comments: The enzyme, which is a complex of five polyketide synthase proteins, is involved in the synthesis of the lipid core common to phthiocerols and phenolphthiocerols. The first protein, PpsA, can accept either a C18 or C20 long-chain fatty acyl, or a (4-hydroxyphenyl)-C17 or C19 fatty acyl. The substrates must first be adenylated by EC 6.2.1.59, long-chain fatty acid adenylase/transferase FadD26, which also loads them onto PpsA. PpsA then extends them using a malonyl-CoA extender unit. The PpsB protein adds the next malonyl-CoA extender unit. The absence of a dehydratase and an enoyl reductase domains in the PpsA and PpsB modules results in the formation of the diol portion of the phthiocerol moiety. PpsC adds a third malonyl unit (releasing a water molecule due to its dehydratase domain), PpsD adds an (R)-methylmalonyl unit, releasing a water molecule, and PpsE adds a second (R)-methylmalonyl unit, without releasing a water molecule. The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product. The enzyme does not contain a thioesterase domain [2], and release of the products requires the tesA-encoded type II thioesterase [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Rao, A. and Ranganathan, A. Interaction studies on proteins encoded by the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Mol. Genet. Genomics 272 (2004) 571-579. [PMID: 15668773]
2. Trivedi, O.A., Arora, P., Vats, A., Ansari, M.Z., Tickoo, R., Sridharan, V., Mohanty, D. and Gokhale, R.S. Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid. Mol. Cell 17 (2005) 631-643. [PMID: 15749014]
Accepted name: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I
Reaction: an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acp] + CO2 + an [acyl-carrier protein]
Other name(s): kasA (gene name); β-ketoacyl-acyl carrier protein synthase KasA
Systematic name: ultra-long-chain mono-unsaturated fattyl acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasA differs from KasB (EC 2.3.1.294), by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Schaeffer, M.L., Agnihotri, G., Volker, C., Kallender, H., Brennan, P.J. and Lonsdale, J.T. Purification and biochemical characterization of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases KasA and KasB. J. Biol. Chem. 276 (2001) 47029-47037. [PMID: 11600501]
2. Bhatt, A., Kremer, L., Dai, A.Z., Sacchettini, J.C. and Jacobs, W.R., Jr. Conditional depletion of KasA, a key enzyme of mycolic acid biosynthesis, leads to mycobacterial cell lysis. J. Bacteriol. 187 (2005) 7596-7606. [PMID: 16267284]
3. Luckner, S.R., Machutta, C.A., Tonge, P.J. and Kisker, C. Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin. Structure 17 (2009) 1004-1013. [PMID: 19604480]
Accepted name: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II
Reaction: an ultra-long-chain di-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = an ultra-long-chain di-unsaturated 3-oxo-fatty acyl-[acp] + CO2 + an [acyl-carrier protein]
Other name(s): kasB (gene name); β-ketoacyl-acyl carrier protein synthase KasB
Systematic name: ultra-long-chain di-unsaturated fattyl acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasB differs from KasA (EC 2.3.1.293), by preferring longer substrates (closer to the upper limit), which also contain two double bonds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Schaeffer, M.L., Agnihotri, G., Volker, C., Kallender, H., Brennan, P.J. and Lonsdale, J.T. Purification and biochemical characterization of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases KasA and KasB. J. Biol. Chem 276 (2001) 47029-47037. [PMID: 11600501]
2. Gao, L.Y., Laval, F., Lawson, E.H., Groger, R.K., Woodruff, A., Morisaki, J.H., Cox, J.S., Daffe, M. and Brown, E.J. Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy. Mol. Microbiol. 49 (2003) 1547-1563. [PMID: 12950920]
3. Molle, V., Brown, A.K., Besra, G.S., Cozzone, A.J. and Kremer, L. The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J. Biol. Chem 281 (2006) 30094-30103. [PMID: 16873379]
4. Bhatt, A., Fujiwara, N., Bhatt, K., Gurcha, S.S., Kremer, L., Chen, B., Chan, J., Porcelli, S.A., Kobayashi, K., Besra, G.S. and Jacobs, W.R., Jr. Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. Proc. Natl Acad. Sci. USA 104 (2007) 5157-5162. [PMID: 17360388]
5. Yamada, H., Bhatt, A., Danev, R., Fujiwara, N., Maeda, S., Mitarai, S., Chikamatsu, K., Aono, A., Nitta, K., Jacobs, W.R., Jr. and Nagayama, K. Non-acid-fastness in Mycobacterium tuberculosis Δ kasB mutant correlates with the cell envelope electron density. Tuberculosis (Edinb) 92 (2012) 351-357. [PMID: 22516756]
6. Vilcheze, C., Molle, V., Carrere-Kremer, S., Leiba, J., Mourey, L., Shenai, S., Baronian, G., Tufariello, J., Hartman, T., Veyron-Churlet, R., Trivelli, X., Tiwari, S., Weinrick, B., Alland, D., Guerardel, Y., Jacobs, W.R., Jr. and Kremer, L. Phosphorylation of KasB regulates virulence and acid-fastness in Mycobacterium tuberculosis. PLoS Pathog. 10 (2014) e1004115. [PMID: 24809459]
Accepted name: mycoketide-CoA synthase
Reaction: a medium-chain acyl-CoA + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = a mycoketide-CoA + 10 CO2 + 10 CoA + 22 NADP+ + 11 H2O
Glossary: a mycoketide-CoA = a 4,8,12,16,20-pentamethyl-(long-chain fatty acyl)-CoA
Other name(s): pks12 (gene name)
Systematic name: malonyl-CoA/(S)-methylmalonyl-CoA:heptanoyl-CoA malonyltransferase (mycoketide-CoA-forming)
Comments: The enzyme, found in mycobacteria, is involved in the synthesis of β-D-mannosyl phosphomycoketides. It is a very large polyketide synthase that contains two complete sets of FAS-like fatty acid synthase modules. It binds an acyl-CoA with 5-9 carbons as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units. Depending on the starter unit, the enzyme forms mycoketide-CoAs of different lengths.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Matsunaga, I., Bhatt, A., Young, D.C., Cheng, T.Y., Eyles, S.J., Besra, G.S., Briken, V., Porcelli, S.A., Costello, C.E., Jacobs, W.R., Jr. and Moody, D.B. Mycobacterium tuberculosis pks12 produces a novel polyketide presented by CD1c to T cells. J. Exp. Med. 200 (2004) 1559-1569. [PMID: 15611286]
Accepted name: ω-hydroxyceramide transacylase
Reaction: a linoleate-containing triacyl-sn-glycerol + an ultra-long-chain ω-hydroxyceramide = a diacyl-sn-glycerol + a linoleate-esterified acylceramide
Glossary: an ultra-long-chain fatty acid = ULCFA = a fatty acid with aliphatic chain of 28 or more carbons
an ultra-long-chain ω-hydroxyceramide = a ceramide that contains an ultra-long-chain ω-hydroxyfatty acid moiety (C28-C36)
acylceramide = ω-O-acylceramide = a ceramide that contains an ultra-long-chain ω-hydroxyfatty acid moiety (C28-C36) that is further extended by ω-esterification with linoleic acid.
