EC 2.4.1.1 to EC 2.4.1.50
EC 2.4.1.51 to EC 2.4.1.100
EC 2.4.1.101 to EC 2.4.1.150
EC 2.4.1.151 to EC 2.4.1.200
EC 2.4.1.201 to EC 2.4.1.250
EC 2.4.1.251 to EC 2.4.1.300
Accepted name: 2'-deamino-2'-hydroxyneamine 1-α-D-kanosaminyltransferase
Reaction: (1) UDP-α-D-kanosamine + 2'-deamino-2'-hydroxyneamine = UDP + kanamycin A
(2) UDP-α-D-kanosamine + neamine = UDP + kanamycin B
(3) UDP-α-D-kanosamine + paromamine = UDP + kanamycin C
(4) UDP-α-D-kanosamine + 2'-deamino-2'-hydroxyparomamine = UDP + kanamycin X
For diagram of reaction click here.
Glossary: neamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
paromamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
UDP-α-D-kanosamine = uridine 5'-[3-(3-amino-3-deoxy-α-D-glucopyranosyl) diphosphate]
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
kanamycin B = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
kanamycin C = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
kanamycin X = (1S,2R,3R,4S,6R)-4,6-diamino-3-(α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
Other name(s): kanE (gene name); kanM2 (gene name)
Systematic name: UDP-α-D-kanosamine:2'-deamino-2'-hydroxyneamine 1-α-D-kanosaminyltransferase
Comments: Involved in the biosynthetic pathway of kanamycins. The enzyme characterized from the bacterium Streptomyces kanamyceticus can also accept UDP-α-D-glucose with lower efficiency [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kudo, F., Sucipto, H. and Eguchi, T. Enzymatic activity of a glycosyltransferase KanM2 encoded in the kanamycin biosynthetic gene cluster. J. Antibiot. (Tokyo) 62 (2009) 707-710. [PMID: 19911031]
2. Sucipto, H., Kudo, F. and Eguchi, T. The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK. Angew. Chem. Int. Ed. Engl. 51 (2012) 3428-3431. [PMID: 22374809]
Accepted name: L-demethylnoviosyl transferase
Reaction: dTDP-4-O-demethyl-β-L-noviose + novobiocic acid = dTDP + demethyldecarbamoyl novobiocin
For diagram of reaction click here.
Glossary: novobiocic acid = N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide
dTDP-4-O-demethyl-β-L-noviose = dTDP-6-deoxy-5-methyl-β-L-altropyranose = dTDP-(2S,3R,4R,5R)-6,6-dimethyltetrahydro-2H-pyran-2,3,4,5-tetraol
demethyldecarbamoyl novobiocin = N-{7-[(6-deoxy-5-methyl-β-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide
Other name(s): novM (gene name); dTDP-β-L-noviose:novobiocic acid 7-O-noviosyltransferase; L-noviosyl transferase
Systematic name: dTDP-4-O-demethyl-β-L-noviose:novobiocic acid 7-O-[4-O-demethyl-L-noviosyl]transferase
Comments: The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Freel Meyers, C.L., Oberthur, M., Anderson, J.W., Kahne, D. and Walsh, C.T. Initial characterization of novobiocic acid noviosyl transferase activity of NovM in biosynthesis of the antibiotic novobiocin. Biochemistry 42 (2003) 4179-4189. [PMID: 12680772]
2. Albermann, C., Soriano, A., Jiang, J., Vollmer, H., Biggins, J.B., Barton, W.A., Lesniak, J., Nikolov, D.B. and Thorson, J.S. Substrate specificity of NovM: implications for novobiocin biosynthesis and glycorandomization. Org. Lett. 5 (2003) 933-936. [PMID: 12633109]
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbbD; WbbD β3Gal-transferase; UDP-Gal:GlcNAc-R β1,3-galactosyltransferase; UDP-Gal:GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase; UDP-Gal:GlcNAc-R galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-β-galactosyltransferase (configuration-inverting)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O7:K1 (VW187). Requires Mn2+. cf. EC 2.4.1.343, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Riley, J.G., Menggad, M., Montoya-Peleaz, P.J., Szarek, W.A., Marolda, C.L., Valvano, M.A., Schutzbach, J.S. and Brockhausen, I. The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal: GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase involved in the biosynthesis of O7-specific lipopolysaccharide. Glycobiology 15 (2005) 605-613. [PMID: 15625181]
2. Brockhausen, I., Riley, J.G., Joynt, M., Yang, X. and Szarek, W.A. Acceptor substrate specificity of UDP-Gal: GlcNAc-R β1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1. Glycoconj. J. 25 (2008) 663-673. [PMID: 18536883]
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→4)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfeD; UDP-Gal:GlcNAc-R 1,4-Gal-transferase; UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,4-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn2+ or to a lesser extent by Mg2+, Ca2+, Ni2+ or Pb2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Xu, C., Liu, B., Hu, B., Han, Y., Feng, L., Allingham, J.S., Szarek, W.A., Wang, L. and Brockhausen, I. Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis. J. Bacteriol. 193 (2011) 449-459. [PMID: 21057010]
Accepted name: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase
Reaction: UDP-α-D-glucose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Glc-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfaP; WfgD; UDP-Glc:GlcNAc-pyrophosphate-lipid β-1,3-glucosyltransferase; UDP-Glc:GlcNAc-diphosphate-lipid β-1,3-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,3-glucosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Brockhausen, I., Hu, B., Liu, B., Lau, K., Szarek, W.A., Wang, L. and Feng, L. Characterization of two β-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152. J. Bacteriol. 190 (2008) 4922-4932. [PMID: 18487334]
Accepted name: UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbnH
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol α-1,3-N-acetyl-D-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of Escherichia coli serotype O86.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Yi, W., Yao, Q., Zhang, Y., Motari, E., Lin, S. and Wang, P.G. The wbnH gene of Escherichia coli O86:H2 encodes an α-1,3-N-acetylgalactosaminyl transferase involved in the O-repeating unit biosynthesis. Biochem. Biophys. Res. Commun. 344 (2006) 631-639. [PMID: 16630548]
[EC 2.4.1.307 Deleted entry: UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. Now included in EC 2.4.1.122, glycoprotein-N-acetylgalactosamine β-1,3-galactosyltransferase (EC 2.4.1.307 created 2013, deleted 2016)]
Accepted name: GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = GDP + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbnK
Systematic name: GDP-β-L-fucose:β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,2-fucosyltransferase
Comments: The enzyme is involved in the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040-2041. [PMID: 15713070]
2. Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418-423. [PMID: 20418877]
Accepted name: UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-(α-L-Fuc-(1→2))-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbnI
Systematic name: UDP-α-D-galactose:α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,3-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040-2041. [PMID: 15713070]
2. Yi, W., Zhu, L., Guo, H., Li, M., Li, J. and Wang, P.G. Formation of a new O-polysaccharide in Escherichia coli O86 via disruption of a glycosyltransferase gene involved in O-unit assembly. Carbohydr. Res. 341 (2006) 2254-2260. [PMID: 16839526]
3. Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418-423. [PMID: 20418877]
Accepted name: vancomycin aglycone glucosyltransferase
Reaction: UDP-α-D-glucose + vancomycin aglycone = UDP + devancoaminyl-vancomycin
For diagram of reaction, click here
Glossary: desvancoaminyl-vancomycin = vancomycin pseudoaglycone
Other name(s): GtfB (ambiguous)
Systematic name: UDP-α-D-glucose:vancomycin aglycone 48-O-β-glucosyltransferase
Comments: The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745-4755. [PMID: 11294642]
2. Mulichak, A.M., Losey, H.C., Walsh, C.T. and Garavito, R.M. Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics. Structure 9 (2001) 547-557. [PMID: 11470430]
Accepted name: chloroorienticin B synthase
Reaction: dTDP-β-L-4-epi-vancosamine + desvancosaminyl-vancomycin = dTDP + chloroorienticin B
For diagram of reaction, click here
Glossary: dTDP-β-L-4-epi-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-methyl-β-L-arabino-hexopyranose
desvancosaminyl-vancomycin = vanomycin pseudoaglycone
Other name(s): GtfA
Systematic name: dTDP-L-4-epi-vancosamine:desvancosaminyl-vancomycin vancosaminyltransferase
Comments: The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mulichak, A.M., Losey, H.C., Lu, W., Wawrzak, Z., Walsh, C.T. and Garavito, R.M. Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway. Proc. Natl. Acad. Sci. USA 100 (2003) 9238-9243. [PMID: 12874381]
2. Lu, W., Oberthur, M., Leimkuhler, C., Tao, J., Kahne, D. and Walsh, C.T. Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin. Proc. Natl. Acad. Sci. USA 101 (2004) 4390-4395. [PMID: 15070728]
Accepted name: protein O-mannose β-1,4-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 3-O-(α-D-mannosyl)-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]
For diagram of reaction click here.
Other name(s): GTDC2 (gene name); POMGNT2
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-threonyl-[protein] 4-β-N-acetyl-D-glucosaminyltransferase
Comments: The human protein is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896-899. [PMID: 23929950]
Accepted name: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]
For diagram of reaction click here.
Other name(s): B3GALNT2
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl-threonyl-[protein] 3-β-N-acetyl-D-galactosaminyltransferase
Comments: The human protein is specific for UDP-N-acetyl-α-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hiruma, T., Togayachi, A., Okamura, K., Sato, T., Kikuchi, N., Kwon, Y.D., Nakamura, A., Fujimura, K., Gotoh, M., Tachibana, K., Ishizuka, Y., Noce, T., Nakanishi, H. and Narimatsu, H. A novel human β1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcβ1-3GlcNAc. J. Biol. Chem. 279 (2004) 14087-14095. [PMID: 14724282]
2. Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896-899. [PMID: 23929950]
Accepted name: ginsenoside Rd glucosyltransferase
Reaction: UDP-α-D-glucose + ginsenoside Rd = UDP + ginsenoside Rb1
Glossary: ginsenoside Rd = 20-(β-D-glucopyranosyl)oxy-3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol
ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol
For diagram of reaction click here.
Other name(s): UDPG:ginsenoside Rd glucosyltransferase; UDP-glucose:ginsenoside Rd glucosyltransferase; UGRdGT
Systematic name: UDP-glucose:ginsenoside-Rd β-1,6-glucosyltransferase
Comments: The glucosyl group forms a 1→6 bond to the glucosyloxy moiety at C-20 of ginsenoside Rd. Isolated from sanchi ginseng (Panax notoginseng).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yue, C.-J. and Zhong J.-J. Purification and characterization of UDPG:ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng. Process Biochem. 40 (2005) 3742-3748.
Accepted name: diglucosyl diacylglycerol synthase (1,6-linking)
Reaction: (1) UDP-α-D-glucose + 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
(2) UDP-α-D-glucose + 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
Other name(s): monoglucosyl diacylglycerol (1→6) glucosyltransferase; MGlcDAG (1→6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name)
Systematic name: UDP-α-D-glucose:1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol 6-glucosyltransferase
Comments: The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose [1]. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo [3]. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1′-sn-glycerol) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Jorasch, P., Wolter, F.P., Zahringer, U. and Heinz, E. A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29 (1998) 419-430. [PMID: 9720862]
2. Jorasch, P., Warnecke, D.C., Lindner, B., Zahringer, U. and Heinz, E. Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols. Eur. J. Biochem. 267 (2000) 3770-3783. [PMID: 10848996]
3. Andres, E., Martinez, N. and Planas, A. Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: potential target against mycoplasma infections. J. Biol. Chem. 286 (2011) 35367-35379. [PMID: 21835921]
Accepted name: tylactone mycaminosyltransferase
Reaction: tylactone + dTDP-α-D-mycaminose = dTDP + 5-O-β-D-mycaminosyltylactone
For diagram of reaction click here.
Glossary: tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyloxacyclohexadeca-11,13-diene-2,10-dione
dTDP-α-D-mycaminose = dTDP-3,6-dideoxy-3-dimethylamino-α-D-glucopyranose
Other name(s): tylM2 (gene name)
Systematic name: dTDP-α-D-mycaminose:tylactone 5-O-β-D-mycaminosyltransferase
Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. Activity is significantly enhanced by the presence of an accessory protein encoded by the tylM3 gene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Gandecha, A.R., Large, S.L. and Cundliffe, E. Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome. Gene 184 (1997) 197-203. [PMID: 9031628]
2. Melancon, C.E., 3rd, Takahashi, H. and Liu, H.W. Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient glycosyltransfer in macrolide antibiotic biosynthesis. J. Am. Chem. Soc. 126 (2004) 16726-16727. [PMID: 15612702]
Accepted name: O-mycaminosyltylonolide 6-deoxyallosyltransferase
Reaction: 5-O-β-D-mycaminosyltylonolide + dTDP-6-deoxy-α-D-allose = dTDP + demethyllactenocin
For diagram of reaction click here.
