EC |
2.4.1.382 | Relevance: 100% |
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 |
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. [DOI] [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 7:391 (2017). [DOI] [PMID: 28929089] |
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[EC 2.4.1.382 created 2021] |
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EC |
2.4.1.138 | Relevance: 99.6% |
Accepted name: |
mannotetraose 2-α-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-D-Man = UDP + α-D-Man-(1→3)-[α-D-GlcNAc-(1→2)]-α-D-Man-(1→2)-α-D-Man-(1→2)-D-Man |
Other name(s): |
α-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine mannoside α1→2-αcetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:mannotetraose α-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-D-mannose α-N-acetyl-D-glucosaminyltransferase (configuration-retaining) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81032-47-5 |
References: |
1. |
Douglas, R.H. and Ballou, C.E. Purification of an α-N-acetylglucosaminyltransferase from the yeast Kluyveromyces lactis and a study of mutants defective in this enzyme activity. Biochemistry 21 (1982) 1561–1570. [PMID: 6211189] |
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[EC 2.4.1.138 created 1984] |
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EC |
2.3.1.303 | Relevance: 98.4% |
Accepted name: |
α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und 2IV-O-acetyltransferase |
Reaction: |
acetyl-CoA + α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = CoA + 2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und |
Glossary: |
α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
rfbL (gene name); wbaL (gene name) |
Systematic name: |
acetyl-CoA:α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 2IV-O-acetyltransferase |
Comments: |
The enzyme, present in Salmonella strains that belong to group C2, participates in the biosynthesis of the repeat unit of O antigens produced by these strains. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Brown, P.K., Romana, L.K. and Reeves, P.R. Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen (strain M67): the genetic basis of the polymorphism between groups C2 and B. Mol. Microbiol. 6 (1992) 1385–1394. [DOI] [PMID: 1379320] |
2. |
Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084–4088. [DOI] [PMID: 7541787] |
3. |
Zhao, X., Dai, Q., Jia, R., Zhu, D., Liu, M., Wang, M., Chen, S., Sun, K., Yang, Q., Wu, Y. and Cheng, A. two novel Salmonella bivalent vaccines confer dual protection against two Salmonella serovars in mice. Front Cell Infect Microbiol 7:391 (2017). [DOI] [PMID: 28929089] |
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[EC 2.3.1.303 created 2021] |
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EC |
2.4.1.371 | Relevance: 96.8% |
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 |
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. [DOI] [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. [DOI] [PMID: 25422321] |
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[EC 2.4.1.371 created 2019] |
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EC |
3.2.1.50 | Relevance: 93.6% |
Accepted name: |
α-N-acetylglucosaminidase |
Reaction: |
Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-α-D-glucosaminides |
Other name(s): |
α-acetylglucosaminidase; N-acetyl-α-D-glucosaminidase; N-acetyl-α-glucosaminidase; α-D-2-acetamido-2-deoxyglucosidase |
Systematic name: |
α-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase |
Comments: |
Hydrolyses UDP-N-acetylglucosamine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-40-7 |
References: |
1. |
von Figura, K. Human α-N-acetylglucosaminidase. 1. Purification and properties. Eur. J. Biochem. 80 (1977) 523–533. [PMID: 411658] |
2. |
von Figura, K. Human α-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition forms. Eur. J. Biochem. 80 (1977) 535–542. [DOI] [PMID: 923593] |
3. |
Weissmann, B., Rowen, G., Marshall, J. and Friederici, D. Mammalian α-acetylglucosaminidase. Enzymic properties, tissue distribution, and intracellular localization. Biochemistry 6 (1967) 207–214. [PMID: 4291567] |
4. |
Werries, E., Wollek, E., Gottschalk, A. and Buddecke, E. Separation of N-acetyl-α-glucosaminidase and N-acetyl-α-galactosaminidase from ox spleen. Cleavage of the O-glycosidic linkage between carbohydrate and polypeptide in ovine and bovine submaxillary glycoprotein by N-acetyl-α-galactosaminidase. Eur. J. Biochem. 10 (1969) 445–449. [DOI] [PMID: 5348072] |
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[EC 3.2.1.50 created 1972] |
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EC |
2.7.1.181 | Relevance: 89.1% |
Accepted name: |
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase |
Reaction: |
ATP + 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 = ADP + 3-O-phospho-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
|
Other name(s): |
WbdD; ATP: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)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phosphotransferase |
Systematic name: |
ATP: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 3-phosphotransferase |
Comments: |