Other name(s): PNPLA1 (gene name)
Systematic name: triacyl-sn-glycerol:ultra-long-chain ω-hydroxyceramide ω-O-linoleoyltransferase
Comments: The enzyme participates in the production of acylceramides in the stratum corneum, the outermost layer of the epidermis. Acylceramides are crucial components of the skin permeability barrier.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ohno, Y., Kamiyama, N., Nakamichi, S. and Kihara, A. PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide. Nat. Commun. 8 (2017) 14610. [PMID: 28248318]
Accepted name: very-long-chain ceramide synthase
Reaction: a very-long-chain fatty acyl-CoA + a sphingoid base = a very-long-chain ceramide + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
Other name(s): sphingoid base N-very-long-chain fatty acyl-CoA transferase; mammalian ceramide synthase 2; CERS3 (gene name); LASS3 (gene name); LAG1 (gene name); LAC1 (gene name); LOH1 (gene name); LOH3 (gene name)
Systematic name: very-long-chain fatty acyl-coA:sphingoid base N-acyltransferase
Comments: This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates. The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base. The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated. The mammalian CERS3 isoform catalyses this activity, but has a broader substrate range and also catalyses the activity of EC 2.3.1.298, ultra-long-chain ceramide synthase. Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Guillas, I., Kirchman, P.A., Chuard, R., Pfefferli, M., Jiang, J.C., Jazwinski, S.M. and Conzelmann, A. C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p. EMBO J. 20 (2001) 2655-2665. [PMID: 11387200]
2. Pan, H., Qin, W.X., Huo, K.K., Wan, D.F., Yu, Y., Xu, Z.G., Hu, Q.D., Gu, K.T., Zhou, X.M., Jiang, H.Q., Zhang, P.P., Huang, Y., Li, Y.Y. and Gu, J.R. Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1. Genomics 77 (2001) 58-64. [PMID: 11543633]
3. Schorling, S., Vallee, B., Barz, W.P., Riezman, H. and Oesterhelt, D. Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisae. Mol. Biol. Cell 12 (2001) 3417-3427. [PMID: 11694577]
4. Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263-271. [PMID: 15823095]
5. Laviad, E.L., Albee, L., Pankova-Kholmyansky, I., Epstein, S., Park, H., Merrill, A.H., Jr. and Futerman, A.H. Characterization of ceramide synthase 2: tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate. J. Biol. Chem 283 (2008) 5677-5684. [PMID: 18165233]
6. Imgrund, S., Hartmann, D., Farwanah, H., Eckhardt, M., Sandhoff, R., Degen, J., Gieselmann, V., Sandhoff, K. and Willecke, K. Adult ceramide synthase 2 (CERS2)-deficient mice exhibit myelin sheath defects, cerebellar degeneration, and hepatocarcinomas. J. Biol. Chem 284 (2009) 33549-33560. [PMID: 19801672]
Accepted name: ultra-long-chain ceramide synthase
Reaction: an ultra-long-chain fatty acyl-CoA + a sphingoid base = an ultra-long-chain ceramide + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
an ultra-long-chain fatty acyl-CoA = an acyl-CoA with a chain length of 28 or longer.