Glossary: mycaminose = 3,6-dideoxy-3-dimethylamino-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxooxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-β-D-allopyranoside
Other name(s): tylN (gene name)
Systematic name: dTDP-6-deoxy-α-D-allose:5-O-β-D-mycaminosyltylonolide 23-O-6-deoxy-α-D-allosyltransferase
Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wilson, V.T. and Cundliffe, E. Characterization and targeted disruption of a glycosyltransferase gene in the tylosin producer, Streptomyces fradiae. Gene 214 (1998) 95-100. [PMID: 9651492]
Accepted name: demethyllactenocin mycarosyltransferase
Reaction: dTDP-β-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin
For diagram of reaction click here.
Glossary: dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-D-allopyranoside
Other name(s): tylCV (gene name); tylC5 (gene name)
Systematic name: dTDP-β-L-mycarose:demethyllactenocin 4'-O-α-L-mycarosyltransferase
Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bate, N., Butler, A.R., Smith, I.P. and Cundliffe, E. The mycarose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. Microbiology 146 (2000) 139-146. [PMID: 10658660]
Accepted name: β-1,4-mannooligosaccharide phosphorylase
Reaction: [(1→4)-β-D-mannosyl]n + phosphate = [(1→4)-β-D-mannosyl]n-1 + α-D-mannose 1-phosphate
Other name(s): RaMP2
Systematic name: 1,4-β-D-mannooligosaccharide::phosphate α-D-mannosyltransferase
Comments: The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of β-1,4-mannooligosaccharide with a minimum size of three monomers.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Kawahara, R., Saburi, W., Odaka, R., Taguchi, H., Ito, S., Mori, H. and Matsui, H. Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, β-1,4-mannooligosaccharide phosphorylase. J. Biol. Chem. 287 (2012) 42389-42399. [PMID: 23093406]
Accepted name: 1,4-β-mannosyl-N-acetylglucosamine phosphorylase
Reaction: 4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + α-D-mannose 1-phosphate
Other name(s): BT1033
Systematic name: 4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine:phosphate α-D-mannosyltransferase
Comments: The enzyme isolated from the anaerobic bacterium Bacteroides thetaiotaomicron is involved in the degradation of host-derived N-glycans.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Nihira, T., Suzuki, E., Kitaoka, M., Nishimoto, M., Ohtsubo, K. and Nakai, H. Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans. J. Biol. Chem. 288 (2013) 27366-27374. [PMID: 23943617]
Accepted name: cellobionic acid phosphorylase
Reaction: 4-O-β-D-glucopyranosyl-D-gluconate + phosphate = α-D-glucose 1-phosphate + D-gluconate
Glossary: 4-O-β-D-glucopyranosyl-D-gluconate = cellobionate
Systematic name: 4-O-β-D-glucopyranosyl-D-gluconate:phosphate α-D-glucosyltransferase
Comments: The enzyme occurs in cellulolytic bacteria and fungi. It catalyses the reversible phosphorolysis of cellobionic acid. In the synthetic direction it produces 4-O-β-D-glucopyranosyl-D-glucuronate from α-D-glucose 1-phosphate and D-glucuronate with low activity
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nihira, T., Saito, Y., Nishimoto, M., Kitaoka, M., Igarashi, K., Ohtsubo, K. and Nakai, H. Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi. FEBS Lett 587 (2013) 3556-3561. [PMID: 24055472]
Accepted name: devancosaminyl-vancomycin vancosaminetransferase
Reaction: dTDP-β-L-vancosamine + devancosaminyl-vancomycin = dTDP + vancomycin
For diagram of reaction click here.
Glossary: dTDP-β-L-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-C-methyl-β-L-lyxo-hexopyranose
Other name(s): devancosaminyl-vancomycin TDP-vancosaminyltransferase; GtfD; dTDP-β-L-vancomycin:desvancosaminyl-vancomycin β-L-vancosaminetransferase; desvancosaminyl-vancomycin vancosaminetransferase
Systematic name: dTDP-β-L-vancomycin:devancosaminyl-vancomycin β-L-vancosaminetransferase
Comments: The enzyme, isolated from the bacterium Amycolatopsis orientalis, catalyses the ultimate step in the biosynthesis of the antibiotic vancomycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745-4755. [PMID: 11294642]
2. Mulichak, A.M., Lu, W., Losey, H.C., Walsh, C.T. and Garavito, R.M. Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43 (2004) 5170-5180. [PMID: 15122882]
Accepted name: 7-deoxyloganetic acid glucosyltransferase
Reaction: UDP-α-D-glucose + 7-deoxyloganetate = UDP + 7-deoxyloganate
For diagram of reaction click here.
Other name(s): UGT8
Systematic name: UDP-α-D-glucose:7-deoxyloganetate O-D-glucosyltransferase
Comments: Isolated from the plant Catharanthus roseus (Madagascar periwinkle). Involved in loganin and secologanin biosynthesis. Does not react with 7-deoxyloganetin. cf. EC 2.4.1.324 7-deoxyloganetin glucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Asada, K., Salim, V., Masada-Atsumi, S., Edmunds, E., Nagatoshi, M., Terasaka, K., Mizukami, H. and De Luca, V. A 7-deoxyloganetic acid glucosyltransferase contributes a key step in secologanin biosynthesis in madagascar periwinkle. Plant Cell 25 (2013) 4123-4134. [PMID: 24104568]
Accepted name: 7-deoxyloganetin glucosyltransferase
Reaction: UDP-α-D-glucose + 7-deoxyloganetin = UDP + 7-deoxyloganin
For diagram of reaction click here.
Other name(s): UDPglucose:iridoid glucosyltransferase; UGT6; UGT85A24
Systematic name: UDP-α-D-glucose:7-deoxyloganetin O-D-glucosyltransferase
Comments: Isolated from the plants Catharanthus roseus (Madagascar periwinkle) and Gardenia jasminoides (cape jasmine). With Gardenia it also acts on genipin. Involved in loganin and secologanin biosynthesis. Does not react with 7-deoxyloganetate. cf. EC 2.4.1.323 7-deoxyloganetic acid glucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Nagatoshi, M., Terasaka, K., Nagatsu, A. and Mizukami, H. Iridoid-specific glucosyltransferase from Gardenia jasminoides. J. Biol. Chem. 286 (2011) 32866-32874. [PMID: 21799001]
2. Asada, K., Salim, V., Masada-Atsumi, S., Edmunds, E., Nagatoshi, M., Terasaka, K., Mizukami, H. and De Luca, V. A 7-deoxyloganetic acid glucosyltransferase contributes a key step in secologanin biosynthesis in madagascar periwinkle. Plant Cell 25 (2013) 4123-4134. [PMID: 24104568]
Accepted name: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Reaction: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)
Systematic name: dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase
Comments: Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509-6516. [PMID: 11673418]
Accepted name: aklavinone 7-L-rhodosaminyltransferase
Reaction: dTDP-β-L-rhodosamine + aklavinone = dTDP + aclacinomycin T
For diagram of reaction click here.
Glossary: dTDP-β-L-rhodosamine = dTDP-2,3,6-trideoxy-3-dimethylamino-β-L-lyxo-hexose
aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
aclacinomycin T = 7-O-(α-L-rhodosaminyl)aklavinone
Other name(s): AknS/AknT; aklavinone 7-β-L-rhodosaminyltransferase; dTDP-β-L-rhodosamine:aklavinone 7-α-L-rhodosaminyltransferase
Systematic name: dTDP-β-L-rhodosamine:aklavinone 7-α-L-rhodosaminyltransferase (configuration-inverting)
Comments: Isolated from the bacterium Streptomyces galilaeus. Forms a complex with its accessory protein AknT, and has very low activity in its absence. The enzyme can also use dTDP-2-deoxy-β-L-fucose. Involved in the biosynthesis of other aclacinomycins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lu, W., Leimkuhler, C., Gatto, G.J., Jr., Kruger, R.G., Oberthur, M., Kahne, D. and Walsh, C.T. AknT is an activating protein for the glycosyltransferase AknS in L-aminodeoxysugar transfer to the aglycone of aclacinomycin A. Chem. Biol. 12 (2005) 527-534. [PMID: 15911373]
2. Leimkuhler, C., Fridman, M., Lupoli, T., Walker, S., Walsh, C.T. and Kahne, D. Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A. J. Am. Chem. Soc. 129 (2007) 10546-10550. [PMID: 17685523]
Accepted name: aclacinomycin-T 2-deoxy-L-fucose transferase
Reaction: dTDP-2-deoxy-β-L-fucose + aclacinomycin T = dTDP + aclacinomycin S
For diagram of reaction click here.
Glossary: idarubicin = (7S,9S)-9-acetyl-7-(3-amino-2,3,6-trideoxy-β-L-lyxo-hexosyloxy)-6,9,11-trihydroxy-7,8,9,10-tetrahydrotetracene-5,12-dione
aclacinomycin S = 7-O-(2-deoxy-α-L-fucosyl-(1→4)-rhodosaminyl)aklavinone
aclacinomycin T = 7-O-(α-L-rhodosaminyl)aklavinone
Other name(s): AknK
Systematic name: dTDP-2-deoxy-β-L-fucose:7-(α-L-rhodosaminyl)aklavinone 2-deoxy-α-L-fucosyltransferase
Comments: The enzyme, isolated from the bacterium Streptomyces galilaeus, is involved in the biosynthesis of other aclacinomycins. Also acts on idarubicin. It will slowly add a second 2-deoxy-L-fucose unit to aclacinomycin S in vitro.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lu, W., Leimkuhler, C., Oberthur, M., Kahne, D. and Walsh, C.T. AknK is an L-2-deoxyfucosyltransferase in the biosynthesis of the anthracycline aclacinomycin A. Biochemistry 43 (2004) 4548-4558. [PMID: 15078101]
Accepted name: erythronolide mycarosyltransferase
Reaction: dTDP-β-L-mycarose + erythronolide B = dTDP + 3-α-L-mycarosylerythronolide B
For diagram of reaction click here.
Glossary: dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
L-mycarose = 2,6-dideoxy-3-C-methyl-L-ribo-hexose
Other name(s): EryBV
Systematic name: dTDP-β-L-mycarose:erythronolide B L-mycarosyltransferase
Comments: Isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Zhang, C., Fu, Q., Albermann, C., Li, L. and Thorson, J.S. The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification. Chembiochem 8 (2007) 385-390. [PMID: 17262863]
Accepted name: sucrose 6F-phosphate phosphorylase
Reaction: sucrose 6F-phosphate + phosphate = α-D-glucopyranose 1-phosphate + β-D-fructofuranose 6-phosphate
Other name(s): sucrose 6'-phosphate phosphorylase
Systematic name: sucrose 6F-phosphate:phosphate 1-α-D-glucosyltransferase
Comments: The enzyme, isolated from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum, catalyses the reversible phosphorolysis of sucrose 6F-phosphate. It also acts on sucrose with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Verhaeghe, T., Aerts, D., Diricks, M., Soetaert, W. and Desmet, T. The quest for a thermostable sucrose phosphorylase reveals sucrose 6'-phosphate phosphorylase as a novel specificity. Appl. Microbiol. Biotechnol. 98 (2014) 7027-7037. [PMID: 24599311]
Accepted name: β-D-glucosyl crocetin β-1,6-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + β-D-gentiobiosyl crocetin
(2) UDP-α-D-glucose + bis(β-D-glucosyl) crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl β-D-glucosyl crocetin = UDP + crocin
For diagram of reaction click here.
Glossary: crocin = bis(β-D-gentiobiosyl) crocetin
crocetin = (2E,4E,6E,8E,10E,12E,14E)-2,6,11,15-tetramethylhexadeca-2,4,6,8,10,12,14-heptaenedioate
Other name(s): UGT94E5; UDP-glucose:crocetin glucosyl ester glucosyltransferasee
Systematic name: UDP-α-D-glucose:β-D-glucosyl crocetin β-1,6-glucosyltransferase
Comments: The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271, crocetin glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett 586 (2012) 1055-1061. [PMID: 22569263]
Accepted name: 8-demethyltetracenomycin C L-rhamnosyltransferase
Reaction: dTDP-β-L-rhamnose + 8-demethyltetracenomycin C = dTDP + 8-demethyl-8-α-L-rhamnosyltetracenomycin C
For diagram of reaction click here.