The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the methylation of 3-phospho-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 (cf. EC 2.1.1.294, 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709–35718. [DOI] [PMID: 15184370] |
2. |
Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662–30672. [DOI] [PMID: 19734145] |
3. |
Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391–41401. [DOI] [PMID: 21990359] |
4. |
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. [DOI] [PMID: 25422321] |
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[EC 2.7.1.181 created 2014, modified 2017] |
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EC |
2.4.1.267 | Relevance: 89.1% |
Accepted name: |
dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase |
Reaction: |
dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate |
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For diagram of dolichyltetradecasaccharide biosynthesis, click here |
Other name(s): |
ALG6; Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase |
Systematic name: |
dolichyl β-D-glucosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting) |
Comments: |
The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493–498. [DOI] [PMID: 8877369] |
2. |
Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412–417. [PMID: 6423630] |
3. |
Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420–421. [DOI] [PMID: 14517965] |
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[EC 2.4.1.267 created 2011, modified 2012] |
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EC |
2.4.1.265 | Relevance: 88.1% |
Accepted name: |
dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase |
Reaction: |
dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate |
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For diagram of dolichyltetradecasaccharide biosynthesis, click here |
Other name(s): |
ALG8; Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase |
Systematic name: |
dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting) |
Comments: |
The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977–5981. [DOI] [PMID: 8016100] |
2. |
Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582–15590. [PMID: 3536907] |
3. |
Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962–9971. [DOI] [PMID: 12480927] |
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[EC 2.4.1.265 created 2011, modified 2012] |
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EC |
2.4.3.7 | Relevance: 88% |
Accepted name: |
α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-D-galactosaminyl-R |
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For diagram of reaction, click here |
Other name(s): |
sialyltransferase; cytidine monophosphoacetylneuraminate-(α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetylgalactosaminide-α-2,6-sialyltransferase; α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetyl-galactosaminide α-2,6-sialyltransferase; SIAT7; ST6GALNAC; (α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetyl-galactosaminide 6-α-sialyltransferase; CMP-N-acetylneuraminate:(α-N-acetylneuraminyl-2,3-β-D-galactosyl-1,3)-N-acetyl-D-galactosaminide α-2,6-N-acetylneuraminyl-transferase |
Systematic name: |
CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)- N-acetyl-D-galactosaminide galactosamine-6-α-N-acetylneuraminyltransferase |
Comments: |
Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetylgalactosamine only when present in the structure of α-N-acetylneuraminyl-(2→3)-β-galactosyl-(1→3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.3.3 α-N-acetylgalactosaminide α-2,6-sialyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129924-24-9 |
References: |
1. |
Bergh, M.L.E., Hooghwinkel, G.J.M. and Van den Eijnden, D.H. Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an α-N-acetylgalactosaminide α2→6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. J. Biol. Chem. 258 (1983) 7430–7436. [PMID: 6190802] |
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[EC 2.4.3.7 created 1984 as EC 2.4.99.7, modified 1986, modified 2004, transferred 2022 to EC 2.4.3.7] |
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EC |
3.2.1.49 | Relevance: 87.8% |
Accepted name: |
α-N-acetylgalactosaminidase |
Reaction: |
Cleavage of non-reducing α-(1→3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids |
Other name(s): |
α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase |
Systematic name: |
α-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase |
Comments: |
The human lysosomal enzyme is involved in the degradation of blood type A epitope. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-63-2 |
References: |
1. |
Asfaw, B., Schindler, D., Ledvinova, J., Cerny, B., Smid, F. and Conzelmann, E. Degradation of blood group A glycolipid A-6-2 by normal and mutant human skin fibroblasts. J. Lipid Res. 39 (1998) 1768–1780. [PMID: 9741689] |
2. |
Zhu, A., Monahan, C., Wang, Z.K. and Goldstein, J. Expression, purification, and characterization of recombinant α-N-acetylgalactosaminidase produced in the yeast Pichia pastoris. Protein Expr. Purif. 8 (1996) 456–462. [DOI] [PMID: 8954893] |
3. |
Clark, N.E. and Garman, S.C. The 1.9 Å structure of human α-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases. J. Mol. Biol. 393 (2009) 435–447. [DOI] [PMID: 19683538] |