Other name(s): mammalian ceramide synthase 3; sphingoid base N-ultra-long-chain fatty acyl-CoA transferase; CERS3 (gene name)
Systematic name: ultra-long-chain fatty acyl-coA:sphingoid base N-acyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 3 (CERS3) is the only enzyme that is active with ultra-long-chain acyl-CoA donors (C28 or longer). It is active in the epidermis, where its products are incorporated into acylceramides. CERS3 also accepts (2R)-2-hydroxy fatty acids and ω-hydroxy fatty acids, and can accept very-long-chain acyl-CoA substrates (see EC 2.3.1.297, very-long-chain ceramide synthase). It can use multiple sphingoid bases including sphinganine, sphingosine, phytosphingosine, and (6R)-6-hydroxysphingosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Mizutani, Y., Kihara, A. and Igarashi, Y. LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity. Biochem. J. 398 (2006) 531-538. [PMID: 16753040]
2. Mizutani, Y., Kihara, A., Chiba, H., Tojo, H. and Igarashi, Y. 2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length. J. Lipid Res. 49 (2008) 2356-2364. [PMID: 18541923]
3. Jennemann, R., Rabionet, M., Gorgas, K., Epstein, S., Dalpke, A., Rothermel, U., Bayerle, A., van der Hoeven, F., Imgrund, S., Kirsch, J., Nickel, W., Willecke, K., Riezman, H., Grone, H.J. and Sandhoff, R. Loss of ceramide synthase 3 causes lethal skin barrier disruption. Hum. Mol. Genet. 21 (2012) 586-608. [PMID: 22038835]
4. Mizutani, Y., Sun, H., Ohno, Y., Sassa, T., Wakashima, T., Obara, M., Yuyama, K., Kihara, A. and Igarashi, Y. Cooperative synthesis of ultra long-chain fatty acid and ceramide during keratinocyte differentiation. PLoS One 8 (2013) e67317. [PMID: 23826266]
Accepted name: sphingoid base N-stearoyltransferase
Reaction: stearoyl-CoA + a sphingoid base = an N-(stearoyl)-sphingoid base + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
Other name(s): mammalian ceramide synthase 1; LASS1 (gene name); UOG1 (gene name); CERS1 (gene name)
Systematic name: stearoyl-CoA:sphingoid base N-stearoyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 1 (CERS1) is structurally and functionally distinctive from all other CERS enzymes, and is specific for stearoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Venkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J.C., Sullards, M.C., Merrill, A.H., Jr. and Futerman, A.H. Upstream of growth and differentiation factor 1 (uog1), a mammalian homolog of the yeast longevity assurance gene 1 (LAG1), regulates N-stearoyl-sphinganine (C18-(dihydro)ceramide) synthesis in a fumonisin B1-independent manner in mammalian cells. J. Biol. Chem 277 (2002) 35642-35649. [PMID: 12105227]
2. Kim, H.J., Qiao, Q., Toop, H.D., Morris, J.C. and Don, A.S. A fluorescent assay for ceramide synthase activity. J. Lipid Res. 53 (2012) 1701-1707. [PMID: 22661289]
3. Wang, Z., Wen, L., Zhu, F., Wang, Y., Xie, Q., Chen, Z. and Li, Y. Overexpression of ceramide synthase 1 increases C18-ceramide and leads to lethal autophagy in human glioma. Oncotarget 8 (2017) 104022-104036. [PMID: 29262618]
4. Turpin-Nolan, S.M., Hammerschmidt, P., Chen, W., Jais, A., Timper, K., Awazawa, M., Brodesser, S. and Bruning, J.C. CerS1-derived C18:0 ceramide in skeletal muscle promotes obesity-induced insulin resistance. Cell Rep. 26 (2019) 1-10.e7. [PMID: 30605666]
Accepted name: branched-chain β-ketoacyl-[acyl-carrier-protein] synthase
Reaction: (1) 3-methylbutanoyl-CoA + a malonyl-[acyl-carrier protein] = a 5-methyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
(2) 2-methylpropanoyl-CoA + a malonyl-[acyl-carrier protein] = a 4-methyl-3-oxopentanoyl-[acyl-carrier-protein] + CoA + CO2
(3) (2S)-2-methylbutanoyl-CoA + a malonyl-[acyl-carrier protein] = a (4S)-4-methyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
Glossary: 3-methylbutanoyl-CoA = isovaleryl-CoA
2-methylpropanoyl-CoA = isobutanoyl-CoA = isobutyryl-CoA
Systematic name: 3-methylbutanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
Comments: The enzyme is responsible for initiating branched-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system (FAS-II) in some bacteria, using molecules derived from degradation of the branched-chain amino acids L-leucine, L-valine, and L-isoleucine to form the starting molecules for elongation by the FAS-II system. In some organisms the enzyme is also able to use acetyl-CoA, leading to production of a mix of branched-chain and straight-chain fatty acids [3] (cf. EC 2.3.1.180, β-ketoacyl-[acyl-carrier-protein] synthase III).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Han, L., Lobo, S. and Reynolds, K.A. Characterization of β-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis. J. Bacteriol. 180 (1998) 4481-4486. [PMID: 9721286]
2. Choi, K.H., Heath, R.J. and Rock, C.O. β-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis. J. Bacteriol. 182 (2000) 365-370. [PMID: 10629181]
3. Khandekar, S.S., Gentry, D.R., Van Aller, G.S., Warren, P., Xiang, H., Silverman, C., Doyle, M.L., Chambers, P.A., Konstantinidis, A.K., Brandt, M., Daines, R.A. and Lonsdale, J.T. Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae β-ketoacyl-acyl carrier protein synthase III (FabH). J. Biol. Chem. 276 (2001) 30024-30030. [PMID: 11375394]
4. Singh, A.K., Zhang, Y.M., Zhu, K., Subramanian, C., Li, Z., Jayaswal, R.K., Gatto, C., Rock, C.O. and Wilkinson, B.J. FabH selectivity for anteiso branched-chain fatty acid precursors in low-temperature adaptation in Listeria monocytogenes. FEMS Microbiol. Lett. 301 (2009) 188-192. [PMID: 19863661]
5. Yu, Y.H., Hu, Z., Dong, H.J., Ma, J.C. and Wang, H.H. Xanthomonas campestris FabH is required for branched-chain fatty acid and DSF-family quorum sensing signal biosynthesis. Sci. Rep. 6 (2016) 32811. [PMID: 27595587]
Accepted name: mycobacterial β-ketoacyl-[acyl carrier protein] synthase III
Reaction: dodecanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: dodecanoyl-CoA = lauroyl-CoA
Other name(s): fabH (gene name) (ambiguous); mycobacterial 3-oxoacyl-[acyl carrier protein] synthase III
Systematic name: dodecanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
Comments: The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms. The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids. The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, β-ketoacyl-[acyl-carrier-protein] synthase III, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300, branched-chain β-ketoacyl-[acyl-carrier-protein] synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Scarsdale, J.N., Kazanina, G., He, X., Reynolds, K.A. and Wright, H.T. Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III. J. Biol. Chem. 276 (2001) 20516-20522. [PMID: 11278743]
2. Musayev, F., Sachdeva, S., Scarsdale, J.N., Reynolds, K.A. and Wright, H.T. Crystal structure of a substrate complex of Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. J. Mol. Biol. 346 (2005) 1313-1321. [PMID: 15713483]
3. Brown, A.K., Sridharan, S., Kremer, L., Lindenberg, S., Dover, L.G., Sacchettini, J.C. and Besra, G.S. Probing the mechanism of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. J. Biol. Chem. 280 (2005) 32539-32547. [PMID: 16040614]
4. Sachdeva, S., Musayev, F.N., Alhamadsheh, M.M., Scarsdale, J.N., Wright, H.T. and Reynolds, K.A. Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH. Chem. Biol. 15 (2008) 402-412. [PMID: 18420147]
] Accepted name: hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-hydroxycinnamoyltransferase
Reaction: (1) (E)-4-coumaroyl-CoA + 5-hydroxyanthranilate = avenanthramide A + CoA
(2) (E)-caffeoyl-CoA + 5-hydroxyanthranilate = avenanthramide C + CoA
Glossary: avenanthramide A = 5-hydroxy-2-[(2E)-3-(4-hydroxyphenyl)prop-2-enamido]benzoate
avenanthramide C = 2-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enamido]-5-hydroxybenzoate
Other name(s): HHT1 (gene name); HHT4 (gene name)
Systematic name: hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-hydroxycinnamoyltransferase
Comments: The enzyme participates in the biosynthesis of avenanthramides, phenolic alkaloids found mainly in oats (Avena sativa). It is related to EC 2.3.1.133, shikimate O-hydroxycinnamoyltransferase. The enzyme from oat does not accept feruloyl-CoA as a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ishihara, A., Matsukawa, T., Miyagawa, H., Ueno, T. and Mayama, S. Induction of hydroxycinnamoyl-CoA: hydroxyanthranilate N-hydroxycinnamoyltransferase (HHT) activity in oat leaves by victorin C. Z. Naturforsch. C 52 (1997) 756-760.
