EC 2.5.1.1 to EC 2.5.1.50
EC 2.1.1.51 to EC 2.1.1.100
Accepted name: N,N'-diacetyllegionaminate synthase
Reaction: 2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose + phosphoenolpyruvate + H2O = N,N'-diacetyllegionaminate + phosphate
For diagram of reaction click here and mechanism click here.
Glossary: legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate
Other name(s): SSL-1 (gene name); hpnD (gene name)
Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate-forming)
Comments: Requires a divalent metal such as Mn2+. Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni, where it is involved in the biosynthesis of legionaminic acid, a virulence-associated, cell surface sialic acid-like derivative.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272-3282. [PMID: 18275154]
2. Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715-725. [PMID: 19282391]
Accepted name: geranyl-pyrophosphate—olivetolic acid geranyltransferase
Reaction: geranyl diphosphate + 2,4-dihydroxy-6-pentylbenzoate = diphosphate + cannabigerolate
For diagram of reaction click here.
Glossary: 2,4-dihydroxy-6-pentylbenzoate = olivetolate
cannabigerolate = CBGA = 3-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-2,4-dihydroxy-6-pentylbenzoate
cannabinerolate = 3-[(2Z)-3,7-dimethylocta-2,6-dien-1-yl]-2,4-dihydroxy-6-pentylbenzoate
Other name(s): GOT (ambiguous)
Systematic name: geranyl-diphosphate:olivetolate geranyltransferase
Comments: Part of the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme can also use neryl diphosphate as substrate, forming cannabinerolate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fellermeier, M. and Zenk, M.H. Prenylation of olivetolate by a hemp transferase yields cannabigerolic acid, the precursor of tetrahydrocannabinol. FEBS Lett 427 (1998) 283-285. [PMID: 9607329]
Accepted name: presqualene diphosphate synthase
Reaction: 2 (2E,6E)-farnesyl diphosphate = presqualene diphosphate + diphosphate
For diagram of reaction click here.
Other name(s): SSL-1 (gene name); hpnD (gene name)
Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate-forming)
Comments: Isolated from the green alga Botryococcus braunii BOT22. Unlike EC 2.5.1.21, squalene synthase, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme. This compound is then converted into either squalene (by EC 1.3.1.96, Botryococcus squalene synthase) or botryococcene (EC 1.3.1.97, botryococcene synthase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Niehaus, T.D., Okada, S., Devarenne, T.P., Watt, D.S., Sviripa, V. and Chappell, J. Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii. Proc. Natl. Acad. Sci. USA 108 (2011) 12260-12265. [PMID: 21746901]
2. Pan, J.J., Solbiati, J.O., Ramamoorthy, G., Hillerich, B.S., Seidel, R.D., Cronan, J.E., Almo, S.C. and Poulter, C.D. Biosynthesis of squalene from farnesyl diphosphate in bacteria: three steps catalyzed by three enzymes. ACS Cent Sci 1 (2015) 77-82. [PMID: 26258173]
Accepted name: N1-aminopropylagmatine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-(3-aminopropyl)agmatine
For diagram of reaction click here.
Glossary: S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE (ambiguous); agmatine aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase
Comments: The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and Oshima, T. N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J. Biol. Chem. 280 (2005) 30073-30082. [PMID: 15983049]
2. Cacciapuoti, G., Porcelli, M., Moretti, M.A., Sorrentino, F., Concilio, L., Zappia, V., Liu, Z.J., Tempel, W., Schubot, F., Rose, J.P., Wang, B.C., Brereton, P.S., Jenney, F.E. and Adams, M.W. The first agmatine/cadaverine aminopropyl transferase: biochemical and structural characterization of an enzyme involved in polyamine biosynthesis in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 189 (2007) 6057-6067. [PMID: 17545282]
3. Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991-5001. [PMID: 20675472]
4. Ohnuma, M., Ganbe, T., Terui, Y., Niitsu, M., Sato, T., Tanaka, N., Tamakoshi, M., Samejima, K., Kumasaka, T. and Oshima, T. Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus. J. Mol. Biol. 408 (2011) 971-986. [PMID: 21458463]
Accepted name: 7,8-dihydropterin-6-yl-methyl-4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate synthase
Reaction: (7,8-dihydropterin-6-yl)methyl diphosphate + 4-(β-D-ribofuranosyl)aniline 5'-phosphate = N-[(7,8-dihydropterin-6-yl)methyl]-4-(β-D-ribofuranosyl)aniline 5'-phosphate + diphosphate
For diagram of reaction click here.
Other name(s): MJ0301 (gene name); dihydropteroate synthase (ambiguous)
Systematic name: (7,8-dihydropterin-6-yl)methyl-diphosphate:4-(β-D-ribofuranosyl)aniline 5'-phosphate 6-hydroxymethyl-7,8-dihydropterintransferase
Comments: The enzyme, which has been studied in the archaeon Methanocaldococcus jannaschii, is involved in the biosynthesis of tetrahydromethanopterin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Xu, H., Aurora, R., Rose, G.D. and White, R.H. Identifying two ancient enzymes in Archaea using predicted secondary structure alignment. Nat. Struct. Biol. 6 (1999) 750-754. [PMID: 10426953]
Accepted name: tryprostatin B synthase
Reaction: dimethylallyl diphosphate + brevianamide F = diphosphate + tryprostatin B
For diagram of reaction click here.
Glossary: brevianamide F = (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
tryprostatin B = (3S,8aS)-3-{[2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
Other name(s): ftmPT1 (gene name); brevianamide F prenyltransferase (ambiguous)
Systematic name: dimethylallyl-diphosphate:brevianamide-F dimethylallyl-C-2-transferase
Comments: The enzyme from the fungus Aspergillus fumigatus can also prenylate other tryptophan-containing cyclic dipeptides. Prenylation occurs mainly at C-2 [1], but also at C-3 [2]. Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, cyclotryprostatins, spirotryprostatins, fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Grundmann, A. and Li, S.M. Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus. Microbiology 151 (2005) 2199-2207. [PMID: 16000710]
2. Wollinsky, B., Ludwig, L., Xie, X. and Li, S.M. Breaking the regioselectivity of indole prenyltransferases: identification of regular C3-prenylated hexahydropyrrolo[2,3-b]indoles as side products of the regular C2-prenyltransferase FtmPT1. Org. Biomol. Chem. 10 (2012) 9262-9270. [PMID: 23090579]
Accepted name: verruculogen prenyltransferase
Reaction: dimethylallyl diphosphate + verruculogen = diphosphate + fumitremorgin A
For diagram of reaction click here.
Glossary: verruculogen = (5R,10S,10aR,14aS,15bS)-10,10a-dihydroxy-6-methoxy-2,2-dimethyl-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(2H,13H)-dione
fumitremorgin A = (5R,10S,10aR,14aS,15bS)-10a-hydroxy-7-methoxy-2,2-dimethyl-10-[(3-methylbut-2-en-1-yl)oxy]-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(H,13H)-dione
Other name(s): FtmPT3
Systematic name: dimethylallyl-diphosphate:verruculogen dimethylallyl-O-transferase
Comments: Found in a number of fungi. Catalyses the last step in the biosynthetic pathway of the indole alkaloid fumitremorgin A. The enzyme from the fungus Neosartorya fischeri is also active with fumitremorgin B and 12α,13α-dihydroxyfumitremorgin C.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Mundt, K., Wollinsky, B., Ruan, H.L., Zhu, T. and Li, S.M. Identification of the verruculogen prenyltransferase FtmPT3 by a combination of chemical, bioinformatic and biochemical approaches. ChemBioChem. 13 (2012) 2583-2592. [PMID: 23109474]
Accepted name: 2-(3-amino-3-carboxypropyl)histidine synthase
For diagram of reaction click here.
Reaction: S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] = S-methyl-5-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
Other name(s): Dph2
Systematic name: S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase
Comments: A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The enzyme is a member of the ÕAdoMet radicalÕ (radical SAM) family and generates the 3-amino-3-carboxypropyl radical by an uncanonical clevage of S-adenosyl-L-methionine. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Liu, S., Milne, G.T., Kuremsky, J.G., Fink, G.R. and Leppla, S.H. Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol. Cell Biol. 24 (2004) 9487-9497. [PMID: 15485916]
2. Zhang, Y., Zhu, X., Torelli, A.T., Lee, M., Dzikovski, B., Koralewski, R.M., Wang, E., Freed, J., Krebs, C., Ealick, S.E. and Lin, H. Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature 465 (2010) 891-896. [PMID: 20559380]
3. Zhu, X., Dzikovski, B., Su, X., Torelli, A.T., Zhang, Y., Ealick, S.E., Freed, J.H. and Lin, H. Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis. Mol Biosyst 7 (2011) 74-81. [PMID: 20931132]
4. Dong, M., Horitani, M., Dzikovski, B., Pandelia, M.E., Krebs, C., Freed, J.H., Hoffman, B.M. and Lin, H. Organometallic complex formed by an unconventional radical S-adenosylmethionine enzyme. J. Am. Chem. Soc. 138 (2016) 9755Ð9758. [PMID: 27465315]
Accepted name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)
Reaction: prenyl diphosphate + brevianamide F = diphosphate + deoxybrevianamide E
For diagram of reaction click here.