Glossary: dTDP-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose
Other name(s): elmGT
Systematic name: dTDP-β-L-rhamnose:8-demethyltetracenomycin C 3-α-L-rhamnosyltransferase
Comments: Isolated from Streptomyces olivaceus Tü2353. Involved in elloramycin biosynthesis. In vitro it can also utilize other 6-deoxy D- or L-hexoses.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Blanco, G., Patallo, E.P., Brana, A.F., Trefzer, A., Bechthold, A., Rohr, J., Mendez, C. and Salas, J.A. Identification of a sugar flexible glycosyltransferase from Streptomyces olivaceus, the producer of the antitumor polyketide elloramycin. Chem. Biol. 8 (2001) 253-263. [PMID: 11306350]
Accepted name: 1,2-α-glucosylglycerol phosphorylase
Reaction: 2-O-α-D-glucopyranosyl-glycerol + phosphate = β-D-glucose 1-phosphate + glycerol
Other name(s): 2-O-α-D-glucopyranosylglycerol phosphorylase
Systematic name: 2-O-α-D-glucopyranosyl-glycerol:phosphate β-D-glucosyltransferase
Comments: The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nihira, T., Saito, Y., Ohtsubo, K., Nakai, H. and Kitaoka, M. 2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate. PLoS One 9 (2014) e86548. [PMID: 24466148]
2. Touhara, K.K., Nihira, T., Kitaoka, M., Nakai, H. and Fushinobu, S. Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase. J. Biol. Chem. 289 (2014) 18067-18075. [PMID: 24828502]
Accepted name: 1,2-β-oligoglucan phosphorylase
Reaction: [(1→2)-β-D-glucosyl]n + phosphate = [(1→2)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Systematic name: 1,2-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1→2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nakajima, M., Toyoizumi, H., Abe, K., Nakai, H., Taguchi, H. and Kitaoka, M. 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One 9 (2014) e92353. [PMID: 24647662]
Accepted name: 1,3-α-oligoglucan phosphorylase
Reaction: [(1→3)-α-D-glucosyl]n + phosphate = [(1→3)-α-D-glucosyl]n-1 + β-D-glucose 1-phosphate
Systematic name: 1,3-α-D-glucan:phosphate β-D-glucosyltransferase
Comments: The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyses a reversible reaction. Substrates for the phosphorolytic reaction are α-1,3-linked oligoglucans with a polymerisation degree of 3 or more. Nigerose (i.e. 3-O-α-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279, nigerose phosphorylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Nihira, T., Nishimoto, M., Nakai, H., Ohtsubo, K., and Kitaoka, M. Characterization of two phosphorylases for α-1,3-oligoglucans from Clostridium phytofermentans. J. Appl. Glycosci. 61 (2014) 59-66.
Accepted name: dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase
Reaction: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate + an archaeal dolichyl N-acetyl-α-D-glucosaminyl phosphate = UDP + an archaeal dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-β-D-glucuronsyl)-N-acetyl-α-D-glucosaminyl phosphate
Other name(s): AglC; UDP-Glc-2,3-diNAcA glycosyltransferase
Systematic name: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate:dolichyl N-acetyl-α-D-glucosaminyl-phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase
Comments: The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, participates in the N-glycosylation of proteins. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367-373. [PMID: 23624439]
Accepted name: monoglucosyldiacylglycerol synthase
Reaction: UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol
Glossary: a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = a β-monoglucosyldiacylglycerol = a GlcDG
Other name(s): mgdA (gene name)
Systematic name: UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-β-D-glucosyltransferase
Comments: The enzymes from cyanobacteria are involved in the biosynthesis of galactolipids found in their photosynthetic membranes. The enzyme belongs to the GT2 family of configuration-inverting glycosyltranferases [2]. cf. EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sato, N. and Murata, N. Lipid biosynthesis in the blue-green-alga (cyanobacterium), Anabaena variabilis. 3. UDP-glucose-diacylglycerol glucosyltransferase activity in vitro. Plant Cell Physiol. 23 (1982) 1115-1120.
2. Awai, K., Kakimoto, T., Awai, C., Kaneko, T., Nakamura, Y., Takamiya, K., Wada, H. and Ohta, H. Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria. Plant Physiol. 141 (2006) 1120-1127. [PMID: 16714404]
3. Yuzawa, Y., Shimojima, M., Sato, R., Mizusawa, N., Ikeda, K., Suzuki, M., Iwai, M., Hori, K., Wada, H., Masuda, S. and Ohta, H. Cyanobacterial monogalactosyldiacylglycerol-synthesis pathway is involved in normal unsaturation of galactolipids and low-temperature adaptation of Synechocystis sp. PCC 6803. Biochim. Biophys. Acta 1841 (2014) 475-483. [PMID: 24370445]
Accepted name: 1,2-diacylglycerol 3-α-glucosyltransferase
Reaction: UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol
Other name(s): mgs (gene name); UDP-glucose:diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol glucosyltransferase; uridine diphosphoglucose-diacylglycerol glucosyltransferase; UDP-glucose-diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol 3-D-glucosyltransferase; UDP-glucose:1,2-diacyl-sn-glycerol 3-D-glucosyltransferase; 1,2-diacylglycerol 3-glucosyltransferase (ambiguous)
Systematic name: UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-α-D-glucosyltransferase
Comments: The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC 2.4.1.336, monoglucosyldiacylglycerol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Karlsson, O.P., Dahlqvist, A., Vikstrom, S. and Wieslander, A. Lipid dependence and basic kinetics of the purified 1,2-diacylglycerol 3-glucosyltransferase from membranes of Acholeplasma laidlawii. J. Biol. Chem. 272 (1997) 929-936. [PMID: 8995384]
2. Li, L., Storm, P., Karlsson, O.P., Berg, S. and Wieslander, A. Irreversible binding and activity control of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer surface. Biochemistry 42 (2003) 9677-9686. [PMID: 12911309]
3. Berg, S., Edman, M., Li, L., Wikstrom, M. and Wieslander, A. Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes. Recognition of a large group of lipid glycosyltransferases in eubacteria and archaea. J. Biol. Chem. 276 (2001) 22056-22063. [PMID: 11294844]
4. Semeniuk, A., Sohlenkamp, C., Duda, K. and Holzl, G. A bifunctional glycosyltransferase from Agrobacterium tumefaciens synthesizes monoglucosyl and glucuronosyl diacylglycerol under phosphate deprivation. J. Biol. Chem. 289 (2014) 10104-10114. [PMID: 24558041]
Accepted name: validoxylamine A glucosyltransferase
Reaction: UDP-α-D-glucose + validoxylamine A = UDP + validamycin A
For diagram of reaction click here.
Glossary: validoxylamine A = (1S,2S,3R,6S)-4-(hydroxymethyl)-6-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol
Other name(s): vldK (gene name); valG (gene name)
Systematic name: UDP-α-D-glucose:validoxylamine-A D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bai, L., Li, L., Xu, H., Minagawa, K., Yu, Y., Zhang, Y., Zhou, X., Floss, H.G., Mahmud, T. and Deng, Z. Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A. Chem. Biol. 13 (2006) 387-397. [PMID: 16632251]
2. Xu, H., Minagawa, K., Bai, L., Deng, Z. and Mahmud, T. Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4''-epi-validamycin A. J Nat Prod 71 (2008) 1233-1236. [PMID: 18563934]
Accepted name: β-1,2-mannobiose phosphorylase
Reaction: β-D-mannopyranosyl-(1→2)-D-mannopyranose + phosphate = D-mannopyranose + α-D-mannose 1-phosphate
Systematic name: β-D-mannopyranosyl-(1→2)-D-mannopyranose:phosphate α-D-mannosyltransferase
Comments: The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. cf. EC 2.4.1.340, 1,2-β-oligomannan phosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Chiku, K., Nihira, T., Suzuki, E., Nishimoto, M., Kitaoka, M., Ohtsubo, K. and Nakai, H. Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514. PLoS One 9 (2014) e114882. [PMID: 25500577]
2. Tsuda, T., Nihira, T., Chiku, K., Suzuki, E., Arakawa, T., Nishimoto, M., Kitaoka, M., Nakai, H. and Fushinobu, S. Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from Listeria innocua. FEBS Lett. 589 (2015) 3816-3821. [PMID: 26632508]
Accepted name: 1,2-β-oligomannan phosphorylase
Reaction: [(1→2)-β-D-mannosyl]n + phosphate = [(1→2)-β-D-mannosyl]n-1 + α-D-mannose 1-phosphate
Systematic name: (1→2)-β-D-mannan:phosphate β-D-mannosyl transferase (configuration-inverting)
Comments: The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. In the synthetic direction it produces oligosaccharides with a degree of polymerization (DP) of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues. cf. EC 2.4.1.339, β-1,2-mannobiose phosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Chiku, K., Nihira, T., Suzuki, E., Nishimoto, M., Kitaoka, M., Ohtsubo, K. and Nakai, H. Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514. PLoS One 9 (2014) e114882. [PMID: 25500577]
Accepted name: α-1,2-colitosyltransferase
Reaction: GDP-β-L-colitose + β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = GDP + α-L-colitosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-D-glucosamine
Glossary: β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = lacto-N-biose
Other name(s): wbgN (gene name)
Systematic name: GDP-β-L-colitose:β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine L-colitosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the bacterium Escherichia coli O55:H7, participates in the biosynthesis of an O-antigen. The reaction involves anomeric inversion, and does not require any metal ions. The enzyme is highly specific towards the acceptor, exclusively recognizing lacto-N-biose, but can accept GDP-L-fucose as the donor with almost the same activity as with GDP-β-L-colitose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wu, Z., Zhao, G., Li, T., Qu, J., Guan, W., Wang, J., Ma, C., Li, X., Zhao, W., Wang, P.G. and Li, L. Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. Glycobiology (2015) . [PMID: 26703456]
Accepted name: α-maltose-1-phosphate synthase
Reaction: ADP-α-D-glucose + α-D-glucose-1-phosphate = ADP + α-maltose-1-phosphate
Glossary: maltose = α-D-glucopyranosyl-(1→4)-D-glucose
Other name(s): glgM (gene name)
Systematic name: ADP-α-D-glucose:α-D-glucose-1-phosphate 4-α-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme, found in Mycobacteria, can also use UDP-α-D-glucose with much lower catalytic efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Koliwer-Brandl, H., Syson, K., van de Weerd, R., Chandra, G., Appelmelk, B., Alber, M., Ioerger, T.R., Jacobs, W.R., Jr., Geurtsen, J., Bornemann, S. and Kalscheuer, R. Metabolic network for the biosynthesis of intra- and extracellular α-glucans required for virulence of Mycobacterium tuberculosis. PLoS Pathog. 12 (2016) e1005768. [PMID: 27513637]
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): wclR (gene name)
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-galactosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O3. Requires a divalent metal ion (Mn2+, Mg2+ or Fe2+). cf. EC 2.4.1.303, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Chen, C., Liu, B., Xu, Y., Utkina, N., Zhou, D., Danilov, L., Torgov, V., Veselovsky, V. and Feng, L. Biochemical characterization of the novel α-1, 3-galactosyltransferase WclR from Escherichia coli O3. Carbohydr. Res. 430 (2016) 36-43. [PMID: 27196310]
Accepted name: type 2 galactoside α-(1,2)-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase (ambiguous); α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); H-gene-encoded β-galactoside α(1→2)fucosyltransferase; β-galactoside α(1→2)fucosyltransferase (ambiguous); GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT1 (gene name); FUT2 (gene name)
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)
Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956-2962. [PMID: 804484]
2. Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351-353.