4. |
Hoskins, L.C., Boulding, E.T. and Larson, G. Purification and characterization of blood group A-degrading isoforms of α-N-acetylgalactosaminidase from Ruminococcus torques strain IX-70. J. Biol. Chem. 272 (1997) 7932–7939. [DOI] [PMID: 9065462] |
5. |
Harun-Or-Rashid, M., Matsuzawa, T., Satoh, Y., Shiraishi, T., Ando, M., Sadik, G. and Uda, Y. Purification and characterization of α-N-acetylgalactosaminidases I and II from the starfish Asterina amurensis. Biosci. Biotechnol. Biochem. 74 (2010) 256–261. [DOI] [PMID: 20139603] |
6. |
Weignerova, L., Filipi, T., Manglova, D. and Kren, V. Induction, purification and characterization of α-N-acetylgalactosaminidase from Aspergillus niger. Appl. Microbiol. Biotechnol. 79 (2008) 769–774. [DOI] [PMID: 18443780] |
7. |
Ashida, H., Tamaki, H., Fujimoto, T., Yamamoto, K. and Kumagai, H. Molecular cloning of cDNA encoding α-N-acetylgalactosaminidase from Acremonium sp. and its expression in yeast. Arch. Biochem. Biophys. 384 (2000) 305–310. [DOI] [PMID: 11368317] |
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[EC 3.2.1.49 created 1972, modified 2011] |
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EC
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2.4.99.7
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Transferred entry: | α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase. Now EC 2.4.3.7, α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase
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[EC 2.4.99.7 created 1984, modified 1986, modified 2004, deleted 2022] |
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EC |
2.4.1.256 | Relevance: 86.3% |
Accepted name: |
dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase |
Reaction: |
dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = dolichyl phosphate + α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol |
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For diagram of dolichyltetradecasaccharide biosynthesis, click here |
Other name(s): |
ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-glucosyltransferase |
Systematic name: |
dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase (configuration-retaining) |
Comments: |
This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455–462. [DOI] [PMID: 9597543] |
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[EC 2.4.1.256 created 2011, modified 2012] |
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EC |
1.1.1.426 | Relevance: 86.2% |
Accepted name: |
UDP-N-acetyl-α-D-quinovosamine dehydrogenase |
Reaction: |
UDP-N-acetyl-α-D-quinovosamine + NAD(P)+ = UDP-2-acetamido-2,6-dideoxy-α-D-xylohex-4-ulose + NAD(P)H + H+ |
Glossary: |
UDP-N-acetyl-α-D-quinovosamine = UDP-N-acetyl-6-deoxy-α-D-glucosamine |
Other name(s): |
wbpV (gene name); wreQ (gene name) |
Systematic name: |
UDP-N-acetyl-α-D-quinovosamine:NAD(P)+ 4-dehydrogenase |
Comments: |
The enzyme participates in the biosynthesis of N-acetyl-α-D-quinovosamine, a 6-deoxy sugar that is present in the O antigens of many Gram-negative bacteria, including Pseudomonas aeruginosa serotypes O6 and O10, Rhizobium etli, and Brucella abortus. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Belanger, M., Burrows, L.L. and Lam, J.S. Functional analysis of genes responsible for the synthesis of the B-band O antigen of Pseudomonas aeruginosa serotype O6 lipopolysaccharide. Microbiology (Reading) 145 (1999) 3505–3521. [DOI] [PMID: 10627048] |
2. |
Forsberg, L.S., Noel, K.D., Box, J. and Carlson, R.W. Genetic locus and structural characterization of the biochemical defect in the O-antigenic polysaccharide of the symbiotically deficient Rhizobium etli mutant, CE166. Replacement of N-acetylquinovosamine with its hexosyl-4-ulose precursor. J. Biol. Chem. 278 (2003) 51347–51359. [DOI] [PMID: 14551189] |
3. |
Li, T., Simonds, L., Kovrigin, E.L. and Noel, K.D. In vitro biosynthesis and chemical identification of UDP-N-acetyl-D-quinovosamine (UDP-D-QuiNAc). J. Biol. Chem. 289 (2014) 18110–18120. [DOI] [PMID: 24817117] |
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[EC 1.1.1.426 created 2021] |
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EC |
2.4.1.378 | Relevance: 85.7% |
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 |
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. [DOI] [PMID: 7684736] |
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[EC 2.4.1.378 created 2021] |
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EC |
3.2.1.24 | Relevance: 85.7% |
Accepted name: |
α-mannosidase |
Reaction: |
Hydrolysis of terminal, non-reducing α-D-mannose residues in α-D-mannosides |
Other name(s): |
α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase |
Systematic name: |
α-D-mannoside mannohydrolase |
Comments: |
Also hydrolyses α-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9025-42-7 |
References: |
1. |
Li, Y.-T. Presence of α-D-mannosidic linkage in glycoproteins. Liberation of D-mannose from various glycoproteins by α-mannosidase isolated from jack bean meal. J. Biol. Chem. 241 (1966) 1010–1012. [PMID: 5905120] |
2. |
Winchester, B. Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins. Biochem. Soc. Trans. 12 (1984) 522–524. [PMID: 6428944] |
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[EC 3.2.1.24 created 1961] |