Glossary: brevianamide F = (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
deoxybrevianamide E = (3S,8aS)-3-{[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl}-octahydropyrrolo[1,2-a]piperazine-1,4-dione
Other name(s): NotF; BrePT; brevianamide F reverse prenyltransferase; dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase
Systematic name: dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase
Comments: The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F [1], while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides [2]. Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ding, Y., de Wet, J.R., Cavalcoli, J., Li, S., Greshock, T.J., Miller, K.A., Finefield, J.M., Sunderhaus, J.D., McAfoos, T.J., Tsukamoto, S., Williams, R.M. and Sherman, D.H. Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp. J. Am. Chem. Soc. 132 (2010) 12733-12740. [PMID: 20722388]
2. Yin, S., Yu, X., Wang, Q., Liu, X.Q. and Li, S.M. Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides. Appl. Microbiol. Biotechnol. 97 (2013) 1649-1660. [PMID: 22660767]
EC 2.5.1.110
Accepted name: 12α,13α-dihydroxyfumitremorgin C prenyltransferase
Reaction: dimethylallyl diphosphate + 12α,13α-dihydroxyfumitremorgin C = diphosphate + fumitremorgin B
For diagram of reaction click here.
Glossary: 12α,13α-dihydroxyfumitremorgin = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmH (gene name); FtmPT2
Systematic name: dimethylallyl-diphosphate:12α,13α-dihydroxyfumitremorgin C dimethylallyl-N-1-transferase
Comments: The enzyme from the fungus Aspergillus fumigatus also shows some activity with fumitremorgin C. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Grundmann, A., Kuznetsova, T., Afiyatullov, S.Sh and Li, S.M. FtmPT2, an N-prenyltransferase from Aspergillus fumigatus, catalyses the last step in the biosynthesis of fumitremorgin B. ChemBioChem. 9 (2008) 2059-2063. [PMID: 18683158]
EC 2.5.1.111
Accepted name: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Reaction: prenyl diphosphate + 4-hydroxyphenylpyruvate = diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate
For diagram of reaction, click here
Glossary: 3-dimethylallyl-4-hydroxyphenylpyruvate = 3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]-2-oxopropanoate
Other name(s): CloQ; 4HPP dimethylallyltransferase; NovQ; dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Systematic name: prenyl-diphosphate:4-hydroxyphenylpyruvate 3'-prenyltransferase
Comments: The enzyme is involved in the biosynthesis of the 3-dimethylallyl-4-hydroxyphenylpyruvate moiety of the aminocoumarin antibiotics clorobiocin and novobiocin [1].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Pojer, F., Wemakor, E., Kammerer, B., Chen, H., Walsh, C.T., Li, S.M. and Heide, L. CloQ, a prenyltransferase involved in clorobiocin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 2316-2321. [PMID: 12618544]
2. Keller, S., Pojer, F., Heide, L. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1153-1155. [PMID: 17077503]
3. Metzger, U., Keller, S., Stevenson, C.E., Heide, L. and Lawson, D.M. Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J. Mol. Biol. 404 (2010) 611-626. [PMID: 20946900]
4. Ozaki, T., Mishima, S., Nishiyama, M. and Kuzuyama, T. NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids. J. Antibiot. (Tokyo) 62 (2009) 385-392. [PMID: 19557032]
EC 2.5.1.112
Accepted name: adenylate dimethylallyltransferase (ADP/ATP-dependent)
Reaction: (1) dimethylallyl diphosphate + ADP = diphosphate + N6-(dimethylallyl)adenosine 5′-diphosphate
For diagram of reaction, click here
Other name(s): cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:ADP/ATP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); dimethylallyl diphosphate:ATP/ADP isopentenyltransferase: IPT
Systematic name: dimethylallyl-diphosphate:ADP/ATP dimethylallyltransferase
Comments: Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP [1]. Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus [3], also have a lower activity with AMP [cf. EC 2.5.1.27, adenylate dimethylallyltransferase (AMP-dependent)].
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Kakimoto, T. Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate:ATP/ADP isopentenyltransferases. Plant Cell Physiol 42 (2001) 677-685. [PMID: 11479373]
2. Takei, K., Sakakibara, H. and Sugiyama, T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 26405-26410. [PMID: 11313355]
3. Sakano, Y., Okada, Y., Matsunaga, A., Suwama, T., Kaneko, T., Ito, K., Noguchi, H. and Abe, I. Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.). Phytochemistry 65 (2004) 2439-2446. [PMID: 15381407]
EC 2.5.1.113
Accepted name: [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase
Reaction: O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH = [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
Other name(s): CysM
Systematic name: O-phospho-L-serine:thiocarboxylated [CysO sulfur-carrier protein] 2-amino-2-carboxyethyltransferase
Comments: A pyridoxal-phosphate protein. The enzyme participates in an alternative pathway for L-cysteine biosynthesis that involves a protein-bound thiocarboxylate as the sulfide donor. The enzyme from the bacterium Mycobacterium tuberculosis also has very low activity with O3-acetyl-L-serine (cf. EC 2.5.1.65, O-phosphoserine sulfhydrylase).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. O'Leary, S.E., Jurgenson, C.T., Ealick, S.E. and Begley, T.P. O-Phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis. Biochemistry 47 (2008) 11606-11615. [PMID: 18842002]
2. Jurgenson, C.T., Burns, K.E., Begley, T.P. and Ealick, S.E. Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis. Biochemistry 47 (2008) 10354-10364. [PMID: 18771296]
3. Ågren, D., Schnell, R., Oehlmann, W., Singh, M. and Schneider, G. Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J. Biol. Chem. 283 (2008) 31567-31574. [PMID: 18799456]
4. Ågren, D., Schnell, R. and Schneider, G. The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity. FEBS Lett 583 (2009) 330-336. [PMID: 19101553]
EC 2.5.1.114
Accepted name: tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase
Reaction: S-adenosyl-L-methionine + 4-demethylwyosine37 in tRNAPhe = S-methyl-5′-thioadenosine + 7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine37 in tRNAPhe
For diagram of reaction, click here
Glossary: 4-demethylwyosine = imG-14 = 6-methyl-3-(β-D-ribofuranosyl)-3,5-dihydro-9H-imidazo[1,2-a]purin-9-one
Other name(s): TYW2; tRNA-yW synthesizing enzyme-2; TRM12 (gene name); taw2 (gene name)
Systematic name: S-adenosyl-L-methionine:tRNAPhe (4-demethylwyosine37-C7)-[(3S)-3-amino-3-carboxypropyl]transferase
Comments: The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Umitsu, M., Nishimasu, H., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2. Proc. Natl. Acad. Sci. USA 106 (2009) 15616-15621. [PMID: 19717466]
2. Rodriguez, V., Vasudevan, S., Noma, A., Carlson, B.A., Green, J.E., Suzuki, T. and Chandrasekharappa, S.C. Structure-function analysis of human TYW2 enzyme required for the biosynthesis of a highly modified Wybutosine (yW) base in phenylalanine-tRNA. PLoS One 7 (2012) e39297. [PMID: 22761755]
3. de Crecy-Lagard, V., Brochier-Armanet, C., Urbonavicius, J., Fernandez, B., Phillips, G., Lyons, B., Noma, A., Alvarez, S., Droogmans, L., Armengaud, J. and Grosjean, H. Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea. Mol Biol Evol 27 (2010) 2062-2077. [PMID: 20382657]
EC 2.5.1.115
Accepted name: homogentisate phytyltransferase
Reaction: phytyl diphosphate + homogentisate = diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
For diagram of reaction click here.
Glossary: 2-methyl-6-phytylbenzene-1,4-diol = MPBQ
Other name(s): HPT; VTE2 (gene name)
Systematic name: phytyl-diphosphate:homogentisate phytyltransferase
Comments: Requires Mg2+ for activity [3]. Involved in the biosynthesis of the vitamin E tocopherols. While the enzyme from the cyanobacterium Synechocystis PCC 6803 has an appreciable activity with geranylgeranyl diphosphate (EC 2.5.1.116, homogentisate geranylgeranyltransferase), the enzyme from the plant Arabidopsis thaliana has only a low activity with that substrate [1,3,4].
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References:
1. Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113-1124. [PMID: 11706191]
2. Savidge, B., Weiss, J.D., Wong, Y.H., Lassner, M.W., Mitsky, T.A., Shewmaker, C.K., Post-Beittenmiller, D. and Valentin, H.E. Isolation and characterization of homogentisate phytyltransferase genes from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 129 (2002) 321-332. [PMID: 12011362]
3. Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett 580 (2006) 5357-5362. [PMID: 16989822]
4. Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206-217. [PMID: 21223386]
EC 2.5.1.116
Accepted name: homogentisate geranylgeranyltransferase
Reaction: geranylgeranyl diphosphate + homogentisate = diphosphate + 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2
For diagram of reaction click here.
Glossary: 6-geranylgeranyl-2-methylbenzene-1,4-diol = MGGBQ
Other name(s): HGGT; slr1736 (gene name)
Systematic name: geranylgeranyl-diphosphate:homogentisate geranylgeranyltransferase
Comments: Requires Mg2+ for activity. Involved in the biosynthesis of the vitamin E, tocotrienols. While the enzyme from the bacterium Synechocystis PCC 6803 has higher activity with phytyl diphosphate (EC 2.5.1.115, homogentisate phytyltransferase), the enzymes from barley, rice and wheat have only a low activity with that substrate [2].
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References:
1. Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113-1124. [PMID: 11706191]
2. Cahoon, E.B., Hall, S.E., Ripp, K.G., Ganzke, T.S., Hitz, W.D. and Coughlan, S.J. Metabolic redesign of vitamin E biosynthesis in plants for tocotrienol production and increased antioxidant content. Nat. Biotechnol. 21 (2003) 1082-1087. [PMID: 12897790]
3. Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206-217. [PMID: 21223386]
EC 2.5.1.117
Accepted name: homogentisate solanesyltransferase
Reaction: all-trans-nonaprenyl diphosphate + homogentisate = diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2
For diagram of reaction click here.