3. Ernst, L.K., Rajan, V.P., Larsen, R.D., Ruff, M.M. and Lowe, J.B. Stable expression of blood group H determinants and GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264 (1989) 3436-3447. [PMID: 2464598]
4. Larsen, R.D., Ernst, L.K., Nair, R.P. and Lowe, J.B. Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc. Natl. Acad. Sci. USA 87 (1990) 6674-6678. [PMID: 2118655]
Accepted name: phosphatidyl-myo-inositol α-mannosyltransferase
Reaction: GDP-α-D-mannose + 1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns
Other name(s): mannosyltransferase PimA; PimA; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase (ambiguous)
Systematic name: GDP-α-D-mannose:1-phosphatidyl-1D-myo-inositol 2-α-D-mannosyltransferase (configuration-retaining)
Comments: Requires Mg2+. 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. Kordulakova, J., Gilleron, M., Mikusova, K., Puzo, G., Brennan, P.J., Gicquel, B. and Jackson, M. Definition of the first mannosylation step in phosphatidylinositol mannoside synthesis. PimA is essential for growth of mycobacteria. J. Biol. Chem. 277 (2002) 31335-31344. [PMID: 12068013]
2. Gu, X., Chen, M., Wang, Q., Zhang, M., Wang, B. and Wang, H. Expression and purification of a functionally active recombinant GDP-mannosyltransferase (PimA) from Mycobacterium tuberculosis H37Rv. Protein Expr. Purif. 42 (2005) 47-53. [PMID: 15939292]
3. Giganti, D., Albesa-Jove, D., Urresti, S., Rodrigo-Unzueta, A., Martinez, M.A., Comino, N., Barilone, N., Bellinzoni, M., Chenal, A., Guerin, M.E. and Alzari, P.M. Secondary structure reshuffling modulates glycosyltransferase function at the membrane. Nat. Chem. Biol. 11 (2015) 16-18. [PMID: 25402770]
4. Rodrigo-Unzueta, A., Martinez, M.A., Comino, N., Alzari, P.M., Chenal, A. and Guerin, M.E. Molecular basis of membrane association by the phosphatidylinositol mannosyltransferase PimA enzyme from Mycobacteria. J. Biol. Chem. 291 (2016) 13955-13963. [PMID: 27189944]
Accepted name: phosphatidyl-myo-inositol dimannoside synthase
Reaction: (1) GDP-α-D-mannose + 2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = GDP + 2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2) GDP-α-D-mannose + 2-O-(6-O-acyl-α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(6-O-acyl-α-D-mannosyl)-6-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns
Other name(s): mannosyltransferase PimB; PimB; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase (ambiguous)
Systematic name: GDP-α-D-mannose:2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol 6-α-D-mannosyltransferase (configuration-retaining)
Comments: Requires Mg2+. 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. Guerin, M.E., Kaur, D., Somashekar, B.S., Gibbs, S., Gest, P., Chatterjee, D., Brennan, P.J. and Jackson, M. New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis. J. Biol. Chem. 284 (2009) 25687-25696. [PMID: 19638342]
2. Mishra, A.K., Batt, S., Krumbach, K., Eggeling, L. and Besra, G.S. Characterization of the Corynebacterium glutamicum Δ pimB' Δ mgtA double deletion mutant and the role of Mycobacterium tuberculosis orthologues Rv2188c and Rv0557 in glycolipid biosynthesis. J. Bacteriol. 191 (2009) 4465-4472. [PMID: 19395496]
3. Batt, S.M., Jabeen, T., Mishra, A.K., Veerapen, N., Krumbach, K., Eggeling, L., Besra, G.S. and Futterer, K. Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'. J. Biol. Chem. 285 (2010) 37741-37752. [PMID: 20843801]
Accepted name: α,α-trehalose-phosphate synthase (ADP-forming)
Reaction: ADP-α-D-glucose + D-glucose 6-phosphate = ADP + α,α-trehalose 6-phosphate
Other name(s): otsA (gene name); ADP-glucose —glucose-phosphate glucosyltransferase
Systematic name: ADP-α-D-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme has been reported from the yeast Saccharomyces cerevisiae and from mycobacteria. The enzyme from Mycobacterium tuberculosis can also use UDP-α-D-glucose, but the activity with ADP-α-D-glucose, which is considered the main substrate in vivo, is higher.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number:
References:
1. Ferreira, J.C., Thevelein, J.M., Hohmann, S., Paschoalin, V.M., Trugo, L.C. and Panek, A.D. Trehalose accumulation in mutants of Saccharomyces cerevisiae deleted in the UDPG-dependent trehalose synthase-phosphatase complex. Biochim. Biophys. Acta 1335 (1997) 40-50. [PMID: 9133641]
2. Pan, Y.T., Carroll, J.D. and Elbein, A.D. Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme. Eur. J. Biochem. 269 (2002) 6091-6100. [PMID: 12473104]
3. Asencion Diez, M.D., Demonte, A.M., Syson, K., Arias, D.G., Gorelik, A., Guerrero, S.A., Bornemann, S. and Iglesias, A.A. Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis. Biochim. Biophys. Acta 1850 (2015) 13-21. [PMID: 25277548]
Accepted name: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase
Reaction: GDP-α-D-mannose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = GDP + α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdC
Systematic name: GDP-α-D-mannose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the biosynthesis of the linker region of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotypes O8, O9 and O9a.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078-35091. [PMID: 22875852]
Accepted name: mannosyl-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase
Reaction: 2 GDP-α-D-mannose + α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = 2 GDP + α-D-mannosyl-(1→3)-α-D-mannosyl-(1→3)-α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdB
Systematic name: GDP-α-D-mannose:α-D-mannosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the biosynthesis of the linker region of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotypes O8, O9 and O9a. It has no activity with N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.4.1.348, N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078-35091. [PMID: 22875852]
Accepted name: mogroside IE synthase
Reaction: UDP-α-D-glucose + mogrol = mogroside IE + UDP
Glossary: mogrol = (23R)-cucurbit-5-ene-3β,11α,23,25-tetraol
Other name(s): UGT74AC1; mogrol C-3 hydroxyl glycosyltransferase
Systematic name: UDP-α-D-glucose:mogrol 3-O-glucosyltransferase
Comments: Isolated from the plant Siraitia grosvenorii (monk fruit).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Dai, L., Liu, C., Zhu, Y., Zhang, J., Men, Y., Zeng, Y. and Sun, Y. Functional characterization of cucurbitadienol synthase and triterpene glycosyltransferase involved in biosynthesis of mogrosides from Siraitia grosvenorii. Plant Cell Physiol 56 (2015) 1172-1182. [PMID: 25759326]
Accepted name: rhamnogalacturonan I rhamnosyltransferase
Reaction: UDP-β-L-rhamnose + α-D-galacturonosyl-[(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n = UDP + [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n+1
Other name(s): RRT; RG I rhamnosyltransferase
Systematic name: UDP-β-L-rhamnose:rhamnogalacturonan I 4-rhamnosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan type I. It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 7.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Uehara, Y., Tamura, S., Maki, Y., Yagyu, K., Mizoguchi, T., Tamiaki, H., Imai, T., Ishii, T., Ohashi, T., Fujiyama, K. and Ishimizu, T. Biochemical characterization of rhamnosyltransferase involved in biosynthesis of pectic rhamnogalacturonan I in plant cell wall. Biochem. Biophys. Res. Commun. 486 (2017) 130-136. [PMID: 28283389]
Accepted name: glucosylglycerate phosphorylase
Reaction: 2-O-(α-D-glucopyranosyl)-D-glycerate + phosphate = α-D-glucopyranose 1-phosphate + D-glycerate
Systematic name: 2-O-(α-D-glucopyranosyl)-D-glycerate:phosphate α-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme has been characterized from the bacterium Meiothermus silvanus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Franceus, J., Pinel, D. and Desmet, T. Glucosylglycerate phosphorylase, an enzyme with novel specificity involved in compatible solute metabolism. Appl. Environ. Microbiol. 83 (2017) . [PMID: 28754708]
Accepted name: sordaricin 6-deoxyaltrosyltransferase
Reaction: GDP-6-deoxy-α-D-altrose + sordaricin = 4'-O-demethylsordarin + GDP
For diagram of reaction click here.
Glossary: sordaricin = (1R,3aR,4S,4aR,7R,7aR,8aR)-4-formyl-8a-(hydroxymethyl)-7-methyl-3-(propan-2-yl)-1,3a,4,4a,5,6,7,7a,8,8-decahydro-1,4-methanocyclopenta[f]indene-3a-carboxylic acid
Other name(s): SdnJ
Systematic name: GDP-6-deoxy-α-D-altrose:sordaricin 6-deoxy-D-altrosyltransferase
Comments: The enzyme, isolated from the fungus Sordaria araneosa, is involved in the biosynthesis of the glycoside antibiotic sordarin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kudo, F., Matsuura, Y., Hayashi, T., Fukushima, M. and Eguchi, T. Genome mining of the sordarin biosynthetic gene cluster from Sordaria araneosa Cain ATCC 36386: characterization of cycloaraneosene synthase and GDP-6-deoxyaltrose transferase. J. Antibiot. (Tokyo) 69 (2016) 541-548. [PMID: 27072286]
Accepted name: (R)-mandelonitrile β-glucosyltransferase
Reaction: UDP-α-D-glucose + (R)-mandelonitrile = UDP + (R)-prunasin
Glossary: (R)-mandelonitrile = (2R)-hydroxy(phenyl)acetonitrile
(R)-prunasin = (2R)-(β-D-glucosyloxy)(phenyl)acetonitrile
Other name(s): UGT85A19 (gene name)
Systematic name: UDP-α-D-glucose:(R)-mandelonitrile β-D-glucosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from Prunus dulcis (almond), is involved in the biosynthesis of the cyanogenic glycosides (R)-prunasin and (R)-amygdalin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Franks, T. K., Yadollahi, A., Wirthensohn, M. G., Guerin, J. R., Kaiser, B. N., Sedgley, M. and Ford, C. M. A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond (Prunus dulcis) kernels. Funct. Plant Biol. 35 (2008) 236-246.
Accepted name: poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase
Reaction: n UDP-N-acetyl-α-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-β-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TarS
Systematic name: UDP-N-acetyl-α-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of poly(ribitol-phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-β-D-glucosamine to the OH group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.70 [poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Nathenson, S. G., Strominger, J. L. Enzymatic synthesis of N-acetylglucosaminylribitol linkages in teichoic acid from Staphylococcus aureus, strain Copenhagen. J. Biol. Chem. 238 (1963) 3161-3169. [PMID: 14085356]
2. Brown, S., Xia, G., Luhachack, L.G., Campbell, J., Meredith, T.C., Chen, C., Winstel, V., Gekeler, C., Irazoqui, J.E., Peschel, A. and Walker, S. Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids. Proc. Natl Acad. Sci. USA 109 (2012) 18909-18914. [PMID: 23027967]
3. Sobhanifar, S., Worrall, L.J., King, D.T., Wasney, G.A., Baumann, L., Gale, R.T., Nosella, M., Brown, E.D., Withers, S.G. and Strynadka, N.C. Structure and mechanism of Staphylococcus aureus TarS, the wall teichoic acid β-glycosyltransferase involved in methicillin resistance. PLoS Pathog. 12 (2016) e1006067. [PMID: 27973583]
Accepted name: glucosyl-dolichyl phosphate glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + an archaeal dolichyl α-D-glucosyl phosphate = UDP + an archaeal dolichyl β-D-glucuronosyl-(1→4)-α-D-glucosyl phosphate
Other name(s): aglG (gene name)
Systematic name: UDP-α-D-glucuronate:dolichyl phosphate glucuronosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the halophilic archaeon Haloferax volcanii, participates in the protein N-glycosylation pathway. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60) and is α,ω-saturated. However, in vitro the enzyme was also able to act on a substrate with an unsaturated end.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H.R., Hitchen, P.G., Dell, A. and Eichler, J. aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol. Microbiol. 69 (2008) 1234-1245. [PMID: 18631242]
2. Elharar, Y., Podilapu, A.R., Guan, Z., Kulkarni, S.S. and Eichler, J. Assembling glycan-charged dolichol phosphates: chemoenzymatic synthesis of a Haloferax volcanii N-glycosylation pathway intermediate. Bioconjug Chem 28 (2017) 2461-2470. [PMID: 28809486]
Accepted name: phlorizin synthase
Reaction: UDP-α-D-glucose + phloretin = UDP + phlorizin
For diagram of reaction click here.
Glossary: phloretin = 3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)propan-1-one
phlorizin = 3-(4-hydroxyphenyl)-1-[2-(β-D-glucopyranosyloxy)-4,6-dihydroxyphenyl]propan-1-one
Other name(s): MdPGT1: P2’GT
Systematic name: UDP-α-D-glucose:phloretin 2'-O-D-glucosyltransferase
Comments: Isolated from Malus X domestica (apple). Phlorizin inhibits sodium-linked glucose transporters. It gives the characteristic flavour of apples and cider.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Jugdé, H., Nguy, D., Moller, I., Cooney, J.M. and Atkinson, R.G. Isolation and characterization of a novel glycosyltransferase that converts phloretin to phlorizin, a potent antioxidant in apple. FEBS J. 275 (2008) 3804-3814. [PMID: 18573104]
2. Yahyaa, M., Davidovich-Rikanati, R., Eyal, Y., Sheachter, A., Marzouk, S., Lewinsohn, E. and Ibdah, M. Identification and characterization of UDP-glucose:Phloretin 4'-O-glycosyltransferase from Malus x domestica Borkh. Phytochemistry 130 (2016) 47-55. [PMID: 27316677]
Accepted name: acylphloroglucinol glucosyltransferase
Reaction: UDP-α-D-glucose + 2-acylphloroglucinol = UDP + 2-acylphloroglucinol 1-O-β-D-glucoside
For diagram of reaction click here.