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EC |
2.4.1.292 | Relevance: 85% |
Accepted name: |
GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase |
Reaction: |
3 UDP-N-acetyl-α-D-galactosamine + GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol = 3 UDP + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol |
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For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here |
Glossary: |
diNAcBac = N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose |
Other name(s): |
PglH |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-α-N-acetyl-D-galactosaminyltransferase |
Comments: |
Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480] |
2. |
Troutman, J.M. and Imperiali, B. Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions. Biochemistry 48 (2009) 2807–2816. [DOI] [PMID: 19159314] |
3. |
Borud, B., Viburiene, R., Hartley, M.D., Paulsen, B.S., Egge-Jacobsen, W., Imperiali, B. and Koomey, M. Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system. Proc. Natl. Acad. Sci. USA 108 (2011) 9643–9648. [DOI] [PMID: 21606362] |
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[EC 2.4.1.292 created 2012] |
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EC |
2.1.1.294 | Relevance: 84.6% |
Accepted name: |
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + 3-O-phospho-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 = S-adenosyl-L-homocysteine + 3-O-methylphospho-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 |
Other name(s): |
WbdD; S-adenosyl-L-methionine:3-O-phospho-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)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-α-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:3-O-phospho-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 3-phospho-methyltransferase |
Comments: |
The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the preceding phosphorylation of 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 (cf. EC 2.7.1.181, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709–35718. [DOI] [PMID: 15184370] |
2. |
Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662–30672. [DOI] [PMID: 19734145] |
3. |
Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391–41401. [DOI] [PMID: 21990359] |
4. |
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. [DOI] [PMID: 25422321] |
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[EC 2.1.1.294 created 2014, modified 2018] |
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EC |
5.4.99.15 | Relevance: 84.4% |
Accepted name: |
(1→4)-α-D-glucan 1-α-D-glucosylmutase |
Reaction: |
4-[(1→4)-α-D-glucosyl]n-1-D-glucose = 1-α-D-[(1→4)-α-D-glucosyl]n-1-α-D-glucopyranoside |
Other name(s): |
malto-oligosyltrehalose synthase; maltodextrin α-D-glucosyltransferase |
Systematic name: |
(1→4)-α-D-glucan 1-α-D-glucosylmutase |
Comments: |
The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1→4)-α-D-glucans containing three or more (1→4)-α-linked D-glucose units. Not active towards maltose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 170780-49-1 |
References: |
1. |
Maruta, K., Nakada, T., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Formation of trehalose from maltooligosaccharides by a novel enzymatic system. Biosci. Biotechnol. Biochem. 59 (1995) 1829–1834. [DOI] [PMID: 8534970] |
2. |
Nakada, T., Maruta, K., Tsusaki, K., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36. Biosci. Biotechnol. Biochem. 59 (1995) 2210–2214. [PMID: 8611744] |
3. |
Nakada, T., Ikegami, S., Chaen, H., Kubota, M., Fukuda, S., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci. Biotechnol. Biochem. 60 (1996) 263–266. [DOI] [PMID: 9063973] |
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[EC 5.4.99.15 created 1999] |
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EC |
2.4.3.3 | Relevance: 84.2% |
Accepted name: |
α-N-acetylgalactosaminide α-2,6-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + glycano-(1→3)-(N-acetyl-α-D-galactosaminyl)-glycoprotein = CMP + glycano-[(2→6)-α-N-acetylneuraminyl]-(N-acetyl-D-galactosaminyl)-glycoprotein |
Systematic name: |
CMP-N-acetylneuraminate:glycano-1,3-(N-acetyl-α-D-galactosaminyl)-glycoprotein α-2,6-N-acetylneuraminyltransferase |
Comments: |
N-acetyl-α-D-galactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 71124-50-0 |
References: |
1. |
Sadler, J.E., Rearick, J.I. and Hill, R.L. Purification to homogeneity and enzymatic characterization of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 5934–5941. [PMID: 447688] |
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[EC 2.4.3.3 created 1984 as EC 2.4.99.3, modified 1986, transferred 2022 to EC 2.4.3.3] |
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EC |
2.4.1.349 | Relevance: 84.1% |
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 |
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. [DOI] [PMID: 22875852] |
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[EC 2.4.1.349 created 2017] |
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EC |
2.4.1.291 | Relevance: 84% |
Accepted name: |
N-acetylgalactosamine-N,N′-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-galactosamine + N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→4)-N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol |
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For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here |
Glossary: |
N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose |
Other name(s): |
PglJ |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:N-acetylgalactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase |
Comments: |
Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480] |
2. |
Chen, M.M., Weerapana, E., Ciepichal, E., Stupak, J., Reid, C.W., Swiezewska, E. and Imperiali, B. Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 46 (2007) 14342–14348. [DOI] [PMID: 18034500] |
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[EC 2.4.1.291 created 2012] |
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EC |
2.3.1.108 | Relevance: 83.9% |
Accepted name: |
α-tubulin N-acetyltransferase |
Reaction: |
acetyl-CoA + [α-tubulin]-L-lysine = CoA + [α-tubulin]-N6-acetyl-L-lysine |
Other name(s): |
ATAT1 (gene name); MEC17 (gene name); α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase (ambiguous); acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase |
Systematic name: |
acetyl-CoA:[α-tubulin]-L-lysine N6-acetyltransferase |
Comments: |
The enzyme is conserved from protists to mammals and is present in flowering plants. In most organisms it acetylates L-lysine at position 40 of α-tubulin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99889-90-4 |
References: |
1. |
Greer, K., Maruta, H., L'Hernault, S.W. and Rosenbaum, J.L. α-Tubulin acetylase activity in isolated Chlamydomonas flagella. J. Cell Biol. 101 (1985) 2081–2084. [PMID: 4066751] |
2. |
Akella, J.S., Wloga, D., Kim, J., Starostina, N.G., Lyons-Abbott, S., Morrissette, N.S., Dougan, S.T., Kipreos, E.T. and Gaertig, J. MEC-17 is an α-tubulin acetyltransferase. Nature 467 (2010) 218–222. [DOI] [PMID: 20829795] |
3. |
Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. and Nachury, M.V. The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 107 (2010) 21517–21522. [DOI] [PMID: 21068373] |
4. |
Taschner, M., Vetter, M. and Lorentzen, E. Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc. Natl. Acad. Sci. USA 109 (2012) 19649–19654. [DOI] [PMID: 23071318] |
5. |
Friedmann, D.R., Aguilar, A., Fan, J., Nachury, M.V. and Marmorstein, R. Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. USA 109 (2012) 19655–19660. [DOI] [PMID: 23071314] |
6. |
Kalebic, N., Sorrentino, S., Perlas, E., Bolasco, G., Martinez, C. and Heppenstall, P.A. αTAT1 is the major α-tubulin acetyltransferase in mice. Nat. Commun. 4:1962 (2013). [DOI] [PMID: 23748901] |
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[EC 2.3.1.108 created 1989, modified 2021] |
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EC
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2.4.99.22
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Transferred entry: | N-acetylglucosaminide α-(2,6)-sialyltransferase. Now EC 2.4.3.10, N-acetylglucosaminide α-(2,6)-sialyltransferase
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[EC 2.4.99.22 created 2020, deleted 2022] |
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EC |
2.4.3.10 | Relevance: 83.8% |
Accepted name: |
N-acetylglucosaminide α-(2,6)-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-β-D-glucosaminyl-R |
Other name(s): |
α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylglucosaminide 6-α-sialyltransferase; N-acetylglucosaminide (α 2→6)-sialyltransferase; ST6GlcNAc |
Systematic name: |
CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminide N-acetyl-β-D-glucosamine-6-α-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetyl-β-D-glucosamine. The enzyme from rat liver also acts on β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl residues, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Paulson, J.C., Weinstein, J. and de Souza-e-Silva, U. Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (α 2→6)-sialyltransferase in Golgi apparatus from rat liver. Eur. J. Biochem. 140 (1984) 523–530. [PMID: 6547092] |
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[EC 2.4.3.10 created 2020 as EC 2.4.99.22, transferred 2022 to EC 2.4.3.10] |
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EC |
2.4.1.380 | Relevance: 83.2% |
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 |
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. [DOI] [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. [DOI] [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. [DOI] [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 7:391 (2017). [DOI] [PMID: 28929089] |
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[EC 2.4.1.380 created 2021] |
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EC
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2.4.99.3
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Transferred entry: | α-N-acetylgalactosaminide α-2,6-sialyltransferase. Now EC 2.4.3.3, α-N-acetylgalactosaminide α-2,6-sialyltransferase
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[EC 2.4.99.3 created 1984, modified 1986, deleted 2022] |
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EC |
3.2.1.198 | Relevance: 82.8% |
Accepted name: |
α-mannan endo-1,2-α-mannanase |