Glossary: 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol = 2-methyl-6-solanesylbenzene-1,4-diol = MSBQ
Other name(s): HST; PDS2 (gene name)
Systematic name: all-trans-nonaprenyl-diphosphate:homogentisate nonaprenyltransferase
Comments: Requires Mg2+ for activity. Part of the biosynthesis pathway of plastoquinol-9. The enzymes purified from the plant Arabidopsis thaliana and the alga Chlamydomonas reinhardtii are also active in vitro with unsaturated C10 to C20 prenyl diphosphates, producing main products that are not decarboxylated [2].
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References:
1. Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett 580 (2006) 5357-5362. [PMID: 16989822]
2. Sadre, R., Frentzen, M., Saeed, M. and Hawkes, T. Catalytic reactions of the homogentisate prenyl transferase involved in plastoquinone-9 biosynthesis. J. Biol. Chem. 285 (2010) 18191-18198. [PMID: 20400515]
EC 2.5.1.118
Accepted name: β-(isoxazolin-5-on-2-yl)-L-alanine synthase
Reaction: O3-acetyl-L-serine + isoxazolin-5-one = 3-(5-oxoisoxazolin-2-yl)-L-alanine + acetate
For diagram of reaction click here.
Systematic name: O3-acetyl-L-serine:isoxazolin-5-one 2-(2-amino-2-carboxyethyl)transferase
Comments: The enzyme from the plants Lathyrus odoratus (sweet pea) and L. sativus (grass pea) also forms 3-(5-oxoisoxazolin-4-yl)-L-alanine in vitro (cf. EC 2.5.1.119). However, only 3-(5-oxoisoxazolin-2-yl)-L-alanine is formed in vivo. 3-(5-oxoisoxazolin-2-yl)-L-alanine is the biosynthetic precursor of the neurotoxin N3-oxalyl-L-2,3-diaminopropanoic acid, the cause of lathyrism. Closely related and possibly identical to EC 2.5.1.47, cysteine synthase, and EC 2.5.1.51, β-pyrazolylalanine synthase.
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References:
1. Ikegami, F., Kamiya, M., Kuo, Y.H., Lambein, F. and Murakoshi, I. Enzymatic synthesis of two isoxazolylalanine isomers by cysteine synthases in Lathyrus species. Biol. Pharm. Bull. 19 (1996) 1214-1215. [PMID: 8889043]
EC 2.5.1.119
Accepted name: β-(isoxazolin-5-on-4-yl)-L-alanine synthase
Reaction: O3-acetyl-L-serine + isoxazolin-5-one = 3-(5-oxoisoxazolin-4-yl)-L-alanine + acetate
For diagram of reaction click here.
Systematic name: O3-acetyl-L-serine:isoxazolin-5-one 4-(2-amino-2-carboxyethyl)transferase
Comments: 3-(5-Oxoisoxazolin-4-yl)-L-alanine is an antifungal antibiotic produced by the bacterium Streptomyces platensis. The enzymes from the plants Lathyrus odoratus (sweet pea) , L. sativus (grass pea) and Citrullus vulgaris (watermelon) that catalyse EC 2.5.1.118 (β-(isoxazolin-5-on-2-yl)-L-alanine synthase) also catalyse this reaction in vitro, but not in vivo. Closely related and possibly identical to EC 2.5.1.47, cysteine synthase, and EC 2.5.1.51, β-pyrazolylalanine synthase.
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References:
1. Ikegami, F., Kamiya, M., Kuo, Y.H., Lambein, F. and Murakoshi, I. Enzymatic synthesis of two isoxazolylalanine isomers by cysteine synthases in Lathyrus species. Biol. Pharm. Bull. 19 (1996) 1214-1215. [PMID: 8889043]
EC 2.5.1.120
Accepted name: aminodeoxyfutalosine synthase
Reaction: S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O = 6-amino-6-deoxyfutalosine + L-methionine + HCO3-
For diagram of reaction click here.
Glossary: 6-amino-6-deoxyfutalosine = 3-{3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
Other name(s): MqnE; AFL synthase; aminofutalosine synthase
Systematic name: S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (HCO3--hydrolysing, 6-amino-6-deoxyfutalosine-forming)
Comments: This enzyme is a member of the ’AdoMet radical’ (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the transferred adenosyl group. The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
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References:
1. Mahanta, N., Fedoseyenko, D., Dairi, T. and Begley, T.P. Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme. J. Am. Chem. Soc. 135 (2013) 15318-15321. [PMID: 24083939]
EC 2.5.1.121
Accepted name: 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
Reaction: prenyl diphosphate + 5,10-dihydrophenazine-1-carboxylate = diphosphate + 9-prenyl-5,10-dihydrophenazine-1-carboxylate
Glossary: 9-prenyl-5,10-dihydrophenazine-1-carboxylate = 9-(3-methylbut-2-en-1-yl)-5,10-dihydrophenazine-1-carboxylate
Other name(s): PpzP; dihydrophenazine-1-carboxylate dimethylallyltransferase; 5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase; dimethylallyl diphosphate:5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
Systematic name: prenyl-diphosphate:5,10-dihydrophenazine-1-carboxylate 9-prenyltransferase
Comments: The enzyme is involved in the biosynthesis of prenylated phenazines by the bacterium Streptomyces anulatus. It is specific for both prenyl diphosphate and 5,10-dihydrophenazine-1-carboxylate.
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References:
1. Saleh, O., Gust, B., Boll, B., Fiedler, H.P. and Heide, L. Aromatic prenylation in phenazine biosynthesis: dihydrophenazine-1-carboxylate dimethylallyltransferase from Streptomyces anulatus. J. Biol. Chem. 284 (2009) 14439-14447. [PMID: 19339241]
EC 2.5.1.122
Accepted name: 4-O-dimethylallyl-L-tyrosine synthase
Reaction: prenyl diphosphate + L-tyrosine = diphosphate + 4-O-prenyl-L-tyrosine
Other name(s): SirD; dimethylallyl diphosphate:L-tyrosine 4-O-dimethylallyltransferase
Systematic name: prenyl-diphosphate:L-tyrosine 4-O-prenyltransferase
Comments: The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.
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References:
1. Kremer, A. and Li, S.M. A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL. Microbiology 156 (2010) 278-286. [PMID: 19762440]
2. Zou, H.X., Xie, X., Zheng, X.D. and Li, S.M. The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations. Appl. Microbiol. Biotechnol. 89 (2011) 1443-1451. [PMID: 21038099]
EC 2.5.1.123
Accepted name: flaviolin linalyltransferase
Reaction: geranyl diphosphate + flaviolin = 3-linalylflaviolin + diphosphate
For diagram of reaction click here.
Glossary: flaviolin = 2,5,7-trihydroxynaphthalene-1,4-dione
Other name(s): Fnq26
Systematic name: geranyl-diphosphate:flaviolin 3-linalyltransferase
Comments: Does not require Mg2+ or any other metal ions. Isolated from the bacterium Streptomyces cinnamonensis. In vitro the enzyme also forms traces of 3-geranylflaviolin.
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References:
1. Haagen, Y., Unsold, I., Westrich, L., Gust, B., Richard, S.B., Noel, J.P. and Heide, L. A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates. FEBS Lett 581 (2007) 2889-2893. [PMID: 17543953]
EC 2.5.1.124
Accepted name: 6-linalyl-2-O,3-dimethylflaviolin synthase
Reaction: geranyl diphosphate + 2-O,3-dimethylflaviolin = diphosphate + 6-linalyl-2-O,3-dimethylflaviolin
Glossary: flaviolin = 2,5,7-trihydroxy-1,4-naphthoquinone
Other name(s): Fur7; 6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase
Systematic name: geranyl-diphosphate:2-O-methyl-3-methylflaviolin geranyltransferase (6-linalyl-2-O,3-dimethylflaviolin-forming)
Comments: The enzyme is involved in biosynthesis of the polyketide-isoprenoid furaquinocin D in the bacterium Streptomyces sp. KO-3988. It catalyses the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 6-linalyl-2-O,3-dimethylflaviolin and 7-O-geranyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.125, 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase) in a 10:1 ratio.
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References:
1. Kumano, T., Tomita, T., Nishiyama, M. and Kuzuyama, T. Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. J. Biol. Chem. 285 (2010) 39663-39671. [PMID: 20937800]
EC 2.5.1.125
Accepted name: 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase
Reaction: geranyl diphosphate + 2-O,3-dimethylflaviolin = diphosphate + 7-O-geranyl-2-O,3-dimethylflaviolin
Glossary: flaviolin = 2,5,7-trihydroxy-1,4-naphthoquinone
Other name(s): Fur7
Systematic name: geranyl-diphosphate:2-O,3-dimethylflaviolin geranyltransferase (7-O-geranyl-2-O,3-dimethylflaviolin-forming)
Comments: The enzyme is involved in furaquinocin biosynthesis in the bacterium Streptomyces sp. KO-3988. It catalyses the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 7-O-geranyl-2-O,3-dimethylflaviolin and 6-linalyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.124, 6-linalyl-2-O,3-dimethylflaviolin synthase) in a 1:10 ratio.
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References:
1. Kumano, T., Tomita, T., Nishiyama, M. and Kuzuyama, T. Functional characterization of the promiscuous prenyltransferase responsible for furaquinocin biosynthesis: identification of a physiological polyketide substrate and its prenylated reaction products. J. Biol. Chem. 285 (2010) 39663-39671. [PMID: 20937800]
EC 2.5.1.126
Accepted name: norspermine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine
Glossary: norspermidine = bis(3-aminopropyl)amine
Other name(s): long-chain polyamine synthase (ambiguous); S-adenosyl 3-(methylthio)propylamine:norspermidine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:norspermidine 3-aminopropyltransferase
Comments: The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate.