2. Yang, Q., Trinh, H.X., Imai, S., Ishihara, A., Zhang, L., Nakayashiki, H., Tosa, Y. and Mayama, S. Analysis of the involvement of hydroxyanthranilate hydroxycinnamoyltransferase and caffeoyl-CoA 3-O-methyltransferase in phytoalexin biosynthesis in oat. Mol. Plant Microbe Interact. 17 (2004) 81-89. [PMID: 14714871]
3. D'Auria, J.C. Acyltransferases in plants: a good time to be BAHD. Curr. Opin. Plant Biol. 9 (2006) 331-340. [PMID: 16616872]
4. Bontpart, T., Cheynier, V., Ageorges, A. and Terrier, N. BAHD or SCPL acyltransferase? What a dilemma for acylation in the world of plant phenolic compounds. New Phytol. 208 (2015) 695-707. [PMID: 26053460]
5. Li, Z., Chen, Y., Meesapyodsuk, D. and Qiu, X. The biosynthetic pathway of major avenanthramides in oat. Metabolites 9 (2019) . [PMID: 31394723]
Accepted name: α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und 2IV-O-acetyltransferase
Reaction: acetyl-CoA + α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = CoA + 2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): rfbL (gene name); wbaL (gene name)
Systematic name: acetyl-CoA:α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 2IV-O-acetyltransferase
Comments: The enzyme, present in Salmonella strains that belong to group C2, participates in the biosynthesis of the repeat unit of O antigens produced by these strains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Brown, P.K., Romana, L.K. and Reeves, P.R. Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen (strain M67): the genetic basis of the polymorphism between groups C2 and B. Mol. Microbiol. 6 (1992) 1385-1394. [PMID: 1379320]
2. Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084-4088. [PMID: 7541787]
3. Zhao, X., Dai, Q., Jia, R., Zhu, D., Liu, M., Wang, M., Chen, S., Sun, K., Yang, Q., Wu, Y. and Cheng, A. two novel Salmonella bivalent vaccines confer dual protection against two Salmonella serovars in mice. Front Cell Infect Microbiol 7 (2017) 391. [PMID: 28929089]
Accepted name: poly[(R)-3-hydroxyalkanoate] polymerase
Reaction: (3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n = CoA + poly[(R)-3-hydroxyalkanoate]n+1
Other name(s): PHA synthase; phaC (gene name); PhaE
Systematic name: poly(R)-3-hydroxyalkanoate (3R)-3-hydroxyacyltransferase
Comments: This is the key enzyme in the biosynthesis of polyhydroxyalkanoates (PHA), linear polyesters produced by bacteria as a means of carbon and energy storage [6]. The enzyme catalyses the stereoselective, covalent linkage of (3R)-3-hydroxyacyl-CoA thioesters in a transesterification reaction with concomitant release of coenzyme A. The growing polymer is attached to a conserved active site L-cysteine residue. Three types of PHA synthases have been proposed based on their substrate specificity and enzyme structure. Type I and type III synthases preferentially polymerize short chain hydroxyalkanoate monomers containing 3-5 carbon atoms [1,2]. The difference between these two types is that type I synthases are composed of only a single subunit (PhaC), whereas type III synthases are composed of two different subunits, PhaC and PhaE [3,5]. Type II synthases are also composed of a single subunit (PhaC), but preferentially polymerize monomers containing more than 5 carbon atoms [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Anderson, A.J., Haywood, G.W. and Dawes, E.A. Biosynthesis and composition of bacterial poly(hydroxyalkanoates). Int. J. Biol. Macromol. 12 (1990) 102-105. [PMID: 2078525]
2. Liebergesell, M., Sonomoto, K., Madkour, M., Mayer, F. and Steinbuchel, A. Purification and characterization of the poly(hydroxyalkanoic acid) synthase from Chromatium vinosum and localization of the enzyme at the surface of poly(hydroxyalkanoic acid) granules. Eur. J. Biochem. 226 (1994) 71-80. [PMID: 7957260]
3. Muh, U., Sinskey, A.J., Kirby, D.P., Lane, W.S. and Stubbe, J. PHA synthase from Chromatium vinosum: cysteine 149 is involved in covalent catalysis. Biochemistry 38 (1999) 826-837. [PMID: 9888824]
4. Ren, Q., De Roo, G., Kessler, B. and Witholt, B. Recovery of active medium-chain-length-poly-3-hydroxyalkanoate polymerase from inactive inclusion bodies using ion-exchange resin. Biochem. J. 349 (2000) 599-604. [PMID: 10880359]
5. Jia, Y., Yuan, W., Wodzinska, J., Park, C., Sinskey, A.J. and Stubbe, J. Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: class I and III synthases share a similar catalytic mechanism. Biochemistry 40 (2001) 1011-1019. [PMID: 11170423]
6. Zou, H., Shi, M., Zhang, T., Li, L., Li, L. and Xian, M. Natural and engineered polyhydroxyalkanoate (PHA) synthase: key enzyme in biopolyester production. Appl. Microbiol. Biotechnol. 101 (2017) 7417-7426. [PMID: 28884324]
Accepted name: acyl-[acyl-carrier protein]—UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose N-acyltransferase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose = an [acyl-carrier protein] + a UDP-2-acetamido-2,3-dideoxy-3-{[(3R)-3-hydroxyacyl]amino}-α-D-glucopyranose
Other name(s): lpxA (gene name) (ambiguous)