Glossary: phlorisobutyrophenone = 2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one
Other name(s): UGT71K3
Systematic name: UDP-α-D-glucose:2-acylphloroglucinol 1-O-β-glucosyltransferase
Comments: Isolated from strawberries (Fragaria × ananassa). Acts best on phloroisovalerophenone and phlorobutyrophenone but will also glycosylate many other phenolic compounds. A minor product of the reaction is the 5-O-β-D-glucoside
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Song, C., Zhao, S., Hong, X., Liu, J., Schulenburg, K. and Schwab, W. A UDP-glucosyltransferase functions in both acylphloroglucinol glucoside and anthocyanin biosynthesis in strawberry (Fragaria × ananassa). Plant J. 85 (2016) 730-742. [PMID: 26859691]
Accepted name: glucosylglycerol phosphorylase (configuration-retaining)
Reaction: 2-O-α-D-glucopyranosyl-glycerol + phosphate = α-D-glucose 1-phosphate + glycerol
Other name(s): 2-O-α-D-glucosylglycerol phosphorylase (retaining)
Systematic name: 2-O-α-D-glucopyranosyl-glycerol:phosphate α-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-α-D-glucopyranosyl-glycerol when the environmental salt concentration decreases. cf. EC 2.4.1.332, 1,2-α-glucosylglycerol phosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Franceus, J., Decuyper, L., D'hooghe, M. and Desmet, T. Exploring the sequence diversity in glycoside hydrolase family 13_18 reveals a novel glucosylglycerol phosphorylase. Appl. Microbiol. Biotechnol. (2018) . [PMID: 29470619]
Accepted name: 2-hydroxyflavanone C-glucosyltransferase
Reaction: UDP-α-D-glucose + a 2'-hydroxy-β-oxodihydrochalcone = UDP + a 3'-(β-D-glucopyranosyl)-2'-hydroxy-β-oxodihydrochalcone
For diagram of reaction click here
Glossary: 2'-hydroxy-β-oxodihydrochalcone = 1-(2-hydroxyphenyl)-3-phenypropan-1,3-dione
3'-(β-D-glucopyranosyl)-2'-hydroxy-β-oxodihydrochalcone = 1-(3-(β-D-glucopyranosyl)-2-hydroxyphenyl)-3-phenylpropan-1,3-dione
Other name(s): OsCGT
Systematic name: UDP-α-D-glucose:2'-hydroxy-β-oxodihydrochalcone C6/8-β-D-glucosyltransferase
Comments: The enzyme has been characterized in Oryza sativa (rice), various Citrus spp., Glycine max (soybean), and Fagopyrum esculentum (buckwheat). Flavanone substrates require a 2-hydroxy group. The meta-stable flavanone substrates such as 2-hydroxynaringenin exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione, which are the actual substrates for the glucosyl-transfer reaction (see EC 1.14.14.162, flavanone 2-hydroxylase). The enzyme can also act on dihydrochalcones. The enzymes from citrus plants can catalyse a second C-glycosylation reaction at position 5.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Brazier-Hicks, M., Evans, K.M., Gershater, M.C., Puschmann, H., Steel, P.G. and Edwards, R. The C-glycosylation of flavonoids in cereals. J. Biol. Chem. 284 (2009) 17926-17934. [PMID: 19411659]
2. Nagatomo, Y., Usui, S., Ito, T., Kato, A., Shimosaka, M. and Taguchi, G. Purification, molecular cloning and functional characterization of flavonoid C-glucosyltransferases from Fagopyrum esculentum M. (buckwheat) cotyledon. Plant J. 80 (2014) 437-448. [PMID: 25142187]
3. Hirade, Y., Kotoku, N., Terasaka, K., Saijo-Hamano, Y., Fukumoto, A. and Mizukami, H. Identification and functional analysis of 2-hydroxyflavanone C-glucosyltransferase in soybean (Glycine max). FEBS Lett. 589 (2015) 1778-1786. [PMID: 25979175]
4. Ito, T., Fujimoto, S., Suito, F., Shimosaka, M. and Taguchi, G. C-Glycosyltransferases catalyzing the formation of di-C-glucosyl flavonoids in citrus plants. Plant J. 91 (2017) 187-198. [PMID: 28370711]
Accepted name: GDP-mannose:di-myo-inositol-1,3'-phosphate β-1,2-mannosyltransferase
Reaction: 2 GDP-α-D-mannose + bis(myo-inositol) 1,3'-phosphate = 2 GDP + 2-O-(β-D-mannosyl-(1→2)-β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate (overall reaction)
(1a) GDP-α-D-mannose + bis(myo-inositol) 1,3'-phosphate = GDP + 2-O-(β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate
(1b) GDP-α-D-mannose + 2-O-(β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate = GDP + 2-O-(β-D-mannosyl-(1→2)-β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate
Other name(s): MDIP synthase
Systematic name: GDP-α-D-mannose:bis(myo-inositol)-1,3'-phosphate 2-β-D-mannosyltransferase
Comments: The enzyme from the hyperthermophilic bacterium Thermotoga maritima is involved in the synthesis of the solutes 2-O-(β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate and 2-O-(β-D-mannosyl-(1→2)-β-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Rodrigues, M.V., Borges, N., Almeida, C.P., Lamosa, P. and Santos, H. A unique β-1,2-mannosyltransferase of Thermotoga maritima that uses di-myo-inositol phosphate as the mannosyl acceptor. J. Bacteriol. 191 (2009) 6105-6115. [PMID: 19648237]
Accepted name: α-(1→3) branching sucrase
Reaction: sucrose + a (1→6)-α-D-glucan = D-fructose + a (1→6)-α-D-glucan containing a (1→3)-α-D-glucose branch
Other name(s): branching sucrase A; BRS-A; brsA (gene name)
Systematic name: sucrose:(1→6)-α-D-glucan 3-α-D-[(1→3)-α-D-glucosyl]-transferase
Comments: The enzyme from Leuconostoc spp. is responsible for producing α-(1→3) branches in α-(1→6) glucans by transferring the glucose residue from fructose to a 3-hydroxyl group of a glucan.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Vuillemin, M., Claverie, M., Brison, Y., Severac, E., Bondy, P., Morel, S., Monsan, P., Moulis, C. and Remaud-Simeon, M. Characterization of the first α-(1→3) branching sucrases of the GH70 family. J. Biol. Chem 291 (2016) 7687-7702. [PMID: 26763236]
2. Moulis, C., Andre, I. and Remaud-Simeon, M. GH13 amylosucrases and GH70 branching sucrases, atypical enzymes in their respective families. Cell. Mol. Life Sci. 73 (2016) 2661-2679. [PMID: 27141938]
Accepted name: ginsenoside 20-O-glucosyltransferase
Reaction: UDP-α-D-glucose + (20S)-protopanaxadiol = UDP + ginsenoside C-K
For diagram of reaction click here
Glossary: (20S)-protopanaxadiol = (3β,12β)-dammar-24-ene-3,12,20-triol
ginsenoside C-K = (3β,12β)-3,12-dihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGT71A27 (gene name)
Systematic name: UDP-α-D-glucose:(20S)-protopanaxadiol 20-O-glucosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C20(S)-OH group of dammarane derivative substrates, including protopanaxatriol, dammarenediol II, (20S)-ginsenoside Rh2, and (20S)-ginsenoside Rg3. It does not act on the 20R epimer of protopanaxadiol, or on ginsenosides that are glucosylated at the C-6 position, such as ginsenoside Rh1 or ginsenoside Rg2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yan, X., Fan, Y., Wei, W., Wang, P., Liu, Q., Wei, Y., Zhang, L., Zhao, G., Yue, J. and Zhou, Z. Production of bioactive ginsenoside compound K in metabolically engineered yeast. Cell Res 24 (2014) 770-773. [PMID: 24603359]
2. Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412-1424. [PMID: 26032089]
Accepted name: protopanaxadiol-type ginsenoside 3-O-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + (20S)-protopanaxadiol = UDP + (20S)-ginsenoside Rh2
(2) UDP-α-D-glucose + ginsenoside C-K = UDP + ginsenoside F2
For diagram of reaction click here
Glossary: (20S)-protopanaxadiol = (3β,12β)-dammar-24-ene-3,12,20-triol
ginsenoside C-K = (3β,12β)-3,12-dihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGT74AE2 (gene name)
Systematic name: UDP-α-D-glucose:protopanaxadiol-type ginsenoside 3-O-glucosyltransferase (configuration-retaining)
Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C-3-OH group of (20S)-protopanaxadiol and ginsenoside C-K.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Jung, S.C., Kim, W., Park, S.C., Jeong, J., Park, M.K., Lim, S., Lee, Y., Im, W.T., Lee, J.H., Choi, G. and Kim, S.C. Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd. Plant Cell Physiol 55 (2014) 2177-2188. [PMID: 25320211]
Accepted name: protopanaxadiol-type ginsenoside-3-O-glucoside 2"-O-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + (20S)-ginsenoside Rh2 = UDP + (20S)-ginsenoside Rg3
(2) UDP-α-D-glucose + ginsenoside F2 = UDP + ginsenoside Rd
For diagram of reaction click here
Glossary: (20S)-ginsenoside Rh2 = (3β,12β)-12,20-dihydroxydammar-24-en-3-yl β-D-glucopyranoside
ginsenoside F2 = (3β,12β)-20-(β-D-glucopyranosyloxy)-12-hydroxydammar-24-en-3-yl β-D-glucopyranoside
Other name(s): UGT94Q2 (gene name)
Systematic name: UDP-α-D-glucose:3-O-glucosyl-protopanaxadiol-type ginsenoside 2"-O-glucosyltransferase
Comments: The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the 2" position of the glucose moiety in the protopanaxadiol-type ginsenoside-3-O-glucosides (20S)-ginsenoside Rh2 and ginsenoside F2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Jung, S.C., Kim, W., Park, S.C., Jeong, J., Park, M.K., Lim, S., Lee, Y., Im, W.T., Lee, J.H., Choi, G. and Kim, S.C. Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd. Plant Cell Physiol 55 (2014) 2177-2188. [PMID: 25320211]
Accepted name: ginsenoside F1 6-O-glucosyltransferase
Reaction: UDP-α-D-glucose + ginsenoside F1 = UDP + (20S)-ginsenoside Rg1
For diagram of reaction click here
Glossary: ginsenoside F1 = 3β,6α,12β-trihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGTPg101 (gene name)
Systematic name: UDP-α-D-glucose:ginsenoside F1 6-O-glucosyltransferase
Comments: The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of ginsenoside F1. The enzyme also glucosylates the C-20 position of protopanaxatriol, which forms ginsenoside F1 (cf. EC 2.4.1.363, ginsenoside 20-O-glucosyltransferase). However, unlike EC 2.4.1.367, ginsenoside 6-O-glucosyltransferase, it is not able to glucosylate the C-6 position of protopanaxatriol when position C-20 is not glucosylated.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412-1424. [PMID: 26032089]
Accepted name: ginsenoside 6-O-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + protopanaxatriol = UDP + ginsenoside Rh1
(2) UDP-α-D-glucose + ginsenoside F1 = UDP + (20S)-ginsenoside Rg1
For diagram of reaction click here
Glossary: protopanaxatriol = (3β,6α,12β)-dammar-24-ene-3,6,12,20-tetrol
ginsenoside F1 = (3β,6α,12β)-trihydroxydammar-24-en-20-yl β-D-glucopyranoside
Other name(s): UGTPg100 (gene name)
Systematic name: UDP-α-D-glucose:ginsenoside 6-O-glucosyltransferase
Comments: The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of protopanaxatriol and ginsenoside F1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wei, W., Wang, P., Wei, Y., Liu, Q., Yang, C., Zhao, G., Yue, J., Yan, X. and Zhou, Z. Characterization of Panax ginseng UDP-glycosyltransferases catalyzing protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in metabolically engineered yeasts. Mol. Plant 8 (2015) 1412-1424. [PMID: 26032089]
Accepted name: oleanolate 3-O-glucosyltransferase
Reaction: UDP-α-D-glucose + oleanolate = UDP + oleanolate 3-O-β-D-glucoside
Glossary: oleanolate = 3β-hydroxyolean-12-en-28-oate
Other name(s): UGT73C10 (gene name); UGT73C11 (gene name)
Systematic name: UDP-α-D-glucose:oleanolate 3-O-glucosyltransferase
Comments: The enzyme has been characterized from the saponin-producing crucifer plant Barbarea vulgaris.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Augustin, J.M., Drok, S., Shinoda, T., Sanmiya, K., Nielsen, J.K., Khakimov, B., Olsen, C.E., Hansen, E.H., Kuzina, V., Ekstrom, C.T., Hauser, T. and Bak, S. UDP-glycosyltransferases from the UGT73C subfamily in Barbarea vulgaris catalyze sapogenin 3-O-glucosylation in saponin-mediated insect resistance. Plant Physiol. 160 (2012) 1881-1895. [PMID: 23027665]
Accepted name: enterobactin C-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + enterobactin = UDP + monoglucosyl-enterobactin
(2) UDP-α-D-glucose + monoglucosyl-enterobactin = UDP + diglucosyl-enterobactin
(3) UDP-α-D-glucose + diglucosyl-enterobactin = UDP + triglucosyl-enterobactin
For diagram of reaction, click here
Glossary: enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone
monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-3→1(3)-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE
diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = salmochelin S4 = di-C-glucosyl-enterobactin
triglucosyl-enterobactin = N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = tri-C-glucosyl-enterobactin = salmochelin TGE
Other name(s): iroB (gene name)
Systematic name: UDP-α-D-glucose:enterobactin 5'-C-β-D-glucosyltransferase (configuration-inverting)
Comments: The enzyme, found in pathogenic strains of the bacteria Escherichia coli and Salmonella enterica, catalyses the transfer of glucosyl groups to C-5 of one, two, or three of the 2,3-hydroxybenzoyl units of the siderophore enterobactin, forming C-glucosylated derivatives known as salmochelins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Fischbach, M.A., Lin, H., Liu, D.R. and Walsh, C.T. In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase. Proc. Natl Acad. Sci. USA 102 (2005) 571-576. [PMID: 15598734]
Accepted name: inositol phosphorylceramide mannosyltransferase
Reaction: GDP-α-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide = a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
Glossary: a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide = a very-long-chain mannosylinositol phospho-α-hydroxyphytoceramide = MIPC
Other name(s): SUR1 (gene name); CSH1 (gene name)
Systematic name: GDP-α-D-mannose:inositol phospho-(2'R)-2'-hydroxyphytoceramide mannosyltransferase