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References:
1. Knott, J.M. Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum. FEBS Lett 583 (2009) 3519-3524. [PMID: 19822146]
EC 2.5.1.127
Accepted name: caldopentamine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + norspermine = S-methyl-5'-thioadenosine + caldopentamine
Glossary: caldopentamine = N-(3-aminopropyl)-N'-{3-[(3-aminopropyl)amino]propyl}-1,3-propanediamine
Other name(s): long-chain polyamine synthase (ambiguous); S-adenosyl 3-(methylthio)propylamine:norspermine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:norspermine 3-aminopropyltransferase
Comments: The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine.
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1. Knott, J.M. Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum. FEBS Lett 583 (2009) 3519-3524. [PMID: 19822146]
EC 2.5.1.128
Reaction: 2 S-adenosyl 3-(methylsulfaynyl)propylamine + spermidine = 2 S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine (overall reaction)
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase [N4-bis(aminopropyl)spermidine synthesizing]
Comments: The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N4-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature. When spermine is used as substrate, the enzyme forms N4-aminopropylspermine.
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References:
1. Okada, K., Hidese, R., Fukuda, W., Niitsu, M., Takao, K., Horai, Y., Umezawa, N., Higuchi, T., Oshima, T., Yoshikawa, Y., Imanaka, T. and Fujiwara, S. Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles. J. Bacteriol. 196 (2014) 1866-1876. [PMID: 24610711]
EC 2.5.1.129
Accepted name: flavin prenyltransferase
Reaction: prenyl phosphate + FMNH2 = prenylated FMNH2 + phosphate
For diagram of reaction click here.
Glossary: prenylated FMNH2 = 3,3,4,5-tetramethyl-7-[(2S,3S,4R)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]-2,3-dihydro-1H,7H-naphtho[1,8-fg]pteridine-9,11(8H,10H)-dione
Other name(s): ubiX (gene name); PAD1 (gene name); dimethylallyl-phosphate:FMNH2 prenyltransferase
Systematic name: prenyl-phosphate:FMNH2 prenyltransferase
Comments: The enzyme produces the modified flavin cofactor prenylated FMNH2, which is required by EC 4.1.1.98, 4-hydroxy-3-polyprenylbenzoate decarboxylase, and EC 4.1.1.102, phenacrylate decarboxylase. The enzyme acts as a flavin prenyltransferase, linking a prenyl moiety to the flavin N-5 and C-6 atoms and thus adding a fourth non-aromatic ring to the flavin isoalloxazine group.
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1. White, M.D., Payne, K.A., Fisher, K., Marshall, S.A., Parker, D., Rattray, N.J., Trivedi, D.K., Goodacre, R., Rigby, S.E., Scrutton, N.S., Hay, S. and Leys, D. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature 522 (2015) 502-506. [PMID: 26083743]
EC 2.5.1.130
Accepted name: 2-carboxy-1,4-naphthoquinone phytyltransferase
Reaction: phytyl diphosphate + 2-carboxy-1,4-naphthoquinone = demethylphylloquinone + diphosphate + CO2
For diagram of reaction click here.
Glossary: 2-carboxy-1,4-naphthoquinone = 1,4-dioxo-2-naphthoic acid
Other name(s): menA (gene name); ABC4 (gene name); 1,4-dioxo-2-naphthoate phytyltransferase; 1,4-diketo-2-naphthoate phytyltransferase
Systematic name: phytyl-diphosphate:2-carboxy-1,4-naphthoquinone phytyltransferase
Comments: This enzyme, found in plants and cyanobacteria, catalyses a step in the synthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme catalyses the transfer of the phytyl chain synthesized by EC 1.3.1.83, geranylgeranyl diphosphate reductase, to 2-carboxy-1,4-naphthoquinone.
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References:
1. Johnson, T.W., Shen, G., Zybailov, B., Kolling, D., Reategui, R., Beauparlant, S., Vassiliev, I.R., Bryant, D.A., Jones, A.D., Golbeck, J.H. and Chitnis, P.R. Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275 (2000) 8523-8530. [PMID: 10722690]
2. Shimada, H., Ohno, R., Shibata, M., Ikegami, I., Onai, K., Ohto, M.A. and Takamiya, K. Inactivation and deficiency of core proteins of photosystems I and II caused by genetical phylloquinone and plastoquinone deficiency but retained lamellar structure in a T-DNA mutant of Arabidopsis. Plant J. 41 (2005) 627-637. [PMID: 15686525]
EC 2.5.1.131
Accepted name: (4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase
Reaction: [5-(aminomethyl)furan-3-yl]methyl diphosphate + γ-L-glutamyltyramine = (4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine + diphosphate
For diagram of reaction click here.
Other name(s): MfnF
Systematic name: [5-(aminomethyl)furan-3-yl]methyl-diphosphate:γ-L-glutamyltyramine [5-(aminomethyl)furan-3-yl]methyltransferase
Comments: The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.
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1. Wang, Y., Xu, H., Jones, M.K. and White, R.H. Identification of the final two genes functioning in methanofuran biosynthesis in Methanocaldococcus jannaschii. J. Bacteriol. 197 (2015) 2850-2858. [PMID: 26100040]
EC 2.5.1.132
Accepted name: 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase
Reaction: phosphoenolpyruvate + D-mannose 6-phosphate + H2O = 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate 9-phosphate + phosphate
Glossary: phosphoenolpyruvate = 2-(phosphooxy)prop-2-enoate
Other name(s): 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase; Kdn 9-P synthase
Systematic name: phosphoenolpyruvate:D-mannose-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase
Comments: The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (Kdn). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
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1. Angata, T., Nakata, D., Matsuda, T., Kitajima, K. and Troy, F.A., 2nd. Biosynthesis of KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid). Identification and characterization of a KDN-9-phosphate synthetase activity from trout testis. J. Biol. Chem. 274 (1999) 22949-22956. [PMID: 10438460]
2. Lawrence, S.M., Huddleston, K.A., Pitts, L.R., Nguyen, N., Lee, Y.C., Vann, W.F., Coleman, T.A. and Betenbaugh, M.J. Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability. J. Biol. Chem. 275 (2000) 17869-17877. [PMID: 10749855]
3. Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893-897. [PMID: 18804026]
EC 2.5.1.133
Accepted name: bacteriochlorophyll a synthase
Reaction: geranylgeranyl diphosphate + bacteriochlorophyllide a = geranylgeranyl-bacteriochlorophyllide a + diphosphate
For diagram of reaction click here.
Other name(s): bchG (gene name)
Systematic name: geranylgeranyl-diphosphate:bacteriochlorophyllide-a geranylgeranytransferase
Comments: The enzyme catalyses the addition of a geranylgeranyl hydrophobic chain to bacteriochlorophyllide a via an ester bond with the 17-propionate residue. The side chain is later modified to a phytyl chain, resulting in bacteriochlorophyll a.
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References:
1. Oster, U., Bauer, C.E. and Rüdiger, W. Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli. J. Biol. Chem. 272 (1997) 9671-9676. [PMID: 9092496]
2. Addlesee, H.A., Fiedor, L. and Hunter, C.N. Physical mapping of bchG, orf427, and orf177 in the photosynthesis gene cluster of Rhodobacter sphaeroides: functional assignment of the bacteriochlorophyll synthetase gene. J. Bacteriol. 182 (2000) 3175-3182. [PMID: 10809697]
3. Garcia-Gil, L.J., Gich, F.B. and Fuentes-Garcia, X. A comparative study of bchG from green photosynthetic bacteria. Arch. Microbiol. 179 (2003) 108-115. [PMID: 12560989]
4. Saga, Y., Hirota, K., Harada, J. and Tamiaki, H. In vitro enzymatic activities of bacteriochlorophyll a synthase derived from the green sulfur photosynthetic bacterium Chlorobaculum tepidum. Biochemistry 54 (2015) 4998-5005. [PMID: 26258685]
EC 2.5.1.134
Accepted name: cystathionine β-synthase (O-acetyl-L-serine)
Reaction: O-acetyl-L-serine + L-homocysteine = L-cystathionine + acetate
For diagram of reaction click here.
Other name(s): MccB; O-acetylserine dependent cystathionine β-synthase
Systematic name: O-acetyl-L-serine:L-homocysteine 2-amino-2-carboxyethyltransferase
Comments: A pyridoxal 5'-phosphate protein. The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22, cystathionine β-synthase).
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References:
1. Hullo, M.F., Auger, S., Soutourina, O., Barzu, O., Yvon, M., Danchin, A. and Martin-Verstraete, I. Conversion of methionine to cysteine in Bacillus subtilis and its regulation. J. Bacteriol. 189 (2007) 187-197. [PMID: 17056751]
EC 2.5.1.135
Accepted name: validamine 7-phosphate valienyltransferase
Reaction: GDP-valienol + validamine 7-phosphate = validoxylamine A 7'-phosphate + GDP
For diagram of reaction click here
Glossary: valienol = (1S,2S,3S,4R)-5-(hydroxymethyl)cyclohex-5-ene-1,2,3,4-tetrol
Other name(s): vldE (gene name); valL (gene name)
Systematic name: GDP-valienol:validamine 7-phosphate valienyltransferase
Comments: The enzyme, characterized from several Streptomyces strains, is involved in the biosynthesis of the antifungal agent validamycin A.