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier-protein]:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose 3-N-[(3R)-hydroxyacyl]transferase
Comments: The enzyme is found in bacterial species whose lipid A contains 2,3-diamino-2,3-dideoxy-D-glucopyranose. Some enzymes, such as that from Leptospira interrogans, are highly specific for 2,3-diamino-2,3-dideoxy-D-glucopyranose, while others, such as the enzyme from Acidithiobacillus ferrooxidans, are also able to accept UDP-N-acetyl-α-D-glucosamine (cf. EC 2.3.1.129, acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase). The enzymes from different organisms also differ in their specificity for the acyl donor. The enzyme from Leptospira interrogans is highly specific for (3R)-3-hydroxydodecanoyl-[acp], while that from Mesorhizobium loti functions almost equally well with 10-, 12-, and 14-carbon 3-hydroxyacyl-[acp]s.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sweet, C.R., Williams, A.H., Karbarz, M.J., Werts, C., Kalb, S.R., Cotter, R.J. and Raetz, C.R. Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group. J. Biol. Chem. 279 (2004) 25411-25419. [PMID: 15044493]
2. Robins, L.I., Williams, A.H. and Raetz, C.R. Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA. Biochemistry 48 (2009) 6191-6201. [PMID: 19456129]
Accepted name: acetyl-CoA:lysine N6-acetyltransferase
Reaction: acetyl-CoA + L-lysine = CoA + N6-acetyl-L-lysine
Other name(s): LYC1 (gene name); lysine N6-acetyltransferase (ambiguous)
Systematic name: acetyl-CoA:L-lysine N6-acetyltransferase
Comments: The enzyme catalyses the first step of an L-lysine degradation pathway found in many fungal species. The enzyme is specific for acetyl-CoA as the acetyl donor. cf. EC 2.3.1.32, lysine N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Schmidt, H., Bode, R., and Birnbaum , D. Lysine degradation in Candida maltosa: occurrence of a novel enzyme, acetyl-CoA: L-lysine N-acetyltransferase. Arch. Microbiol. 150 (1988) 215-218.
2. Large, P.J. and Robertson, A. The route of lysine breakdown in Candida tropicalis, FEMS Microbiol. Lett. 66 (1991) 209-213. [PMID: 1682209]
3. Bode, R., Thurau, A.M. and Schmidt, H. Characterization of acetyl-CoA: L-lysine N6-acetyltransferase, which catalyses the first step of carbon catabolism from lysine in Saccharomyces cerevisiae, Arch. Microbiol. 160 (1993) 397-400. [PMID: 8257283]
4. Beckerich, J.M., Lambert, M. and Gaillardin, C. LYC1 is the structural gene for lysine N-6-acetyl transferase in yeast. Curr. Genet. 25 (1994) 24-29. [PMID: 8082161]
Accepted name: 6-diazo-5-oxo-L-norleucine Nα-acetyltranferase
Reaction: acetyl-CoA + 6-diazo-5-oxo-L-norleucine = CoA + N-acetyl-6-diazo-5-oxo-L-norleucine
Other name(s): azpI (gene name)
Systematic name: acetyl-CoA:6-diazo-5-oxo-L-norleucine Nα-acetyltransferase
Comments: The enzyme, characterized from the bacterium Streptacidiphilus griseoplanus, participates in the biosynthesis of the tripeptide alazopeptin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kawai, S., Sugaya, Y., Hagihara, R., Tomita, H., Katsuyama, Y. and Ohnishi, Y. Complete biosynthetic pathway of alazopeptin, a tripeptide consisting of two molecules of 6-diazo-5-oxo-L-norleucine and one molecule of alanine. Angew. Chem. Int. Ed. Engl. 60 (2021) 10319-10325. [PMID: 33624374]
Accepted name: tubulin N-terminal N-acetyltransferase NAT9
Reaction: acetyl-CoA + an N-terminal-L-methionyl-[tubulin] = an N-terminal-Nα-acetyl-L-methionyl-[tubulin] + CoA
Other name(s): NAT9 (gene name); microtubule-associated N-acetyltransferase NAT9
Systematic name: acetyl-CoA:N-terminal-Met-[tubulin] Met-Nα-acetyltransferase
Comments: The enzyme, characterized from the fruit fly (Drosophila melanogaster), acetylates the N-terminal of both α- and β-tubulin. The enzyme acts cotranslationally, and can't act on a preformed tubulin α/β heterodimer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Mok, J.W. and Choi, K.W. Novel function of N-acetyltransferase for microtubule stability and JNK signaling in Drosophila organ development. Proc. Natl. Acad. Sci. USA 118 (2021) . [PMID: 33479178]
Accepted name: [β-tubulin]-L-lysine N-acetyltransferase
Reaction: acetyl-CoA + a [β-tubulin]-L-lysine = CoA + a [β-tubulin]-N6-acetyl-L-lysine
Other name(s): San; NatE; NAA50 (gene name)
Systematic name: acetyl-CoA:[β-tubulin]-L-lysine N6-acetyltransferase
Comments: The enzyme acetylates L-lysine at position 252 of β-tubulin, which is located at the interface of α/β-tubulin heterodimers and interacts with the phosphate group of the α-tubulin-bound GTP. The acetylation is thought to attenuate tubulin incorporation into microtubules. The enzyme catalysing this activity (NAA50) also catalyses the acetylation of certain N-terminal methionyl residues. That activity is classified as EC 2.3.1.258, N-terminal methionine Nα-acetyltransferase NatE. cf. EC 2.3.1.108, α-tubulin N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Chu, C.W., Hou, F., Zhang, J., Phu, L., Loktev, A.V., Kirkpatrick, D.S., Jackson, P.K., Zhao, Y. and Zou, H. A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol. Biol. Cell 22 (2011) 448-456. [PMID: 21177827]