Comments: The simplest complex sphingolipid of yeast, inositol-phospho-α-hydroxyphytoceramide (IPC), is usually mannosylated to yield mannosyl-inositol-phospho-α hydroxyphytoceramide (MIPC). The enzyme is located in the Golgi apparatus, and utilizes GDP-mannose as the mannosyl group donor. It consists of a catalytic subunit (SUR1 or CSH1) and a regulatory subunit (CSG2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Beeler, T.J., Fu, D., Rivera, J., Monaghan, E., Gable, K. and Dunn, T.M. SUR1 (CSG1/BCL21), a gene necessary for growth of Saccharomyces cerevisiae in the presence of high Ca2+ concentrations at 37 degrees C, is required for mannosylation of inositolphosphorylceramide. Mol. Gen. Genet. 255 (1997) 570-579. [PMID: 9323360]
2. Dean, N., Zhang, Y.B. and Poster, J.B. The VRG4 gene is required for GDP-mannose transport into the lumen of the Golgi in the yeast, Saccharomyces cerevisiae. J. Biol. Chem 272 (1997) 31908-31914. [PMID: 9395539]
3. Uemura, S., Kihara, A., Inokuchi, J. and Igarashi, Y. Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p. J. Biol. Chem 278 (2003) 45049-45055. [PMID: 12954640]
Accepted name: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosylpolymerase
Reaction: (1) 2 GDP-α-D-mannose + [α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = 2 GDP + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
(2) 2 GDP-α-D-mannose + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = 2 GDP + [α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n+1-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdA
Systematic name: GDP-α-D-mannose:α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the biosynthesis of polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. The enzymes consists of two domains that are responsible for the 1→2 and 1→3 linkages, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078-35091. [PMID: 22875852]
2. Greenfield, L.K., Richards, M.R., Vinogradov, E., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens. J. Biol. Chem. 287 (2012) 38135-38149. [PMID: 22989876]
3. Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075-1085. [PMID: 25422321]
Accepted name: mutansucrase
Reaction: sucrose + [(1→3)-α-D-glucosyl]n = D-fructose + [(1→3)-α-D-glucosyl]n+1
Other name(s): gtfJ (gene name)
Systematic name: sucrose:(1→3)-α-D-glucan 3-α-D-glucosyltransferase
Comments: The glucansucrases transfer a D-glusosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. Currently classified glucansucrases include EC 2.4.1.372, mutansucrase, which extends (1→3)-α-D-glucans; EC 2.4.1.4, amylosucrase, which extends (1→4)-α-D-glucans; EC 2.4.1.5, dextransucrase, which extends (1→6) α-D-glucans; EC 2.4.1.373, α-(1→2) branching sucrase, which introduces α(1→2) branches into (1→6)-α-D-glucans; EC 2.4.1.125, sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase, which extends (1→6) α-D-glucans by both α(1→3) and α(1→6) linkages, with one of the linkage types being dominant; and EC 2.4.1.140, alternansucrase, which forms both α(1→3) and α(1→6) linkages in approximately equal amounts by alternating the linkage type.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Simpson, C.L., Cheetham, N.W., Giffard, P.M. and Jacques, N.A. Four glucosyltransferases, GtfJ, GtfK, GtfL and GtfM, from Streptococcus salivarius ATCC 25975. Microbiology 141 (1995) 1451-1460. [PMID: 7545511]
2. Puanglek, S., Kimura, S., Enomoto-Rogers, Y., Kabe, T., Yoshida, M., Wada, M. and Iwata, T. In vitro synthesis of linear α-1,3-glucan and chemical modification to ester derivatives exhibiting outstanding thermal properties. Sci Rep 6 (2016) 30479. [PMID: 27469976]
Accepted name: α-(1→2) branching sucrase
Reaction: sucrose + a (1→6)-α-D-glucan = D-fructose + a (1→6)-α-D-glucan containing a (1→2)-α-D-glucose branch
Systematic name: sucrose:(1→6)-α-D-glucan 2-α-D-glucosyl-transferase
Comments: The glucansucrases transfer a D-glusosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. Currently classified glucansucrases include EC 2.4.1.372, mutansucrase, which extends (1→3)-α-D-glucans; EC 2.4.1.4, amylosucrase, which extends (1→4)-α-D-glucans; EC 2.4.1.5, dextransucrase, which extends (1→6) α-D-glucans; EC 2.4.1.373, α-(1→2) branching sucrase, which introduces α(1→2) branches into (1→6)-α-D-glucans; EC 2.4.1.125, sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase, which extends (1→6) α-D-glucans by both α(1→3) and α(1→6) linkages, with one of the linkage types being dominant; and EC 2.4.1.140, alternansucrase, which forms both α(1→3) and α(1→6) linkages in approximately equal amounts by alternating the linkage type.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Fabre, E., Bozonnet, S., Arcache, A., Willemot, R.M., Vignon, M., Monsan, P. and Remaud-Simeon, M. Role of the two catalytic domains of DSR-E dextransucrase and their involvement in the formation of highly α-1,2 branched dextran. J. Bacteriol. 187 (2005) 296-303. [PMID: 15601714]
2. Brison, Y., Laguerre, S., Lefoulon, F., Morel, S., Monties, N., Potocki-Veronese, G., Monsan, P. and Remaud-Simeon, M. Branching pattern of gluco-oligosaccharides and 1.5kDa dextran grafted by the α-1,2 branching sucrase GBD-CD2. Carbohydr Polym 94 (2013) 567-576. [PMID: 23544576]
3. Passerini, D., Vuillemin, M., Ufarte, L., Morel, S., Loux, V., Fontagne-Faucher, C., Monsan, P., Remaud-Simeon, M. and Moulis, C. Inventory of the GH70 enzymes encoded by Leuconostoc citreum NRRL B-1299 - identification of three novel α-transglucosylases. FEBS J. 282 (2015) 2115-2130. [PMID: 25756290]
Accepted name: β-1,2-mannooligosaccharide synthase
Reaction: GDP-α-D-mannose + [(1→2)-β-D-mannosyl]n = GDP + [(1→2)-β-D-mannosyl]n+1
Other name(s): MTP1 (gene name); MTP2 (gene name)
Systematic name: GDP-α-D-mannose:(1→2)-β-D-mannan mannosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from Leishmania parasites, is involved in synthesis of mannogen, a β-(1→2)-mannan oligosaccharide used by the organisms as a carbohydrate reserve.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sernee, M.F., Ralton, J.E., Nero, T.L., Sobala, L.F., Kloehn, J., Vieira-Lara, M.A., Cobbold, S.A., Stanton, L., Pires, D.EV., Hanssen, E., Males, A., Ward, T., Bastidas, L.M., van der Peet, P.L., Parker, M.W., Ascher, D.B., Williams, S.J., Davies, G.J. and McConville, M.J. A family of dual-activity glycosyltransferase-phosphorylases mediates mannogen turnover and virulence in Leishmania parasites. Cell Host Microbe 26 (2019) 385-399.e9. [PMID: 31513773]
Accepted name: rhamnogalacturonan I galactosyltransferase
Reaction: Transfer of a β-galactosyl residue in a β-(1→4) linkage from UDP-α-D-galactose to rhamnosyl residues within the rhamnogalacturonan I backbone.
Glossary: rhamnogalacturonan I backbone = [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n
Systematic name: UDP-α-D-galactose:[rhamnogalacturonan I]-α-L-rhamnosyl β-1,4-galactosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the plant Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan I, one of the components of pectin in plant cell wall. It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 9.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Matsumoto, N., Takenaka, Y., Wachananawat, B., Kajiura, H., Imai, T. and Ishimizu, T. Rhamnogalacturonan I galactosyltransferase: Detection of enzyme activity and its hyperactivation. Plant Physiol. Biochem. 142 (2019) S0981-9428(. [PMID: 31299599]
Accepted name: EGF-domain serine glucosyltransferase
Reaction: UDP-α-D-glucose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine
Other name(s): POGLUT1 (gene name) (ambiguous); rumi (gene name) (ambiguous)
Systematic name: UDP-α-D-glucose:[protein with EGF-like domain]-L-serine O-β-glucosyltransferase (configuration-inverting)
Comments: The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-α-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Li, Z., Fischer, M., Satkunarajah, M., Zhou, D., Withers, S.G. and Rini, J.M. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8 (2017) 185. [PMID: 28775322]
Accepted name: dTDP-Rha:α-D-Gal-diphosphoundecaprenol α-1,3-rhamnosyltransferase
Reaction: dTDP-β-L-rhamnose + α-D-galactosyl-diphospho-ditrans,octacis-undecaprenol = dTDP + α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaN (gene name); rfbN (gene name)
Systematic name: dTDP-β-L-rhamnose:α-D-galactosyl-diphospho-ditrans,octacis-undecaprenol 3-α-rhamnosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from several Salmonella strains, participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B, D and E groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408-3413. [PMID: 7684736]
Accepted name: GDP-mannose:α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,4-mannosyltransferase
Reaction: GDP-α-D-mannose + α-L-Rha-(1→3)-α-D-Gal-PP-Und = GDP + α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaU (gene name); rfbU (gene name)
Systematic name: GDP-α-D-mannose:α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 4II-α-rhamnosyltransferase (configuration-retaining)
Comments: The enzyme from Salmonella participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B, and D1 groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408-3413. [PMID: 7684736]
Accepted name: GDP-Man:α-D-Gal-diphosphoundecaprenol α-1,3-mannosyltransferase
Reaction: GDP-α-D-mannose + α-D-galactosyl-diphospho-ditrans-octacis-undecaprenol = GDP + α-D-Man-(1→3)-α-D-Gal-PP-Und
Glossary: α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaZ (gene name); rfbZ (gene name)
Systematic name: GDP-α-D-mannose:α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase (configuration-retaining)
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. Cloning of the rfb gene cluster of a group C2 Salmonella strain: comparison with the rfb regions of groups B and D. Mol. Microbiol. 5 (1991) 1873-1881. [PMID: 1722557]
2. 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]
3. Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408-3413. [PMID: 7684736]
4. 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: GDP-Man:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-mannosyltransferase
Reaction: GDP-α-D-mannose + α-D-Man-(1→3)-α-D-Gal-PP-Und = GDP + α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und
Glossary: α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaW (gene name); rfbW (gene name)
Systematic name: GDP-α-D-mannose:α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 2II-α-mannosyltransferase (configuration-retaining)
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. Cloning of the rfb gene cluster of a group C2 Salmonella strain: comparison with the rfb regions of groups B and D. Mol. Microbiol. 5 (1991) 1873-1881. [PMID: 1722557]
2. 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]
3. Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408-3413. [PMID: 7684736]
Accepted name: dTDP-Rha:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-rhamnosyltransferase
Reaction: dTDP-β-L-rhamnose + α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = dTDP + α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und
Glossary: α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
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): wbaQ (gene name); rfbQ (gene name)
Systematic name: dTDP-β-L-rhamnose:α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 2III-α-rhamnosyltransferase (configuration-inverting)
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. Cloning of the rfb gene cluster of a group C2 Salmonella strain: comparison with the rfb regions of groups B and D. Mol. Microbiol. 5 (1991) 1873-1881. [PMID: 1722557]
2. 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]
3. Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408-3413. [PMID: 7684736]
4. 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: CDP-abequose:α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase
Reaction: CDP-α-D-abequose + 2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = CDP + α-D-Abe-(1→3)-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-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = 2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Abe-(1→3)-2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-abequosyl-(1→3)-2-O-acetyl-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): wbaR (gene name); rfbR (gene name)
Systematic name: CDP-α-D-abequose:2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3IV-α-abequosyltransferase (configuration retaining)
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. 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]
2. 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: GDP-Man:α-L-Rha-(1→3)-α-D-Gal-PP-Und β-1,4-mannosyltransferase
Reaction: GDP-α-D-mannose + α-L-Rha-(1→3)-α-D-Gal-PP-Und = GDP + β-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
β-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = β-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaO (gene name); rfbO (gene name)
Systematic name: GDP-α-D-mannose:α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 4II-β-mannosyltransferase (configuration inverting)
Comments: The enzyme participates in the biosynthesis of the O antigens produced by group E and D2 strains of the pathogenic bacterium Salmonella enterica.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Xiang, S.H., Hobbs, M. and Reeves, P.R. Molecular analysis of the rfb gene cluster of a group D2 Salmonella enterica strain: evidence for its origin from an insertion sequence-mediated recombination event between group E and D1 strains. J. Bacteriol. 176 (1994) 4357-4365. [PMID: 8021222]
2. Zhao, Y., Biggins, J. B. and Thorson, J. S. Acceptor specificity of Salmonella GDP-Man:α-L-Rha-(1→3)-α-D- Gal- PP-Und β(1→4)-mannosyltransferase: A simplified assay based on unnatural acceptors. J. Am. Chem. Soc. 120 (1998) 12986-12987.