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References:
1. Asamizu, S., Yang, J., Almabruk, K.H. and Mahmud, T. Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis. J. Am. Chem. Soc. 133 (2011) 12124-12135. [PMID: 21766819]
2. Zheng, L., Zhou, X., Zhang, H., Ji, X., Li, L., Huang, L., Bai, L. and Zhang, H. Structural and functional analysis of validoxylamine A 7'-phosphate synthase ValL involved in validamycin A biosynthesis. PLoS One 7 (2012) e32033. [PMID: 22384130]
3. Cavalier, M.C., Yim, Y.S., Asamizu, S., Neau, D., Almabruk, K.H., Mahmud, T. and Lee, Y.H. Mechanistic insights into validoxylamine A 7'-phosphate synthesis by VldE using the structure of the entire product complex. PLoS One 7 (2012) e44934. [PMID: 23028689]
EC 2.5.1.136
Accepted name: 2-acylphloroglucinol 4-prenyltransferase
Reaction: prenyl diphosphate + a 2-acylphloroglucinol = diphosphate + a 2-acyl-4-prenylphloroglucinol
For diagram of reaction click here or click here.
Glossary: naringenin chalcone = 2',4,4',6'-tetrahydroxychalcone = 3-(4-hydroxyphemyl)-1-(2,4,6-trihydroxyphenyl)prop-2-en-1-one
Other name(s): PT-1 (gene name); PT1L (gene name); aromatic prenyltransferase (ambiguous); dimethylallyl-diphosphate:2-acylphloroglucinol 4-dimethylallyltransferase
Systematic name: prenyl-diphosphate:2-acylphloroglucinol 4-prenyltransferase
Comments: The enzyme, characterized from hop (Humulus lupulus), acts on phlorisovalerophenone, phlormethylbutanophenone, and phlorisobutanophenone during the synthesis of bitter acids. It also acts with much lower activity on naringenin chalcone. Forms a complex with EC 2.5.1.137, 2-acyl-4-prenylphloroglucinol 6-prenyltransferase, which catalyses additional prenylation reactions. Requires Mg2+.
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References:
1. Tsurumaru, Y., Sasaki, K., Miyawaki, T., Uto, Y., Momma, T., Umemoto, N., Momose, M. and Yazaki, K. HlPT-1, a membrane-bound prenyltransferase responsible for the biosynthesis of bitter acids in hops. Biochem. Biophys. Res. Commun. 417 (2012) 393-398. [PMID: 22166201]
2. Li, H., Ban, Z., Qin, H., Ma, L., King, A.J. and Wang, G. A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway. Plant Physiol. 167 (2015) 650-659. [PMID: 25564559]
EC 2.5.1.137
Accepted name: 2-acyl-4-prenylphloroglucinol 6-prenyltransferase
Reaction: (1) prenyl diphosphate + a 2-acyl-4-prenylphloroglucinol = diphosphate + a 2-acyl-4,6-bis(prenyl)phloroglucinol
For diagram of reaction click here.
Glossary: a 2-acyl-4,6,6-tris(prenyl)phloroglucinol = a β bitter acid
Other name(s): PT2 (gene name); aromatic prenyltransferase (ambiguous); dimethylallyl-diphosphate:2-acyl-4-prenylphloroglucinol 6-dimethylallyltransferase
Systematic name: prenyl-diphosphate:2-acyl-4-prenylphloroglucinol 6-dimethylallyltransferase
Comments: The enzyme, characterized from hop (Humulus lupulus), catalyses two successive prenylations of a 2-acyl-4-prenylphloroglucinol during the synthesis of bitter acids. Forms a complex with EC 2.5.1.136, 2-acylphloroglucinol 4-prenyltransferase, which catalyses the initial prenylation of the substrates. Requires Mg2+.
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References:
1. Li, H., Ban, Z., Qin, H., Ma, L., King, A.J. and Wang, G. A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway. Plant Physiol. 167 (2015) 650-659. [PMID: 25564559]
EC 2.5.1.138
Accepted name: coumarin 8-geranyltransferase
Reaction: (1) geranyl diphosphate + umbelliferone = diphosphate + 8-geranylumbelliferone
Glossary: geranyl diphosphate = (2E)-3,7-dimethylocta-2,6-dien-1-yl diphosphate
Other name(s): ClPT1
Systematic name: geranyl-diphosphate:umbelliferone 8-geranyltransferase
Comments: The enzyme, characterized from the plant Citrus limon, is specific for geranyl diphosphate as a prenyl donor. It also has low activity with the coumarins 5,7-dihydroxycoumarin and 5-methoxy-7-hydroxycoumarin.
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References:
1. Munakata, R., Inoue, T., Koeduka, T., Karamat, F., Olry, A., Sugiyama, A., Takanashi, K., Dugrand, A., Froelicher, Y., Tanaka, R., Uto, Y., Hori, H., Azuma, J., Hehn, A., Bourgaud, F. and Yazaki, K. Molecular cloning and characterization of a geranyl diphosphate-specific aromatic prenyltransferase from lemon. Plant Physiol. 166 (2014) 80-90. [PMID: 25077796]
EC 2.5.1.139
Accepted name: umbelliferone 6-dimethylallyltransferase
Reaction: prenyl diphosphate + umbelliferone = diphosphate + demethylsuberosin
For diagram of reaction click here.
Glossary: demethylsuberosin = 7-hydroxy-6-prenyl-1-benzopyran-2-one
Other name(s): PcPT; dimethylallyl-diphosphate:umbelliferone 6-dimethylallyltransferase
Systematic name: prenyl-diphosphate:umbelliferone 6-dimethylallyltransferase
Comments: The enzyme from parsley (Petroselinum crispum) is specific for umbelliferone and prenyl diphosphate. A minor product is osthenol, which is produced by transfer of the dimethylallyl group to C-8 of umbelliferone.
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References:
1. Hamerski, D., Schmitt, D. and Matern, U. Induction of two prenyltransferases for the accumulation of coumarin phytoalexins in elicitor-treated Ammi majus cell suspension cultures. Phytochemistry 29 (1990) 1131-1135. [PMID: 1366425]
2. Karamat, F., Olry, A., Munakata, R., Koeduka, T., Sugiyama, A., Paris, C., Hehn, A., Bourgaud, F. and Yazaki, K. A coumarin-specific prenyltransferase catalyzes the crucial biosynthetic reaction for furanocoumarin formation in parsley. Plant J. 77 (2014) 627-638. [PMID: 24354545]
EC 2.5.1.140
Accepted name: N-(2-amino-2-carboxyethyl)-L-glutamate synthase
Reaction: O-phospho-L-serine + L-glutamate = N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
Other name(s): SbnA; ACEGA synthase
Systematic name: O-phospho-L-serine:L-glutamate N-(2S)-2-amino-2-carboxyethyltransferase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
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References:
1. Beasley, F.C., Cheung, J. and Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 11 (2011) 199. [PMID: 21906287]
2. Kobylarz, M.J., Grigg, J.C., Takayama, S.J., Rai, D.K., Heinrichs, D.E. and Murphy, M.E. Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. Chem. Biol. 21 (2014) 379-388. [PMID: 24485762]
EC 2.5.1.141
Accepted name: heme o synthase
Reaction: (2E,6E)-farnesyl diphosphate + protoheme IX + H2O = diphosphate + ferroheme o
For diagram of reaction click here
Other name(s): ctaB (gene name); COX10 (gene name)
Systematic name: (2E,6E)-farnesyl-diphosphate:protoheme IX farnesyltranstransferase
Comments: The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group
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References:
1. Saiki, K., Mogi, T. and Anraku, Y. Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase. Biochem. Biophys. Res. Commun. 189 (1992) 1491-1497. [PMID: 1336371]
2. Svensson, B., Lubben, M. and Hederstedt, L. Bacillus subtilis CtaA and CtaB function in haem A biosynthesis. Mol. Microbiol. 10 (1993) 193-201. [PMID: 7968515]
3. Glerum, D.M. and Tzagoloff, A. Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant. Proc. Natl. Acad. Sci. USA 91 (1994) 8452-8456. [PMID: 8078902]
4. Lubben, M. and Morand, K. Novel prenylated hemes as cofactors of cytochrome oxidases. Archaea have modified hemes A and O. J. Biol. Chem 269 (1994) 21473-21479. [PMID: 8063781]
5. Brown, B.M., Wang, Z., Brown, K.R., Cricco, J.A. and Hegg, E.L. Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli. Biochemistry 43 (2004) 13541-13548. [PMID: 15491161]
6. Mogi, T. Over-expression and characterization of Bacillus subtilis heme O synthase. J. Biochem. 145 (2009) 669-675. [PMID: 19204012]
EC 2.5.1.142
Accepted name: nerylneryl diphosphate synthase
Reaction: prenyl diphosphate + 3 (3-methylbut-3-en-1-yl diphosphate) = 3 diphosphate + nerylneryl diphosphate
For diagram of reaction click here
Glossary: nerylneryl diphosphate = all-cis-tetraprenyl diphosphate
Other name(s): CPT2; dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 3 isopentenyl units)
Systematic name: prenyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate cistransferase (adding 3 units of 3-methylbut-3-en-1-yl)
Comments: Isolated from the plant Solanum lycopersicum (tomato).
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References:
1. Akhtar, T.A., Matsuba, Y., Schauvinhold, I., Yu, G., Lees, H.A., Klein, S.E. and Pichersky, E. The tomato cis-prenyltransferase gene family. Plant J. 73 (2013) 640-652. [PMID: 23134568]
2. Matsuba, Y., Zi, J., Jones, A.D., Peters, R.J. and Pichersky, E. Biosynthesis of the diterpenoid lycosantalonol via nerylneryl diphosphate in Solanum lycopersicum. PLoS One 10 (2015) e0119302. [PMID: 25786135]
EC 2.5.1.143
Accepted name: pyridinium-3,5-biscarboxylic acid mononucleotide synthase
Reaction: deamido-NAD+ + hydrogencarbonate = AMP + pyridinium-3,5-biscarboxylate mononucleotide
Other name(s): LarB; P2CMN synthase; nicotinic acid adenine dinucleotide carboxylase/hydrolase; NaAD carboxylase/hydrolase
Systematic name: deamido-NAD+:hydrogencarbonate nicotinate-β-D-ribonucleotidyltransferase
Comments: This enzyme, found in the bacterium Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. It carboxylates the pyridinium ring of deamido-NAD+ and cleaves the phosphoanhydride bond to release AMP and generate pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN).