Accepted name: benzoylsuccinyl-CoA thiolase
Reaction: (S)-2-benzoylsuccinyl-CoA + CoA = benzoyl-CoA + succinyl-CoA
Other name(s): bbsAB (gene names)
Systematic name: (S)-2-benzoylsuccinyl-CoA:CoA benzoyltransferase (benzoyl-CoA-forming)
Comments: The enzyme, characterized from the bacteria Thauera aromatica and Geobacter metallireducens, participates in an anaerobic toluene degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Leuthner, B. and Heider, J. Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of β oxidation of the intermediate benzylsuccinate. J. Bacteriol. 182 (2000) 272-277. [PMID: 10629170]
2. Weidenweber, S., Schuhle, K., Lippert, M.L., Mock, J., Seubert, A., Demmer, U., Ermler, U. and Heider, J. Finis tolueni: a new type of thiolase with an integrated Zn-finger subunit catalyzes the final step of anaerobic toluene metabolism. FEBS J. (2022) . [PMID: 35313080]
Accepted name: tRNA carboxymetyluridine synthase
Reaction: acetyl-CoA + uridine34 in tRNA + S-adenosyl-L-methionine + H2O = CoA + 5-(carboxymethyl)uridine34 in tRNA + L-methionine + 5'-deoxyadenosine
Other name(s): elongator complex; ELP3
Systematic name: acetyl-CoA:tRNA uridine carboxymethyltransferase
Comments: The enzyme, found in eukaryotes, most archaea, and some bacteria, catalyses the first step in modification of the wobble uridine base of certain tRNAs. In eukaryotes the enzyme is a complex of six conserved subunits, with ELP3 being the catalytic subunit. In archaea and bacteria the enzyme consists of a single subunit, homologous to ELP3. The enzyme contains an [4Fe-4S] cluster and uses radical chemistry. A 5'-deoxyadenosyl radical generated in the radical AdoMet (SAM) domain attacks the acetyl-CoA donor, activating its methyl group, which forms a C-C bond with C5 of the uridine moiety.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Paraskevopoulou, C., Fairhurst, S.A., Lowe, D.J., Brick, P. and Onesti, S. The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine. Mol. Microbiol. 59 (2006) 795-806. [PMID: 16420352]
2. Selvadurai, K., Wang, P., Seimetz, J. and Huang, R.H. Archaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism. Nat. Chem. Biol. 10 (2014) 810-812. [PMID: 25151136]
3. Lin, T.Y., Abbassi, N.EH., Zakrzewski, K., Chramiec-Glabik, A., Jemiola-Rzeminska, M., Rozycki, J. and Glatt, S. The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase. Nat. Commun. 10 (2019) 625. [PMID: 30733442]
Accepted name: D-glutamate N-acetyltransferase
Reaction: acetyl-CoA + D-glutamate = N-acetyl-D-glutamate + CoA
Other name(s): dgcN (gene name)
Systematic name: acetyl-CoA:D-glutamate N-acetyltransferase
Comments: The enzyme, present in bacteria and archaea, participates in a pathway for the degradation of D-glutamate. The enzyme from the marine bacterium Pseudoalteromonas sp. CF6-2 can also acetylate D-glutamine, D-aspartate, and D-asparagine with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yu, Y., Wang, P., Cao, H.Y., Teng, Z.J., Zhu, Y., Wang, M., McMinn, A., Chen, Y., Xiang, H., Zhang, Y.Z., Chen, X.L. and Zhang, Y.Q. Novel D-glutamate catabolic pathway in marine Proteobacteria and halophilic archaea. ISME J. (2023) . [PMID: 36690779]
Accepted name: NAD-dependent lipoamidase
Reaction: [lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine + NAD+ + H2O = [lipoyl-carrier protein]-L-lysine + 2''-O-lipoyl-ADP-D-ribose + nicotinamide
Other name(s): SIRT4; srtN (gene name); cobB (gene name)
Systematic name: [lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine:NAD+ lipoyltranferase (NAD+-hydrolysing; 2''-O-lipoyl-ADP-D-ribose-forming)
Comments: The enzyme, a member of the sirtuin family, removes the lipoyl group from the dihydrolipoamide acyltransferase (E2) component of 2-oxo acid dehydrogenase complexes such as EC 1.2.1.104, pyruvate dehydrogenase system. The enzyme often has additional activities and can remove other modifications of lysine residues such as acetyl and biotinyl groups. cf. EC 3.5.1.138, lipoamidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Mathias, R.A., Greco, T.M., Oberstein, A., Budayeva, H.G., Chakrabarti, R., Rowland, E.A., Kang, Y., Shenk, T. and Cristea, I.M. Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity. Cell 159 (2014) 1615-1625. [PMID: 25525879]
2. Rowland, E.A., Greco, T.M., Snowden, C.K., McCabe, A.L., Silhavy, T.J. and Cristea, I.M. Sirtuin lipoamidase activity is conserved in bacteria as a regulator of metabolic enzyme complexes. mBio 8 (2017) e01096-17. [PMID: 28900027]
3. Betsinger, C.N. and Cristea, I.M. Mitochondrial function, metabolic regulation, and human disease viewed through the prism of sirtuin 4 (SIRT4) functions. J Proteome Res 18 (2019) 1929-1938. [PMID: 30913880]
Accepted name: phytol O-acyltransferase
Reaction: an acyl-CoA + phytol = a fatty acid phytyl ester + CoA
Other name(s): phytyl ester synthase; PES1 (gene name); PES2 (gene name); slr2103 (locus name)
Systematic name: acyl-CoA:phytol O-acyltransferase