3. Zhao, Y. and Thorson, J.S. Chemoenzymatic synthesis of the Salmonella group E1 core trisaccharide using a recombinant β-(1-→4)-mannosyltransferase. Carbohydr. Res. 319 (1999) 184-191. [PMID: 10520265]
Accepted name: NDP-glycosyltransferase
Reaction: an NDP-glycose + an acceptor = a glycosylated acceptor + NDP
Other name(s): yjiC (gene name)
Systematic name: NDP-glycose:acceptor glycosyltransferase
Comments: The enzyme, characterized from the bacterium Bacillus licheniformis DSM-13, is an extremely promiscuous glycosyltransferase. It can accept ADP-, GDP-, CDP-, TDP-, or UDP-activated glycose molecules as donors, and can glycosylate a large number of substrates, catalysing O-, N-, or S-glycosylation. While D-glucose is the primarily reported sugar being transferred, the enzyme has been shown to transfer D-galactose, 2-deoxy-D-glucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, L-fucose, L-rhamnose, D-glucuronate, and D-viosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Pandey, R.P., Parajuli, P., Koirala, N., Park, J.W. and Sohng, J.K. Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by YjiC. Appl. Environ. Microbiol. 79 (2013) 6833-6838. [PMID: 23974133]
2. Pandey, R.P., Gurung, R.B., Parajuli, P., Koirala, N., Tuoi le, T. and Sohng, J.K. Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids. Carbohydr. Res. 393 (2014) 26-31. [PMID: 24893262]
3. Pandey, R.P., Parajuli, P., Shin, J.Y., Lee, J., Lee, S., Hong, Y.S., Park, Y.I., Kim, J.S. and Sohng, J.K. Enzymatic biosynthesis of novel resveratrol glucoside and glycoside derivatives. Appl. Environ. Microbiol. 80 (2014) 7235-7243. [PMID: 25239890]
4. Parajuli, P., Pandey, R.P., Koirala, N., Yoon, Y.J., Kim, B.G. and Sohng, J.K. Enzymatic synthesis of epothilone A glycosides. AMB Express 4 (2014) 31. [PMID: 24949266]
5. Pandey, R.P., Parajuli, P., Gurung, R.B. and Sohng, J.K. Donor specificity of YjiC glycosyltransferase determines the conjugation of cytosolic NDP-sugar in in vivo glycosylation reactions. Enzyme Microb. Technol. 91 (2016) 26-33. [PMID: 27444326]
6. Bashyal, P., Thapa, S.B., Kim, T.S., Pandey, R.P. and Sohng, J.K. Exploring the nucleophilic N- and S-glycosylation capacity of Bacillus licheniformis YjiC enzyme. J. Microbiol. Biotechnol. 30 (2020) 1092-1096. [PMID: 32238768]
Accepted name: sterol 27-β-glucosyltransferase
Reaction: UDP-α-D-glucose + a 27-hydroxysteroid = UDP + a sterol 27-β-D-glucoside
For diagram of reaction, click here
Systematic name: UDP-α-D-glucose:sterol 27-O-β-D-glucosyltransferase
Comments: The enzyme, isolated from the plant Withania somnifera (ashwagandha), transfers D-glucose to a β-hydroxyl group present at the C-27 position in sterols/withanolides, provided the substrate possesses a 17α-OH group. Natural substrates are 17α-hydroxywithaferin A, 27β-hydroxywithanone, and 5α,6β,17α,27β-tetrahydroxywithanolide. The enzyme's activity with withanolide A and withanolide U, which lack a 17α-hydroxyl group, suggests it may also be able to glucosylate the C-20 β-OH position, although this has not been verified yet. The enzyme does not glucosylate sterols at the C-3 position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Madina, B.R., Sharma, L.K., Chaturvedi, P., Sangwan, R.S. and Tuli, R. Purification and characterization of a novel glucosyltransferase specific to 27β-hydroxy steroidal lactones from Withania somnifera and its role in stress responses. Biochim. Biophys. Acta 1774 (2007) 1199-1207. [PMID: 17704015]
Accepted name: GlcNAc-β-1,3-Gal β-1,6-N-acetylglucosaminyltransferase (distally acting)
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Other name(s): UDP-GlcNAc:GlcNAcβ1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase; dIGnT; C2GnT2 (misleading)
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Involved in the production of milk oligosaccharides in the lacto-N-triose (LNT) series. Cf. EC 2.4.1.150 (N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase; cIGnT) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β 1-3Gal(-R) β 1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385-13390. [PMID: 6490658]
2. Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215-3221. [PMID: 9915862]
Accepted name: isomaltosyltransferase
Reaction: (1) 2 α-isomaltosyl-(1→4)-maltotriose = α-isomaltosyl-(1→3)-α-isomaltosyl-(1→4)-maltotriose + maltotriose
(2) α-isomaltosyl-(1→3)-α-isomaltosyl-(1→4)-maltotriose = cyclobis-(1→6)-α-nigerosyl + maltotriose
Systematic name: α-isomaltosyl-(1→3)-1,4-α-D-glucan:1,4-α-D-glucan 3-α-isomaltosyltransferase
Comments: The enzyme, found in bacteria that produce cyclobis-(1→6)-α-nigerosyl, acts on the products of EC 2.4.1.24, 1,4-α-glucan 6-α;-glucosyltransferase. It catalyses the α-(1→3) transfer of the isomaltosyl moiety of one substrate to another, resulting in α-isomaltosyl-(1→3)-α-isomaltosyl-α-(1→4)-glucan formation. In addition, the enzyme catalyses the intramolecular cyclization of the product, eventually generating cyclobis-(1→6)-α-nigerosyl.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Aga, H., Maruta, K., Yamamoto, T., Kubota, M., Fukuda, S., Kurimoto, M. and Tsujisaka, Y. Cloning and sequencing of the genes encoding cyclic tetrasaccharide-synthesizing enzymes from Bacillus globisporus C11. Biosci. Biotechnol. Biochem. 66 (2002) 1057-1068. [PMID: 12092816]
2. Nishimoto, T., Aga, H., Mukai, K., Hashimoto, T., Watanabe, H., Kubota, M., Fukuda, S., Kurimoto, M. and Tsujisaka, Y. Purification and characterization of glucosyltransferase and glucanotransferase involved in the production of cyclic tetrasaccharide in Bacillus globisporus C11. Biosci. Biotechnol. Biochem. 66 (2002) 1806-1818. [PMID: 12400677]
3. Kim, Y.K., Kitaoka, M., Hayashi, K., Kim, C.H. and Cote, G.L. A synergistic reaction mechanism of a cycloalternan-forming enzyme and a D-glucosyltransferase for the production of cycloalternan in Bacillus sp. NRRL B-21195. Carbohydr. Res. 338 (2003) 2213-2220. [PMID: 14553982]
Accepted name: glucosylgalactose phosphorylase
Reaction: β-D-glucosyl-(1→4)-D-galactose + phosphate = α-D-glucopyranose 1-phosphate + D-galactopyranose
Other name(s): 4-O-β-D-glucosyl-D-galactose phosphorylase
Systematic name: β-D-glucosyl-(1→4)-D-galactose:phosphate α-D-glucosyltransferase (configuration-inverting)
Comments: The enzyme from the bacterium Paenibacillus polymyxa belongs to glycoside hydrolase family 94. It has a much lower activity with 4-O-β-D-glucosyl-L-arabinose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. De Doncker, M., De Graeve, C., Franceus, J., Beerens, K., Kren, V., Pelantova, H., Vercauteren, R. and Desmet, T. Exploration of GH94 sequence space for enzyme discovery reveals a novel glucosylgalactose phosphorylase specificity. ChemBioChem (2021) . [PMID: 34541742]
Accepted name: solabiose phosphorylase
Reaction: solabiose + phosphate = D-galactose + α-D-glucose 1-phosphate
Glossary: solabiose = β-D-glucopyranosyl-(1→3)-D-galactose
Systematic name: solabiose:phosphate α-D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Paenibacillus borealis, belongs to glycoside hydrolase family 94 (GH94).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Saburi, W., Nihira, T., Nakai, H., Kitaoka, M. and Mori, H. Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose. Sci. Rep. 12 (2022) 259. [PMID: 34997180]
Accepted name: 4,3-α-glucanotransferase
Reaction: formation of a mixed (1→4)/(1→3)-α-D-glucan from (1→4)-α-D-glucans
Other name(s): gtfB (gene name) (ambiguous)
Systematic name: (1→4)-α-D-glucan:(1→4)/(1→3)-α-D-glucan 3-α-D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Lactobacillus fermentum NCC 2970, possesses hydrolysis and transglycosylase activities on malto-oligosaccharides with a degree of polymerization of at least 6, as well as polymers such as amylose, potato starch, and amylopectin. The enzyme, which belongs to glycoside hydrolase 70 (GH70) family, attaches the glucosyl residues by α(1→3) linkages in both linear and branched orientations. While capable of forming large polymers, the enzyme produces mainly oligosaccharides in vitro.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Gangoiti, J., van Leeuwen, S.S., Gerwig, G.J., Duboux, S., Vafiadi, C., Pijning, T. and Dijkhuizen, L. 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H. Sci. Rep. 7 (2017) 39761. [PMID: 28059108]
2. Pijning, T., Gangoiti, J., Te Poele, E.M., Borner, T. and Dijkhuizen, L. Insights into broad-specificity starch modification from the crystal structure of Limosilactobacillus reuteri NCC 2613 4,6-α-glucanotransferase GtfB. J. Agric. Food Chem. 69 (2021) 13235-13245. [PMID: 34708648]
Accepted name: β-1,2-glucosyltransferase
Reaction: [(1→2)-β-D-glucosyl]n + a D-glucoside = [(1→2)-β-D-glucosyl]n-1 + a β-D-glucosyl-(1→2)-D-glucoside
Systematic name: 1,2-β-D-glucan:D-glucoside 2-β-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme, characterized from the bacterium Ignavibacterium album, transfers a glucosyl residue from the non-reducing end of a 1,2-β-D-glucan to a glucose residue of an acceptor molecule, forming a β(1,2) linkage. The donor molecule can be as small as sophorose (which contains two glucosyl residues). The enzyme has a very broad specificity for the acceptor, and can act on various aryl- and alkyl-glucosides. In addition, the accepting glucose unit can be in either α or β configuration.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kobayashi, K., Shimizu, H., Tanaka, N., Kuramochi, K., Nakai, H., Nakajima, M. and Taguchi, H. Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages. J. Biol. Chem. 298 (2022) 101606. [PMID: 35065074]
Accepted name: 3-O-β-D-glucopyranosyl-β-D-glucuronide phosphorylase
Reaction: a 3-O-β-D-glucosyl-β-D-glucuronoside + phosphate = a β-D-glucuronoside + α-D-glucopyranose 1-phosphate
Other name(s): PBOR_13355 (locus name)
Systematic name: 3-O-β-D-glucopyranosyl-β-D-glucuronide:phosphate α-D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Paenibacillus borealis, catalyses a reversible reaction, transferring a glucosyl residue attached by a β(1,3) linkage to a D-glucuronate residue (either free or as a part of a β-D-glucuronide) to a free phosphate, generating α-D-glucopyranose 1-phosphate