Reaction: |
Hydrolysis of the terminal α-D-mannosyl-(1→3)-α-D-mannose disaccharide from α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-α-D-mannosyl side chains in fungal cell wall α-mannans. |
Systematic name: |
α-mannan 1,2-[α-D-mannosyl-(1→3)-α-D-mannose] hydrolase |
Comments: |
The enzyme, characterized from the gut bacteria Bacteroides thetaiotaomicron and Bacteroides xylanisolvens, can also catalyse the reaction of EC 3.2.1.130, glycoprotein endo-α-1,2-mannosidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hakki, Z., Thompson, A.J., Bellmaine, S., Speciale, G., Davies, G.J. and Williams, S.J. Structural and kinetic dissection of the endo-α-1,2-mannanase activity of bacterial GH99 glycoside hydrolases from Bacteroides spp. Chemistry 21 (2015) 1966–1977. [DOI] [PMID: 25487964] |
2. |
Cuskin, F., Lowe, E.C., Temple, M.J., Zhu, Y., Cameron, E.A., Pudlo, N.A., Porter, N.T., Urs, K., Thompson, A.J., Cartmell, A., Rogowski, A., Hamilton, B.S., Chen, R., Tolbert, T.J., Piens, K., Bracke, D., Vervecken, W., Hakki, Z., Speciale, G., Munoz-Munoz, J.L., Day, A., Pena, M.J., McLean, R., Suits, M.D., Boraston, A.B., Atherly, T., Ziemer, C.J., Williams, S.J., Davies, G.J., Abbott, D.W., Martens, E.C. and Gilbert, H.J. Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism. Nature 517 (2015) 165–169. [DOI] [PMID: 25567280] |
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[EC 3.2.1.198 created 2016] |
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EC |
2.4.1.306 | Relevance: 82.7% |
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 |
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. [DOI] [PMID: 16630548] |
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[EC 2.4.1.306 created 2013] |
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EC |
2.7.8.32 | Relevance: 82.7% |
Accepted name: |
3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase |
Reaction: |
UDP-xylose + 3-O-α-D-mannopyranosyl-α-D-mannopyranose = UMP + 3-O-(6-O-α-D-xylosylphospho-α-D-mannopyranosyl)-α-D-mannopyranose
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Glossary: |
O-α-D-xylosylphospho-α-D-mannopyranosyl)-α-D-mannopyranose = O-α-D-xylosylphosphono-α-D-mannopyranosyl)-α-D-mannopyranose |
Other name(s): |
XPT1 |
Systematic name: |
UDP-D-xylose:3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase |
Comments: |
Mn2+ required for activity. The enzyme is specific for mannose as an acceptor but is flexible as to the structural context of the mannosyl disaccharide. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Reilly, M.C., Levery, S.B., Castle, S.A., Klutts, J.S. and Doering, T.L. A novel xylosylphosphotransferase activity discovered in Cryptococcus neoformans. J. Biol. Chem. 284 (2009) 36118–36127. [DOI] [PMID: 19864415] |
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[EC 2.7.8.32 created 2011] |
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EC |
2.4.1.381 | Relevance: 82.6% |
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 |
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. [DOI] [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. [DOI] [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. [DOI] [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 7:391 (2017). [DOI] [PMID: 28929089] |
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[EC 2.4.1.381 created 2021] |
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EC |
2.4.1.24 | Relevance: 81.8% |
Accepted name: |
1,4-α-glucan 6-α-glucosyltransferase |
Reaction: |
Transfers an α-D-glucosyl residue in a (1→4)-α-D-glucan to the primary hydroxy group of glucose, free or combined in a (1→4)-α-D-glucan |
Other name(s): |
oligoglucan-branching glycosyltransferase; 1,4-α-D-glucan 6-α-D-glucosyltransferase; T-enzyme; D-glucosyltransferase; 1,4-α-D-glucan:1,4-α-D-glucan(D-glucose) 6-α-D-glucosyltransferase |
Systematic name: |
(1→4)-α-D-glucan:(1→4)-α-D-glucan(D-glucose) 6-α-D-glucosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-12-0 |
References: |
1. |
Abdullah, M. and Whelan, W.J. Synthesis of α-1:6-glucosidic linkages by a transglycosylase from potato. Biochem. J. 75 (1960) 12P. |
2. |
Barker, S.A. and Carrington, T.R. Studies of Aspergillus niger. Part II. Transglycosidation by Aspergillus niger. J. Chem. Soc. (Lond.) (1953) 3588–3593. |
3. |
Saroja, K., Venkataraman, R. and Giri, K.V. Transglucosidation in Penicillium chrysogenum Q-176. Isolation and identification of the oligosaccharide. Biochem. J. 60 (1955) 399–403. [PMID: 13239572] |
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[EC 2.4.1.24 created 1965] |
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EC |
3.2.1.28 | Relevance: 81.7% |
Accepted name: |
α,α-trehalase |
Reaction: |
α,α-trehalose + H2O = β-D-glucose + α-D-glucose |
Other name(s): |
trehalase |
Systematic name: |
α,α-trehalose glucohydrolase |
Comments: |
The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the α-glucosidic O-linkage of α,α-trehalose, releasing initially equimolar amounts of α- and β-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-52-9 |
References: |
1. |
Myrbäck, K. and Örtenblad, B. Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten. Biochem. Z. 291 (1937) 61–69. |
2. |