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References:
1. Desguin, B., Soumillion, P., Hols, P. and Hausinger, R.P. Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion. Proc. Natl Acad. Sci. USA 113 (2016) 5598-5603. [PMID: 27114550]
EC 2.5.1.144
Accepted name: S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent)
Reaction: O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate
For diagram of reaction click here.
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): cysteine synthase B; cysM (gene name); CS26 (gene name)
Systematic name: O-acetyl-L-serine:thiosulfate 2-amino-2-carboxyethyltransferase
Comments: In plants, the activity is catalysed by a chloroplastic enzyme that plays an important role in chloroplast function and is essential for light-dependent redox regulation within the chloroplast. The bacterial enzyme also catalyses the activity of EC 2.5.1.47, cysteine synthase. cf. EC 2.8.5.1, S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent).
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References:
1. Hensel, G. and Truper, H.G. O-Acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Rhodospirillum tenue. Arch. Microbiol. 134 (1983) 227-232. [PMID: 6615127]
2. Nakamura, T., Iwahashi, H. and Eguchi, Y. Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium. J. Bacteriol. 158 (1984) 1122-1127. [PMID: 6373737]
3. Bermudez, M.A., Paez-Ochoa, M.A., Gotor, C. and Romero, L.C. Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control. Plant Cell 22 (2010) 403-416. [PMID: 20179139]
4. Bermudez, M.A., Galmes, J., Moreno, I., Mullineaux, P.M., Gotor, C. and Romero, L.C. Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen. Plant Physiol. 160 (2012) 274-288. [PMID: 22829322]
5. Gotor, C. and Romero, L.C. S-Sulfocysteine synthase function in sensing chloroplast redox status. Plant Signal Behav 8 (2013) e23313. [PMID: 23333972]
EC 2.5.1.145
Accepted name: phosphatidylglycerol—prolipoprotein diacylglyceryl transferase
Reaction: L-1-phosphatidyl-sn-glycerol + a [prolipoprotein]-L-cysteine = sn-glycerol 1-phosphate + an [prolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
Other name(s): lgt (gene name)
Systematic name: L-1-phosphatidyl-sn-glycerol:[prolipoprotein]-L-cysteine diacyl-sn-glyceryltransferase
Comments: This bacterial enzyme, which is associated with the membrane, catalyses the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins.
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References:
1. Sankaran, K. and Wu, H.C. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269 (1994) 19701-19706. [PMID: 8051048]
2. Qi, H.Y., Sankaran, K., Gan, K. and Wu, H.C. Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. J. Bacteriol. 177 (1995) 6820-6824. [PMID: 7592473]
3. Gan, K., Sankaran, K., Williams, M.G., Aldea, M., Rudd, K.E., Kushner, S.R. and Wu, H.C. The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. J. Bacteriol. 177 (1995) 1879-1882. [PMID: 7896715]
4. Sankaran, K., Gan, K., Rash, B., Qi, H.Y., Wu, H.C. and Rick, P.D. Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli. J. Bacteriol. 179 (1997) 2944-2948. [PMID: 9139912]
5. Pailler, J., Aucher, W., Pires, M. and Buddelmeijer, N. Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane. J. Bacteriol. 194 (2012) 2142-2151. [PMID: 22287519]
EC 2.5.1.146
Accepted name: 3-geranyl-3-[(Z)-2-isocyanoethenyl]indole synthase
Reaction: geranyl diphosphate + 3-[(Z)-2-isocyanoethenyl]-1H-indole = 3-geranyl-3-[(Z)-2-isocyanoethenyl]-1H-indole + diphosphate
Other name(s): famD2 (gene name)
Systematic name: geranyl-diphosphate:3-[(Z)-2-isocyanoethenyl]-1H-indole geranyltransferase
Comments: The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, participates in the biosynthesis of hapalindole-type alkaloids.
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1. Li, S., Lowell, A.N., Yu, F., Raveh, A., Newmister, S.A., Bair, N., Schaub, J.M., Williams, R.M. and Sherman, D.H. Hapalindole/ambiguine biogenesis Is mediated by a Cope rearrangement, C-C bond-forming cascade. J. Am. Chem. Soc. 137 (2015) 15366-15369. [PMID: 26629885]
EC 2.5.1.147
Accepted name: 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase
Reaction: 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
For diagram of reaction click here.
Glossary: 5-amino-6-(D-ribitylamino)uracil = 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione
Other name(s): cofH (gene name); cbiF (gene name) (ambiguous)
Systematic name: 5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase
Comments: The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (Fo), the precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. Fo is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to initiate the reaction.
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References:
1. Decamps, L., Philmus, B., Benjdia, A., White, R., Begley, T.P. and Berteau, O. Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. J. Am. Chem. Soc. 134 (2012) 18173-18176. [PMID: 23072415]
2. Philmus, B., Decamps, L., Berteau, O. and Begley, T.P. Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis. J. Am. Chem. Soc. 137 (2015) 5406-5413. [PMID: 25781338]
EC 2.5.1.148
Accepted name: lycopaoctaene synthase
Reaction: 2 geranylgeranyl diphosphate + NADPH + H+ = lycopaoctaene + 2 diphosphate + NADP+ (overall reaction)
For diagram of reaction click here
Glossary: lycopaoctaene = 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
Other name(s): LOS (gene name)
Systematic name: geranylgeranyl-diphosphate:geranylgeranyl-diphosphate geranylgeranyltransferase
Comments: The enzyme, characterized from the green microalga Botryococcus braunii race L, in involved in biosynthesis of (14E,18E)-lycopadiene. In vitro, the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo.
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References:
1. Thapa, H.R., Naik, M.T., Okada, S., Takada, K., Molnar, I., Xu, Y. and Devarenne, T.P. A squalene synthase-like enzyme initiates production of tetraterpenoid hydrocarbons in Botryococcus braunii Race L. Nat Commun 7 (2016) 11198. [PMID: 27050299]
2. Thapa, H.R., Tang, S., Sacchettini, J.C. and Devarenne, T.P. Tetraterpene synthase substrate and product specificity in the green microalga Botryococcus braunii Race L. ACS Chem. Biol. 12 (2017) 2408-2416. [PMID: 28813599]
EC 2.5.1.149
Accepted name: lycopene elongase/hydratase (flavuxanthin-forming)
Reaction: (1) prenyl diphosphate + all-trans-lycopene + acceptor + H2O = nonaflavuxanthin + reduced electron acceptor + diphosphate
For diagram of reaction click here
Glossary: flavuxanthin = 2,2'-bis-(4-hydroxy-3-methylbut-2-enyl)-1,16,1',16'-tetradehydro-1,2,1',2'-tetrahydro-ψ,ψ-carotene = (2E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,28E,34E)-5,32-diisopropenyl-2,8,12,16,21,25,29,35-octamethylhexatriaconta-2,8,10,12,14,16,18,20,22,24,26,28,34-tridecaene-1,36-diol
Other name(s): crtEb (gene name)
Systematic name: prenyl-diphosphate:all-trans-lycopene prenyltransferase (hydrating, flavuxanthin-forming)
Comments: The enzyme, characterized from the bacterium Corynebacterium glutamicum, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2, as well as the hydroxylation of the new isoprene unit. The enzyme acts at both ends of the substrate, forming the C50 carotenoid flavuxanthin via the C45 intermediate nonaflavuxanthin. cf. EC 2.5.1.150, lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming).
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References:
1. Krubasik, P., Kobayashi, M. and Sandmann, G. Expression and functional analysis of a gene cluster involved in the synthesis of decaprenoxanthin reveals the mechanisms for C50 carotenoid formation. Eur. J. Biochem. 268 (2001) 3702-3708. [PMID: 11432736]
2. Heider, S.A., Peters-Wendisch, P. and Wendisch, V.F. Carotenoid biosynthesis and overproduction in Corynebacterium glutamicum. BMC Microbiol. 12 (2012) 198. [PMID: 22963379]
EC 2.5.1.150
Accepted name: lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)
Reaction: (1) prenyl diphosphate + all-trans-lycopene + H2O = dihydroisopentenyldehydrorhodopin + diphosphate
For diagram of reaction click here or click here
Glossary: dihydrobisanhydrobacterioruberin = (2S,2S')-2,2'-bis(3-methylbut-2-en-1-yl)-3,3',4,4'-tetradehydro-1,1',2,2'-tetrahydro-ψ,ψ-carotene-1,1'-diol = (3S,4E,6E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,30R)-2,6,10,14,19,23,27,31-octamethyl-3,30-bis(3-methylbut-2-en-1-yl)dotriaconta-4,6,8,10,12,14,16,18,20,22,24,26-dodecaene-2,31-diol
Other name(s): lbtA (gene name); lyeJ (gene name)
Systematic name: prenyl-diphosphate:all-trans-lycopene prenyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming)
Comments: The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate, and combined with the action of EC 1.3.99.37, 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin. cf. EC 2.5.1.149, lycopene elongase/hydratase (flavuxanthin-forming).