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Isono, N., Mizutani, E., Hayashida, H., Katsuzaki, H. and Saburi, W. Functional characterization of a novel GH94 glycoside phosphorylase, 3-O-β-D-glucopyranosyl β-D-glucuronide phosphorylase, and implication of the metabolic pathway of acidic carbohydrates in Paenibacillus borealis. Biochem. Biophys. Res. Commun. 625 (2022) 60-65. [PMID: 35947916]
Accepted name: MMP α-(1→4)-mannosyltransferase
Reaction: GDP-α-D-mannose + [3-O-methyl-α-D-mannosyl-(1→4)]n-3-O-methyl-α-D-mannose = α-D-mannosyl-(1→4)-[3-O-methyl-α-D-mannosyl-(1→4)]n-3-O-methyl-α-D-mannose + GDP
Glossary: MMP = α-D-mannosyl-(1→4)-[3-O-methyl-α-D-mannosyl-(1→4)]n-1-O,3-O-dimethyl-α-D-mannose
Other name(s): manT (gene name)
Systematic name: GDP-α-D-mannose:[3-O-methyl-α-D-mannosyl-(1→4)]n-3-O-methyl-α-D-mannose [(1→4)-α-D-mannosyl]transferase
Comments: The enzyme, present in mycobacterial species that produce a 3-O-methylmannose polysaccharide (MMP), is involved in recycling and biosynthesis of the polymer. The enzyme has the highest activity with 3-O-methylated mannosides with 4-6 residues. The residue at the reducing end of the substrate is often dimethylated, with the second methyl group attached at the O-1 position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Maranha, A., Costa, M., Ripoll-Rozada, J., Manso, J.A., Miranda, V., Mendes, V.M., Manadas, B., Macedo-Ribeiro, S., Ventura, M.R., Pereira, P.JB. and Empadinhas, N. Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides. Commun Biol 6 (2023) 108. [PMID: 36707645]
Accepted name: 4,6-α-glucanotransferase (linear substrates/linear products)
Reaction: formation of a linear isomalto/malto-polysaccharide from linear malto-oligosaccharides
Other name(s): gtfB (gene name) (ambiguous); gtfC (gene name)
Systematic name: linear (1→4)-α-D-glucan:(1→4)/(1→6)-α-D-glucan 6-α-D-glucosyltransferase
Comments: The enzyme, originally discovered in lactic acid bacteria but later found in other organisms, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving α(1→4) linkages from the non-reducing end of linear maltooligosaccharides and synthesizing linear α(1→6)-glucan chains. It also possesses an endo-α(1→4)-glycosidase activity. Due to its narrow binding groove, it is not able to act on branched substrates. cf. EC 2.4.1.396, 4,6-α-glucanotransferase (linear and branched substrates, branched products).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kralj, S., van Geel-Schutten, G.H., Dondorff, M.MG., Kirsanovs, S., van der Maarel, M.JE.C. and Dijkhuizen, L. Glucan synthesis in the genus Lactobacillus: isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains. Microbiology (Reading) 150 (2004) 3681-3690. [PMID: 15528655]
2. Kralj, S., Grijpstra, P., van Leeuwen, S.S., Leemhuis, H., Dobruchowska, J.M., van der Kaaij, R.M., Malik, A., Oetari, A., Kamerling, J.P. and Dijkhuizen, L. 4,6-α-glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70. Appl. Environ. Microbiol. 77 (2011) 8154-8163. [PMID: 21948833]
3. Dobruchowska, J.M., Gerwig, G.J., Kralj, S., Grijpstra, P., Leemhuis, H., Dijkhuizen, L. and Kamerling, J.P. Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121. Glycobiology 22 (2012) 517-528. [PMID: 22138321]
4. Leemhuis, H., Dijkman, W.P., Dobruchowska, J.M., Pijning, T., Grijpstra, P., Kralj, S., Kamerling, J.P. and Dijkhuizen, L. 4,6-α-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. Appl. Microbiol. Biotechnol. 97 (2013) 181-193. [PMID: 22361861]
5. Gangoiti, J., Pijning, T. and Dijkhuizen, L. The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. Appl. Environ. Microbiol. 82 (2016) 756-766. [PMID: 26590275]
6. Bai, Y., Gangoiti, J., Dijkstra, B.W., Dijkhuizen, L. and Pijning, T. Crystal structure of 4,6-α-glucanotransferase supports diet-driven evolution of GH70 enzymes from α-amylases in oral bacteria. Structure 25 (2017) 231-242. [PMID: 28065507]
7. Te Poele, E.M., van der Hoek, S.E., Chatziioannou, A.C., Gerwig, G.J., Duisterwinkel, W.J., Oudhuis, L.AA.CM., Gangoiti, J., Dijkhuizen, L. and Leemhuis, H. GtfC enzyme of Geobacillus sp. 12AMOR1 represents a novel thermostable type of GH70 4,6-α-glucanotransferase that synthesizes a linear alternating (α1→6)/(α1→4) α-glucan and delays bread staling. J. Agric. Food Chem. 69 (2021) 9859-9868. [PMID: 34427087]
Accepted name: reuteransucrase
Reaction: formation of reuteran from sucrose
Glossary: reuteran = a high-molecular-mass branched α-glucan produced by the lactic acid bacterium Limosilactobacillus reuteri.
Systematic name: sucrose:α-D-glucan 4-α/6-α-D-glucosyltransferase
Comments: The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage of the transferred glucosyl residue. The enzyme, characterized from the lactic acid bacterium Limosilactobacillus reuteri strain 121, catalyses the hydrolysis of sucrose and the transfer of the D-glucose moiety to suitable acceptors (inclduing sucrose), forming the glucan reuteran, which is typical for these strains. The enzyme forms mostly α(1→4) glucosidic linkages, but also α(1→6) linkages. The presence of maltose significantly accelerate the initial rate of the reaction. See EC 2.4.1.5, dextransucrase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kralj, S., van Geel-Schutten, G.H., Rahaoui, H., Leer, R.J., Faber, E.J., van der Maarel, M.J. and Dijkhuizen, L. Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with α-(1→4) and α-(1→6) glucosidic bonds. Appl. Environ. Microbiol. 68 (2002) 4283-4291. [PMID: 12200277]
2. Kralj, S., van Geel-Schutten, G.H., van der Maarel, M.JE.C. and Dijkhuizen, L. Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase. Microbiology (Reading) 150 (2004) 2099-2112. [PMID: 15256553]
3. Kralj, S., Stripling, E., Sanders, P., van Geel-Schutten, G.H. and Dijkhuizen, L. Highly hydrolytic reuteransucrase from probiotic Lactobacillus reuteri strain ATCC 55730. Appl. Environ. Microbiol. 71 (2005) 3942-3950. [PMID: 16000808]
Accepted name: 4,6-α-glucanotransferase (linear and branched substrates, branched products)
Reaction: formation of a branched isomalto/malto-polysaccharide from branched malto-oligosaccharides
Other name(s): gtfB (gene name) (ambiguous); gtfD (gene name)
Systematic name: branched (1→4)-α-D-glucan:(1→4)/(1→6)-α-D-glucan 6-α-D-glucosyltransferase
Comments: The enzyme, discovered in several bacterial species, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving endo α(1→4) linkages from the non-reducing end of maltooligosaccharides and adding the resulting oligosaccharides to the non-reducing end of α-D-glucan chains that terminate with a residue linked by an α-(1→4) linkage, forming an α(1→6) linkage. The enzyme is not able to form successive α(1→6) linkages. Unlike EC 2.4.1.394, 4,6-α-glucanotransferase (linear substrates/linear products), which can only act on linear substrates, this enzyme is able to act on both linear and branched substrates, and can form the branched reuteran type of α-glucan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Gangoiti, J., van Leeuwen, S.S., Vafiadi, C. and Dijkhuizen, L. The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch. Biochim. Biophys Acta 1860 (2016) 1224-1236. [PMID: 26868718]
2. Gangoiti, J., van Leeuwen, S.S., Meng, X., Duboux, S., Vafiadi, C., Pijning, T. and Dijkhuizen, L. Mining novel starch-converting glycoside hydrolase 70 enzymes from the Nestle Culture Collection genome database: the Lactobacillus reuteri NCC 2613 GtfB. Sci. Rep. 7 (2017) 9947. [PMID: 28855510]
3. Pijning, T., Gangoiti, J., Te Poele, E.M., Borner, T. and Dijkhuizen, L. Insights into broad-specificity starch modification from the crystal structure of Limosilactobacillus reuteri NCC 2613 4,6-α-glucanotransferase GtfB. J. Agric. Food Chem. 69 (2021) 13235-13245. [PMID: 34708648]
Accepted name: cyclic β-1,2-glucan glucanotransferase
Reaction: Cyclizes part of a (1→2)-β-D-glucan chain by formation of a (1→2)-β-D-glucosidic bond
Systematic name: (1→2)-β-D-glucan:(1→2)-β-D-glucan 2-β-D-[(1→2)-β-D-glucano]-transferase (cyclizing and configuration-retaining)
Comments: This enzyme is the cyclization domain of cyclic β-1,2-glucan synthase. Enzymes from Brucella abortus and Thermoanaerobacter italicus were characterized. The cyclization domain of cyclic β-1,2-glucan synthase is flanked by an N-terminal β-1,2-glucosyltransferase domain (cf. EC 2.4.1.391) and a C-terminal β-1,2-glucoside phosphorylase domain (cf. EC 2.4.1.333), with the former responsible for elongation and the latter for chain length control. The cyclization domain of Thermoanaerobacter italicus cyclizes linear oligosaccharides with a degree of polymerization (DP) of 21 or higher to produce cyclic glucans with DP 17 or higher. The cyclization domain also disproportionates linear β-1,2-glucooligosaccharides without cycling. The entire cyclic β-1,2-glucan synthase from Brucella abortus synthesizes cyclic β-1,2-glucans with DP 17-22.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Inon de Iannino, N., Briones, G., Tolmasky, M. and Ugalde, R.A. Molecular cloning and characterization of cgs, the Brucella abortus cyclic β(1-2) glucan synthetase gene: genetic complementation of Rhizobium meliloti ndvB and Agrobacterium tumefaciens chvB mutants. J. Bacteriol. 180 (1998) 4392-4400. [PMID: 9721274]
2. Guidolin, L.S., Ciocchini, A.E., Inon de Iannino, N. and Ugalde, R.A. Functional mapping of Brucella abortus cyclic β-1,2-glucan synthase: identification of the protein domain required for cyclization. J. Bacteriol. 191 (2009) 1230-1238. [PMID: 19074375]
3. Guidolin, L.S., Morrone Seijo, S.M., Guaimas, F.F., Comerci, D.J. and Ciocchini, A.E. Interaction network and localization of Brucella abortus membrane proteins involved in the synthesis, transport, and succinylation of cyclic β-1,2-glucans. J. Bacteriol. 197 (2015) 1640-1648. [PMID: 25733613]
4. Tanaka, N., Saito, R., Kobayashi, K., Nakai, H., Kamo, S., Kuramochi, K., Taguchi, H., Nakajima, M. and Masaike, T. Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase. Appl. Microbiol. Biotechnol. 108 (2024) 187. [PMID: 38300345]