Kalf, G.F. and Rieder, S.V. The preparation and properties of trehalase. J. Biol. Chem. 230 (1958) 691–698. [PMID: 13525386] |
3. |
Hehre, E.J., Sawai, T., Brewer, C.F., Nakano, M. and Kanda, T. Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride. Biochemistry 21 (1982) 3090–3097. [PMID: 7104311] |
4. |
Mori, H., Lee, J.H., Okuyama, M., Nishimoto, M., Ohguchi, M., Kim, D., Kimura, A. and Chiba, S. Catalytic reaction mechanism based on α-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase. Biosci. Biotechnol. Biochem. 73 (2009) 2466–2473. [DOI] [PMID: 19897915] |
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[EC 3.2.1.28 created 1961, modified 2012] |
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EC |
3.2.1.207 | Relevance: 81.4% |
Accepted name: |
mannosyl-oligosaccharide α-1,3-glucosidase |
Reaction: |
(1) Glc2Man9GlcNAc2-[protein] + H2O = GlcMan9GlcNAc2-[protein] + β-D-glucopyranose (2) GlcMan9GlcNAc2-[protein] + H2O = Man9GlcNAc2-[protein] + β-D-glucopyranose |
Glossary: |
Glc2Man9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]
GlcMan9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]
Man9GlcNAc2-[protein] = {α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein] |
Other name(s): |
ER glucosidase II; α-glucosidase II; trimming glucosidase II; ROT2 (gene name); GTB1 (gene name); GANAB (gene name); PRKCSH (gene name) |
Systematic name: |
Glc2Man9GlcNAc2-[protein] 3-α-glucohydrolase (configuration-inverting) |
Comments: |
This eukaryotic enzyme cleaves off sequentially the two α-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Trombetta, E.S., Simons, J.F. and Helenius, A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 271 (1996) 27509–27516. [DOI] [PMID: 8910335] |
2. |
Ziak, M., Meier, M., Etter, K.S. and Roth, J. Two isoforms of trimming glucosidase II exist in mammalian tissues and cell lines but not in yeast and insect cells. Biochem. Biophys. Res. Commun. 280 (2001) 363–367. [DOI] [PMID: 11162524] |
3. |
Wilkinson, B.M., Purswani, J. and Stirling, C.J. Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J. Biol. Chem. 281 (2006) 6325–6333. [DOI] [PMID: 16373354] |
4. |
Mora-Montes, H.M., Bates, S., Netea, M.G., Diaz-Jimenez, D.F., Lopez-Romero, E., Zinker, S., Ponce-Noyola, P., Kullberg, B.J., Brown, A.J., Odds, F.C., Flores-Carreon, A. and Gow, N.A. Endoplasmic reticulum α-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction. Eukaryot Cell 6 (2007) 2184–2193. [DOI] [PMID: 17933909] |
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[EC 3.2.1.207 created 2018] |
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EC |
2.4.1.348 | Relevance: 80.1% |
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 |
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. [DOI] [PMID: 22875852] |
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[EC 2.4.1.348 created 2017] |
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EC |
2.4.1.60 | Relevance: 80% |
Accepted name: |
CDP-abequose:α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase |
Reaction: |
CDP-α-D-abequose + α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = CDP + α-D-Abe-(1→3)-α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und |
Glossary: |
D-abequose = 3,6-deoxy-D-xylo-hexose = 3,6-deoxy-D-galactose = 3-deoxy-D-fucose
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
α-D-Abe-(1→3)-α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-abequopyranosyl-(1→3)-α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
wbaV (gene name); rfbV (gene name); trihexose diphospholipid abequosyltransferase; abequosyltransferase (ambiguous); CDP-α-D-abequose:Man(α1→4)Rha(α1→3)Gal(β-1)-diphospholipid D-abequosyltransferase |
Systematic name: |
CDP-α-D-abequose:α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3III-α-abequosyltransferase (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-D3 groups. The enzyme is able to transfer abequose, paratose, or tyvelose, depending on the availability of the specific dideoxyhexose in a particular strain. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-67-1 |
References: |
1. |
Osborn, M.J. and Weiner, I.M. Biosynthesis of a bacterial lipopolysaccharide. VI. Mechanism of incorporation of abequose into the O-antigen of Salmonella typhimurium. J. Biol. Chem. 243 (1968) 2631–2639. [PMID: 4297268] |
2. |
Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084–4088. [DOI] [PMID: 7541787] |
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[EC 2.4.1.60 created 1972, modified 2012, modified 2021] |
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EC |
2.3.1.122 | Relevance: 79.9% |
Accepted name: |
trehalose O-mycolyltransferase |
Reaction: |
2 α,α-trehalose 6-mycolate = α,α-trehalose + α,α-trehalose 6,6′-bismycolate |
Other name(s): |
α,α’-trehalose 6-monomycolate:α,α’-trehalose mycolyltransferase; α,α’-trehalose-6-mycolate:α,α’-trehalose-6-mycolate 6′-mycolyltransferase |
Systematic name: |
α,α-trehalose-6-mycolate:α,α-trehalose-6-mycolate 6′-mycolyltransferase |
Comments: |
Catalyses the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate. Trehalose 6-palmitate can also act as donor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 111694-11-2 |
References: |
1. |