Comments: The enzyme is found in plant chloroplasts and cyanobacteria. The plant enzyme can also employ acyl carrier proteins and galactolipids as acyl donors, while the enzyme from the cyanobacterium Synechocystis sp. PCC 6803 only uses acyl-CoAs. The enzyme also catalyses the activity of EC 2.3.1.20, diacylglycerol O-acyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ischebeck, T., Zbierzak, A.M., Kanwischer, M. and Dormann, P. A salvage pathway for phytol metabolism in Arabidopsis. J. Biol. Chem. 281 (2006) 2470-2477. [PMID: 16306049]
2. Lippold, F., vom Dorp, K., Abraham, M., Holzl, G., Wewer, V., Yilmaz, J.L., Lager, I., Montandon, C., Besagni, C., Kessler, F., Stymne, S. and Dormann, P. Fatty acid phytyl ester synthesis in chloroplasts of Arabidopsis. Plant Cell 24 (2012) 2001-2014. [PMID: 22623494]
3. Aizouq, M., Peisker, H., Gutbrod, K., Melzer, M., Holzl, G. and Dormann, P. Triacylglycerol and phytyl ester synthesis in Synechocystis sp. PCC6803. Proc. Natl. Acad. Sci. USA 117 (2020) 6216-6222. [PMID: 32123083]
4. Tanaka, M., Ishikawa, T., Tamura, S., Saito, Y., Kawai-Yamada, M. and Hihara, Y. Quantitative and qualitative analyses of triacylglycerol production in the wild-type Cyanobacterium Synechocystis sp. PCC 6803 and the strain expressing AtfA from Acinetobacter baylyi ADP1. Plant Cell Physiol. 61 (2020) 1537-1547. [PMID: 32433767]
Accepted name: succinyl-CoA:cyclohexane-1-carboxylate CoA transferase
Reaction: succinyl-CoA + cyclohexane-1-carboxylate = succinate + cyclohexane-1-carbonyl-CoA
Other name(s): Gmet_3304 (locus name)
Systematic name: succinyl-CoA—cyclohexane-1-carboxylate CoA-transferase
Comments: The enzyme, characterized from the bacterium Geobacter metallireducens, participates in an anaerobic degradation pathway for cyclohexane-1-carboxylate. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kung, J.W., Meier, A.K., Mergelsberg, M. and Boll, M. Enzymes involved in a novel anaerobic cyclohexane carboxylic acid degradation pathway. J. Bacteriol. 196 (2014) 3667-3674. [PMID: 25112478]
Accepted name: N-hydroxyputrescine acetyltransferase
Reaction: acetyl-CoA + N-hydroxyputrescine = N1-acetyl-N1-hydroxyputrescine + CoA
Glossary: N-hydroxyputrescine = N-hydroxybutane-1,4-diamine
Other name(s): fbsK (gene name)
Systematic name: acetyl-CoA:N-hydroxyputrescine N-acetyltransferase
Comments: The enzyme, characterized from the bacterium Acinetobacter baumannii ATCC 17978, participates in the biosynthesis of fimsbactin siderophores.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Proschak, A., Lubuta, P., Grun, P., Lohr, F., Wilharm, G., De Berardinis, V. and Bode, H.B. Structure and biosynthesis of fimsbactins A-F, siderophores from Acinetobacter baumannii and Acinetobacter baylyi. Chembiochem 14 (2013) 633-638. [PMID: 23456955]
2. Yang, J. and Wencewicz, T.A. In vitro reconstitution of fimsbactin biosynthesis from Acinetobacter baumannii. ACS Chem. Biol. 17 (2022) 2923-2935. [PMID: 36122366]
Accepted name: 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase
Reaction: 3-dehydrocarnitine + acetyl-CoA = acetoacetate + betainyl-CoA
Other name(s): cdhC (gene name); 3-dehydrocarnitine cleavage enzyme
Systematic name: 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase
Comments: The enzyme, characterized from Pseudomonas aeruginosa and other bacteria, belongs to a class of enzymes known as β-keto acid cleavage enzymes (BKACE). It participates in an L-carnitine degradation pathway. cf. EC 2.3.1.247, (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase, EC 2.3.1.318, 3-oxoadipate:acetyl-CoA acetyltransferase, and EC 2.3.1.319, 3,5-dioxohexanoate:acetyl-CoA acetone transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wargo, M.J. and Hogan, D.A. Identification of genes required for Pseudomonas aeruginosa carnitine catabolism. Microbiology (Reading) 155 (2009) 2411-2419. [PMID: 19406895]
2. Bastard, K., Smith, A.A., Vergne-Vaxelaire, C., Perret, A., Zaparucha, A., De Melo-Minardi, R., Mariage, A., Boutard, M., Debard, A., Lechaplais, C., Pelle, C., Pellouin, V., Perchat, N., Petit, J.L., Kreimeyer, A., Medigue, C., Weissenbach, J., Artiguenave, F., De Berardinis, V., Vallenet, D. and Salanoubat, M. Revealing the hidden functional diversity of an enzyme family. Nat. Chem. Biol. 10 (2014) 42-49. [PMID: 24240508]
Accepted name: 3-oxoadipate:acetyl-CoA acetyltransferase
Reaction: 3-oxoadipate + acetyl-CoA = acetoacetate + succinyl-CoA
Glossary: 3-oxoadipate = β-ketoadipate = 3-oxohexanedioate
Other name(s): 3-oxoadipate cleavage enzyme
Systematic name: 3-oxoadipate:acetyl-CoA acetyltransferase
Comments: The enzyme, characterized from the bacteria Pseudomonas aeruginosa and Cupriavidus necator H16, belongs to a class of enzymes known as β-keto acid cleavage enzymes (BKACE). cf. EC 2.3.1.247, (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase, EC 2.3.1.317, 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase, and EC 2.3.1.319, 3,5-dioxohexanoate:acetyl-CoA acetone transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bastard, K., Smith, A.A., Vergne-Vaxelaire, C., Perret, A., Zaparucha, A., De Melo-Minardi, R., Mariage, A., Boutard, M., Debard, A., Lechaplais, C., Pelle, C., Pellouin, V., Perchat, N., Petit, J.L., Kreimeyer, A., Medigue, C., Weissenbach, J., Artiguenave, F., De Berardinis, V., Vallenet, D. and Salanoubat, M. Revealing the hidden functional diversity of an enzyme family. Nat. Chem. Biol. 10 (2014) 42-49. [PMID: 24240508]