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References:
1. Tao, L., Yao, H. and Cheng, Q. Genes from a Dietzia sp. for synthesis of C40 and C50 β-cyclic carotenoids. Gene 386 (2007) 90-97. [PMID: 17008032]
2. Dummer, A.M., Bonsall, J.C., Cihla, J.B., Lawry, S.M., Johnson, G.C. and Peck, R.F. Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum. J. Bacteriol. 193 (2011) 5658-5667. [PMID: 21840984]
3. Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S. and Nakamura, S. Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica. J. Bacteriol. 197 (2015) 1614-1623. [PMID: 25712483]
EC 2.5.1.151
Accepted name: alkylcobalamin dealkylase
Reaction: (1) methylcob(III)alamin + [alkylcobalamin dealkylase] + glutathione = cob(I)alamin-[alkylcobalamin dealkylase] + an S-methyl glutathione
Other name(s): MMACHC (gene name); alkylcobalamin:glutathione S-alkyltransferase; alkylcobalamin reductase
Systematic name: methylcobalamin:glutathione S-methyltransferase
Comments: This mammalian enzyme, which is cytosolic, can bind internalized methylcob(III)alamin and adenosylcob(III)alamin and process them to cob(I)alamin using the thiolate of glutathione for nucleophilic displacement. The product remains bound to the protein, and, following its oxidation to cob(II)alamin, is transferred by the enzyme, together with its interacting partner MMADHC, directly to downstream enzymes involved in adenosylcob(III)alamin and methylcob(III)alamin biosynthesis. In addition to its dealkylase function, the enzyme also catalyse an entirely different decyanase reaction with cyanocob(III)alamin (cf. EC 1.16.1.6, cyanocobalamin reductase).
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References:
1. Hannibal, L., Kim, J., Brasch, N.E., Wang, S., Rosenblatt, D.S., Banerjee, R. and Jacobsen, D.W. Processing of alkylcobalamins in mammalian cells: A role for the MMACHC (cblC) gene product. Mol. Genet. Metab. 97 (2009) 260-266. [PMID: 19447654]
2. Kim, J., Hannibal, L., Gherasim, C., Jacobsen, D.W. and Banerjee, R. A human vitamin B12 trafficking protein uses glutathione transferase activity for processing alkylcobalamins. J. Biol. Chem. 284 (2009) 33418-33424. [PMID: 19801555]
3. Koutmos, M., Gherasim, C., Smith, J.L. and Banerjee, R. Structural basis of multifunctionality in a vitamin B12-processing enzyme. J. Biol. Chem. 286 (2011) 29780-29787. [PMID: 21697092]
EC 2.5.1.152
Accepted name: D-histidine 2-aminobutanoyltransferase
Reaction: S-adenosyl-L-methionine + D-histidine = N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
For diagram of reaction click here.
Glossary: staphylopine = N-[(3S)-3-{[(1S)-1-carboxyethyl]amino}-3-carboxypropyl]-D-histidine
Other name(s): cntL (gene name)
Systematic name: S-adenosyl-L-methionine:D-histidine N-[(3S)-3-amino-3-carboxypropyl]-transferase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, participates in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
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References:
1. Ghssein, G., Brutesco, C., Ouerdane, L., Fojcik, C., Izaute, A., Wang, S., Hajjar, C., Lobinski, R., Lemaire, D., Richaud, P., Voulhoux, R., Espaillat, A., Cava, F., Pignol, D., Borezee-Durant, E. and Arnoux, P. Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus. Science 352 (2016) 1105-1109. [PMID: 27230378]
EC 2.5.1.153
Accepted name: adenosine tuberculosinyltransferase
Reaction: tuberculosinyl diphosphate + adenosine = 1-tuberculosinyladenosine + diphosphate
Glossary: tuberculosinyl diphosphate = halima-5,13-dien-15-yl diphosphate
Other name(s): Rv3378c (locus name)
Systematic name: tuberculosinyl-diphosphate:adenosine tuberculosinyltransferase
Comments: The enzyme, characterized from the bacterial pathogen Mycobacterium tuberculosis, produces 1-tuberculosinyladenosine, an unusual terpene nucleoside that acts as a phagolysosome disruptor by neutralizing the pH, resulting in swelling of the lysosome and obliteration of its multilamellar structure.
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1. Layre, E., Lee, H.J., Young, D.C., Martinot, A.J., Buter, J., Minnaard, A.J., Annand, J.W., Fortune, S.M., Snider, B.B., Matsunaga, I., Rubin, E.J., Alber, T. and Moody, D.B. Molecular profiling of Mycobacterium tuberculosis identifies tuberculosinyl nucleoside products of the virulence-associated enzyme Rv3378c. Proc. Natl. Acad. Sci. USA 111 (2014) 2978-2983. [PMID: 24516143]
2. Young, D.C., Layre, E., Pan, S.J., Tapley, A., Adamson, J., Seshadri, C., Wu, Z., Buter, J., Minnaard, A.J., Coscolla, M., Gagneux, S., Copin, R., Ernst, J.D., Bishai, W.R., Snider, B.B. and Moody, D.B. In vivo biosynthesis of terpene nucleosides provides unique chemical markers of Mycobacterium tuberculosis infection. Chem. Biol. 22 (2015) 516-526. [PMID: 25910243]
3. Buter, J., Cheng, T.Y., Ghanem, M., Grootemaat, A.E., Raman, S., Feng, X., Plantijn, A.R., Ennis, T., Wang, J., Cotton, R.N., Layre, E., Ramnarine, A.K., Mayfield, J.A., Young, D.C., Jezek Martinot, A., Siddiqi, N., Wakabayashi, S., Botella, H., Calderon, R., Murray, M., Ehrt, S., Snider, B.B., Reed, M.B., Oldfield, E., Tan, S., Rubin, E.J., Behr, M.A., van der Wel, N.N., Minnaard, A.J. and Moody, D.B. Mycobacterium tuberculosis releases an antacid that remodels phagosomes. Nat. Chem. Biol. 15 (2019) 889-899. [PMID: 31427817]
EC 2.5.1.154
Accepted name: corrinoid adenosyltransferase EutT
Reaction: 2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein (overall reaction)
Other name(s): eutT (gene name)
Systematic name: ATP:cob(II)alamin Coβ-adenosyltransferase (diphosphate-forming)
Comments: The corrinoid adenosylation pathway comprises three steps: (i) reduction of Co(III) within the corrinoid to Co(II) by a one-electron transfer. This can occur non-enzymically in the presence of dihydroflavin nucleotides or reduced flavoproteins [1]. (ii) Co(II) is bound by corrinoid adenosyltransferase, resulting in displacement of the lower axial ligand by an aromatic residue. The reduction potential of the 4-coordinate Co(II) intermediate is raised by ~250 mV compared with the free compound, bringing it to within physiological range. This is followed by a second single-electron transfer from either free dihydroflavins or the reduced flavin cofactor of flavoproteins, resulting in reduction to Co(I) [4]. (iii) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP, resulting in transfer of the deoxyadenosyl group and oxidation of the cobalt atom to Co(III) state. Three types of corrinoid adenosyltransferases, not related by sequence, have been described. In the anaerobic bacterium Salmonella enterica they are encoded by the cobA gene (a housekeeping enzyme involved in both the de novo biosynthesis and the salvage of adenosylcobalamin), the pduO gene (involved in (S)-propane-1,2-diol utilization), and the eutT gene (involved in ethanolamine utilization). The first two types, which produce triphosphate, are classified as EC 2.5.1.17, corrinoid adenosyltransferase, while the EutT type hydrolyses triphosphate to diphosphate and phosphate during catalysis and is thus classified separately.
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References:
1. Fonseca, M.V. and Escalante-Semerena, J.C. Reduction of cob(III)alamin to cob(II)alamin in Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 182 (2000) 4304-4309. [PMID: 10894741]
2. Sheppard, D.E., Penrod, J.T., Bobik, T., Kofoid, E. and Roth, J.R. Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica, J. Bacteriol. 186 (2004) 7635-7644. [PMID: 15516577]
3. Buan, N.R. and Escalante-Semerena, J.C. Purification and initial biochemical characterization of ATP:cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica, J. Biol. Chem. 281 (2006) 16971-16977. [PMID: 16636051]
4. Mera, P.E. and Escalante-Semerena, J.C. Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins. J. Biol. Chem. 285 (2010) 2911-2917. [PMID: 19933577]
5. Moore, T.C., Mera, P.E. and Escalante-Semerena, J.C. the Eutt enzyme of Salmonella enterica is a unique ATP:cob(I)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity. J. Bacteriol. 196 (2014) 903-910. [PMID: 24336938]
EC 2.5.1.155
Accepted name: phosphoglycerol geranylfarnesyltransferase
Reaction: all-trans-pentaprenyl diphosphate + sn-glycerol 1-phosphate = sn-3-O-(farnesylgeranyl)glycerol 1-phosphate + diphosphate
Other name(s): GFGP synthase
Systematic name: all-trans pentaprenyl diphosphate:sn-glycerol-1-phosphate pentaprenyltransferase
Comments: The enzyme, characterized from the archaeon Aeropyrum pernix, catalyses the first pathway-specific step in the biosynthesis of the core membrane C25,C25-diether lipids in some archaea. It does not act on geranylgeranyl diphosphate. cf. EC 2.5.1.41, phosphoglycerol geranylgeranyltransferase.
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References:
1. Yoshida, R., Yoshimura, T. and Hemmi, H. Biosynthetic machinery for C25,C25-diether archaeal lipids from the hyperthermophilic archaeon Aeropyrum pernix. Biochem. Biophys. Res. Commun. 497 (2018) 87-92. [PMID: 29427665]
EC 2.5.1.156
Accepted name: geranylfarnesylglycerol-phosphate geranylfarnesyltransferase
Reaction: all-trans-pentaprenyl diphosphate + sn-3-O-(farnesylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylfarnesyl)-sn-glycerol 1-phosphate + diphosphate
Other name(s): DGFGP synthase; 2,3-bis-O-(farnesylgeranyl)-sn-glycerol 1-phosphate synthase; 2,3-di-O-farnesylgeranylglyceryl synthase
Systematic name: all-trans-pentaprenyl diphosphate:sn-3-O-(pentaprenyl)glycerol 1-phosphate pentaprenyltransferase
Comments: The enzyme, characterized from the archaeon Aeropyrum pernix, carries out the second prenyltransfer reaction involved in the formation of C25,C25 membrane diether-lipids in some archaea. Requires a divalent metal cation, such as Mg2+. The enzyme cannot accept sn-3-(O-geranylgeranyl)glycerol 1-phosphate as the prenyl donor. cf. EC 2.5.1.42, geranylgeranylglycerol-phosphate geranylgeranyltransferase.
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References:
1. Yoshida, R., Yoshimura, T. and Hemmi, H. Biosynthetic machinery for C25,C25-diether archaeal lipids from the hyperthermophilic archaeon Aeropyrum pernix. Biochem. Biophys. Res. Commun. 497 (2018) 87-92. [PMID: 29427665]
EC 2.5.1.157
Accepted name: rRNA small subunit aminocarboxypropyltransferase
Reaction: S-adenosyl-L-methionine + an N1-methyl-pseudouridine in rRNA = S-methyl-5'-thioadenosine + an N1-methyl-N3-[(3S)-3-aminocarboxypropyl]-pseudouridine in rRNA
Other name(s): TSR3 (gene name)
Systematic name: S-adenosyl-L-methionine:rRNA N1-pseudouridine 3-[(3S)-3-amino-3-carboxypropyl]transferase
Comments: The enzyme, found in all eukaryotes and some archaea, catalyses the final step in production of the modified rRNA nucleotide N1-methyl-N3-[(3S)-aminocarboxypropyl]-pseudouridine (m1acp3ψ). This modified nucleotide is present in the small subunit of ribosomal RNA (18S in eukaryotes and 16S in archaea). cf. EC 2.5.1.114, tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase, and EC 2.5.1.108, 2-(3-amino-3-carboxypropyl)histidine synthase.
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References:
1. Meyer, B., Wurm, J.P., Sharma, S., Immer, C., Pogoryelov, D., Kotter, P., Lafontaine, D.L., Wohnert, J. and Entian, K.D. Ribosome biogenesis factor Tsr3 is the aminocarboxypropyl transferase responsible for 18S rRNA hypermodification in yeast and humans. Nucleic Acids Res. 44 (2016) 4304-4316. [PMID: 27084949]
EC 2.5.1.158
Accepted name: hexaprenyl diphosphate synthase (prenyl-diphosphate specific)
Reaction: prenyl diphosphate + 5 3-methylbut-3-en-1-yl diphosphate = all-trans-hexaprenyl diphosphate + 5 diphosphate
Glossary: prenyl diphosphate = dimethylallyl diphosphate
Other name(s): HexPPS
Systematic name: prenyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate transferase (adding 5 units of 3-methylbut-3-en-1-yl)
Comments: This activity has been characterized from a number of fungal bifunctional enzymes. Following the formation of hexaprenyl diphosphate, a different domain in the enzymes catalyses its cyclization into a triterpene (see EC 4.2.3.221, macrophomene synthase and EC 4.2.3.220, talaropentaene synthase). cf. EC 2.5.1.82, hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific].
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1. Tao, H., Lauterbach, L., Bian, G., Chen, R., Hou, A., Mori, T., Cheng, S., Hu, B., Lu, L., Mu, X., Li, M., Adachi, N., Kawasaki, M., Moriya, T., Senda, T., Wang, X., Deng, Z., Abe, I., Dickschat, J.S. and Liu, T. Discovery of non-squalene triterpenes. Nature 606 (2022) 414-419. [PMID: 35650436]
EC 2.5.1.159
Accepted name: hapalindole G dimethylallyltransferase
Reaction: (1) prenyl diphosphate + hapalindole G = ambiguine A + diphosphate
For diagram of reaction click here
Glossary: prenyl diphosphate = dimethylallyl diphosphate
Other name(s): ambP3 (gene name); famD1 (gene name)
Systematic name: prenyl-diphosphate:hapalindole G prenyltransferase (ambiguine A-forming)
Comments: Requires Mg2+. The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, is involved in the biosynthesis of hapalindole-type alkaloids. When acting on hapalindole U, the enzyme forms ambiguine H.
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References:
1. Hillwig, M.L., Zhu, Q. and Liu, X. Biosynthesis of ambiguine indole alkaloids in cyanobacterium Fischerella ambigua. ACS Chem. Biol. 9 (2014) 372-377. [PMID: 24180436]
EC 2.5.1.160
Accepted name: plant cystathionine γ-synthase
Reaction: O-phospho-L-homoserine + L-cysteine = L-cystathionine + phosphate
Other name(s): CGS1 (gene name)
Systematic name: O-phospho-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase
Comments: A pyridoxal 5'-phosphate-dependent enzyme, found in plants, that participates in the plant L-methionine biosynthetic pathway. It differs from its bacterial counterpart, EC 2.5.1.48, cystathionine γ-synthase, in being specific for O-phospho-L-homoserine (the bacterial enzyme is specific for O-succinyl-L-homoserine).
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1. Ravanel, S., Gakiere, B., Job, D. and Douce, R. Cystathionine γ-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli. Biochem. J. 331 (1998) 639-648. [PMID: 9531508]
2. Steegborn, C., Messerschmidt, A., Laber, B., Streber, W., Huber, R. and Clausen, T. The crystal structure of cystathionine γ-synthase from Nicotiana tabacum reveals its substrate and reaction specificity. J. Mol. Biol. 290 (1999) 983-996. [PMID: 10438597]
3. Clausen, T., Wahl, M.C., Messerschmidt, A., Huber, R., Fuhrmann, J.C., Laber, B., Streber, W. and Steegborn, C. Cloning, purification and characterisation of cystathionine γ-synthase from Nicotiana tabacum. Biol. Chem. 380 (1999) 1237-1242. [PMID: 10595588]
fumitremorgin B = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-11-(3-methylbut-2-en-1-yl)-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,6]pyrido[3,4-b]indole-5,14-dione
(2) dimethylallyl diphosphate + ATP = diphosphate + N6-(dimethylallyl)adenosine 5′-triphosphate
7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine = yW-89
3-linalylflaviolin = 2,5,7-trihydroxy-3-(3,7-dimethylocta-1,6-dien-3-yl)naphthalene-1,4-dione
2-O,3-dimethylflaviolin = 5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
6-linalyl-2-O,3-dimethylflaviolin = 6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
2-O,3-dimethylflaviolin = 5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
7-O-geranyl-2-O,3-dimethylflaviolin = 7-{[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy}-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione
norspermine = N,N'-bis(3-aminopropyl)-1,3-propanediamine
spermidine = N-(3-aminopropyl)-1,4-butanediamine
thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine
norspermidine = N-(3-aminopropyl)-1,4-butanediamine
norspermine = N,N'-bis(3-aminopropyl)-1,3-propanediamine
spermidine = N-(3-aminopropyl)-1,4-butanediamine
thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine
(1a) S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + N4-aminopropylspermidine
(1b) S-adenosyl 3-(methylsulfanyl)propylamine + N4-aminopropylspermidine = S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine
N4-aminopropylspermidine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
N4-bis(aminopropyl)spermidine = N,N,N′-tris(3-aminopropyl)butane-1,4-diamine
3-deoxy-D-glycero-D-galacto-nononate = Kdn
validamine = (1R,2S,3S,4S,6R)-4-amino-6-(hydroxymethyl)cyclohexane-1,2,3-triol
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one
(2) prenyl diphosphate + a 2-acyl-4,6-bis(prenyl)phloroglucinol = diphosphate + a a 2-acyl-4,6,6-tris(prenyl)cyclohexa-2,4-dien-1-one
(2) geranyl diphosphate + esculetin = diphosphate + 8-geranylesculetin
esculetin = 6,7-dihydroxy-1-benzopyran-2-one
umbelliferone = 7-hydroxy-1-benzopyran-2-one
osthenol = 7-hydroxy-8-prenyl-1-benzopyran-2-one
(1a) prenyl diphosphate + 3-methylbut-3-en-1-yl diphosphate = diphosphate + neryl diphosphate
(1b) neryl diphosphate + 3-methylbut-3-en-1-yl diphosphate = diphosphate + (2Z,6Z)-farnesyl diphosphate
(1c) (2Z,6Z)-farnesyl diphosphate + 3-methylbut-3-en-1-yl diphosphate = diphosphate + nerylneryl diphosphate
(1a) 2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate
(1b) prephytoene diphosphate + NADPH + H+ = lycopaoctaene + diphosphate + NADP+
(2) prenyl diphosphate + nonaflavuxanthin + acceptor + H2O = flavuxanthin + reduced electron acceptor + diphosphate
(2) prenyl diphosphate + isopentenyldehydrorhodopin + H2O = dihydrobisanhydrobacterioruberin + diphosphate
(2) adenosylcob(III)alamin + [alkylcobalamin dealkylase] + glutathione = cob(I)alamin-[alkylcobalamin dealkylase] + S-adenosyl glutathione
(1a) 2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
(1b) a reduced flavoprotein + 2 [corrinoid adenosyltransferase]-cob(II)alamin = an oxidized flavoprotein + 2 [corrinoid adenosyltransferase]-cob(I)alamin (spontaneous)
(1c) 2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)alamin = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + 2 [corrinoid adenosyltransferase]
3-methylbut-3-en-1-yl diphosphate = isopentenyl diphosphate
(2) prenyl diphosphate + hapalindole U = ambiguine H + diphosphate
hapalindole G = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
ambiguine A = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
hapalindole U = (6aS,9R,10R,10aS)-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
ambiguine H = (6aS,9R,10R,10aS)-9-ethenyl-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
Continued with EC 2.6.1.1 to EC 2.6.1.50
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