Accepted name: 3,5-dioxohexanoate:acetyl-CoA acetone transferase
Reaction: 3,5-dioxohexanoate + acetyl-CoA = acetoacetate + acetoacetyl-CoA
Other name(s): 3,5-dioxohexanoate cleavage enzyme
Systematic name: 3,5-dioxohexanoate:acetyl-CoA acetone transferase
Comments: The enzyme, characterized from fungus Blumeria graminis, belongs to a class of enzymes known as β-keto acid cleavage enzymes (BKACE). cf. EC 2.3.1.247, (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase, EC 2.3.1.317, 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase, and EC 2.3.1.318, 3-oxoadipate:acetyl-CoA acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bastard, K., Smith, A.A., Vergne-Vaxelaire, C., Perret, A., Zaparucha, A., De Melo-Minardi, R., Mariage, A., Boutard, M., Debard, A., Lechaplais, C., Pelle, C., Pellouin, V., Perchat, N., Petit, J.L., Kreimeyer, A., Medigue, C., Weissenbach, J., Artiguenave, F., De Berardinis, V., Vallenet, D. and Salanoubat, M. Revealing the hidden functional diversity of an enzyme family. Nat. Chem. Biol. 10 (2014) 42-49. [PMID: 24240508]
Accepted name: taxoid C-13 O-(3-amino-3-phenylpropanoyl)transferase
Reaction: baccatin III + (3R)-3-amino-3-phenylpropanoyl-CoA = 3'-N-debenzoyl-2'-deoxytaxol + CoA
Glossary: (3R)-3-amino-3-phenylpropanoyl-CoA = (3R)-β-phenylalanyl-CoA
Other name(s): BAPT; baccatin III:3-amino-3-phenylpropanoyltransferase; baccatin III-3-amino-13-phenylpropanoyltransferase; 3'-N-de-benzoyl-2'-deoxytaxol-N-benzoyltransferase
Systematic name: (3R)-3-amino-3-phenylpropanoyl-CoA:baccatin III C-13 O-((3R)-3-amino-3-phenylpropanoyl)transferase
Comments: The enzyme is active in the biosynthetic pathway of paclitaxel (Taxol) in Taxus species (yew)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Walker, K., Fujisaki, S., Long, R. and Croteau, R. Molecular cloning and heterologous expression of the C-13 phenylpropanoid side chain-CoA acyltransferase that functions in Taxol biosynthesis. Proc. Natl. Acad. Sci. USA 99 (2002) 12715-12720. [PMID: 12232048]
Accepted name: 3'-N-debenzoyltaxol N-benzoyltransferase
Reaction: benzoyl-CoA + 3'-N-debenzoyltaxol = CoA + paclitaxel
Other name(s): DBTNBT; 3'-N-debenzoyl-2'-deoxytaxol N-benzoyltransferase
Systematic name: benzoyl-CoA:3'-N-debenzoyltaxol 3'-N-benzoyltransferase
Comments: The enzyme, present in Taxus species (yew) catalyses the final step in paclitaxel (Taxol) biosynthesis
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Walker, K., Long, R. and Croteau, R. The final acylation step in taxol biosynthesis: cloning of the taxoid C13-side-chain N-benzoyltransferase from Taxus. Proc. Natl. Acad. Sci. USA 99 (2002) 9166-9171. [PMID: 12089320]
2. Long, R.M., Lagisetti, C., Coates, R.M. and Croteau, R.B. Specificity of the N-benzoyl transferase responsible for the last step of Taxol biosynthesis. Arch. Biochem. Biophys. 477 (2008) 384-389. [PMID: 18621016]
3. Zhang, Y., Wiese, L., Fang, H., Alseekh, S., Perez de Souza, L., Scossa, F., Molloy, J., Christmann, M. and Fernie, A.R. Synthetic biology identifies the minimal gene set required for paclitaxel biosynthesis in a plant chassis. Mol. Plant 16 (2023) 1951-1961. [PMID: 37897038]
Accepted name: akuammiline synthase
Reaction: acetyl-CoA + rhazimol = CoA + akuammiline
For diagram of reaction click here
Other name(s): AsAKS1; AsAKS2
Systematic name: acetyl-CoA:rhazimol O-acetyltransferase
Comments: Isolated from the plant Alstonia scholaris (blackboard tree).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wang, Z., Xiao, Y., Wu, S., Chen, J., Li, A. and Tatsis, E.C. Deciphering and reprogramming the cyclization regioselectivity in bifurcation of indole alkaloid biosynthesis. Chem. Sci. 13 (2022) 12389-12395. [PMID: 36349266]
Accepted name: stemmadenine O-acetyltransferase
Reaction: acetyl-CoA + stemmadenine = CoA + stemmadenine acetate
For diagram of reaction, click here
Other name(s): SAT (gene name)
Systematic name: acetyl-CoA:stemmadenine O-acetyltransferase
Comments: The enzyme, characterized from the plant Catharanthus roseus (Madagascar periwinkle), participates in a pathway that leads to the production of a number of monoterpene alkaloids, as well as the bisindole alkaloids vinblastine and vincristine, which are used as anticancer drugs.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Qu, Y., Easson, M.EA.M., Simionescu, R., Hajicek, J., Thamm, A.MK., Salim, V. and De Luca, V. Solution of the multistep pathway for assembly of corynanthean, strychnos, iboga, and aspidosperma monoterpenoid indole alkaloids from 19E-geissoschizine. Proc. Natl. Acad. Sci. USA 115 (2018) 3180-3185. [PMID: 29511102]