Sathyamoorthy, N. and Takayama, K. Purification and characterization of a novel mycolic acid exchange enzyme from Mycobacterium smegmatis. J. Biol. Chem. 262 (1987) 13417–13423. [PMID: 3654621] |
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[EC 2.3.1.122 created 1990] |
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EC |
2.4.1.101 | Relevance: 79.5% |
Accepted name: |
α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein] |
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For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here |
Glossary: |
Man5GlcNAc2-[protein] = α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]
Man5GlcNAc3-[protein]= β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein] |
Other name(s): |
MGAT1 (gene name); N-acetylglucosaminyltransferase I; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; uridine diphosphoacetylglucosamine-α-1,3-mannosylglycoprotein β-1,2-N-acetylglucosaminyltransferase; UDP-N-acetylglucosaminyl:α-1,3-D-mannoside-β-1,2-N-acetylglucosaminyltransferase I; UDP-N-acetylglucosaminyl:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I; α-1,3-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTI; GlcNAc-T I; UDP-N-acetyl-D-glucosamine:3-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→3)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting) |
Comments: |
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act. While the natural substrate (produced by EC 3.2.1.113, mannosyl-oligosaccharide 1,2-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→3)-β-D-Man-R. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102576-81-8 |
References: |
1. |
Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity. J. Biol. Chem. 255 (1980) 4885–4893. [PMID: 6445358] |
2. |
Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa. Biochemistry 20 (1981) 967–976. [PMID: 6452163] |
3. |
Oppenheimer, C.L. and Hill, R.L. Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase. J. Biol. Chem. 256 (1981) 799–804. [PMID: 6450208] |
4. |
Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. The nonidentity of porcine N-acetylglucosaminyltransferases I and II. J. Biol. Chem. 256 (1981) 11477–11482. [PMID: 6457827] |
5. |
Miyagi, T. and Tsuiki, S. Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas. Biochim. Biophys. Acta 661 (1981) 148–157. [DOI] [PMID: 6170335] |
6. |
Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476] |
7. |
Vella, G.J., Paulsen, H. and Schachter, H. Control of glycoprotein synthesis. IX. A terminal Man alphal-3Man β1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: α-D-mannoside (GlcNAc to Man α1-3) β2-N-acetylglucosaminyltransferase I. Can. J. Biochem. Cell Biol. 62 (1984) 409–417. [PMID: 6235906] |
8. |
Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H. and Rini, J.M. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J. 19 (2000) 5269–5280. [DOI] [PMID: 11032794] |
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[EC 2.4.1.101 created 1983, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018] |
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EC |
2.4.1.393 | Relevance: 79.4% |
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 |
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 6:108 (2023). [DOI] [PMID: 36707645] |
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[EC 2.4.1.393 created 2023] |
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EC |
2.7.7.99 | Relevance: 79.3% |
Accepted name: |
N-acetyl-α-D-muramate 1-phosphate uridylyltransferase |
Reaction: |
UDP + N-acetyl-α-D-muramate 1-phosphate = UDP-N-acetyl-α-D-muramate + phosphate |
Glossary: |
N-acetyl-α-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose |
Other name(s): |
murU (gene name) |
Systematic name: |
UDP:N-acetyl-α-D-muramate 1-phosphate uridylyltransferase |
Comments: |
The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gisin, J., Schneider, A., Nagele, B., Borisova, M. and Mayer, C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat. Chem. Biol. 9 (2013) 491–493. [DOI] [PMID: 23831760] |
2. |
Renner-Schneck, M., Hinderberger, I., Gisin, J., Exner, T., Mayer, C. and Stehle, T. Crystal structure of the N-acetylmuramic acid α-1-phosphate (MurNAc-α1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens. J. Biol. Chem. 290 (2015) 10804–10813. [DOI] [PMID: 25767118] |
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[EC 2.7.7.99 created 2017] |
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EC |
3.2.1.130 | Relevance: 79.1% |
Accepted name: |
glycoprotein endo-α-1,2-mannosidase |
Reaction: |
GlcMan9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + α-D-glucosyl-(1→3)-α-D-mannopyranose |
Glossary: |
GlcMan9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc}-N-Asn-[protein]
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) = {α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc}-N-Asn-[protein] |
Other name(s): |
glucosylmannosidase; endo-α-D-mannosidase; endo-α-mannosidase; endomannosidase; glucosyl mannosidase; MANEA (gene name); glycoprotein glucosylmannohydrolase |
Systematic name: |
glycoprotein glucosylmannohydrolase (configuration-retaining) |
Comments: |
The enzyme catalyses the hydrolysis of the terminal α-D-glucosyl-(1→3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus. The name for the isomer is based on a nomenclature proposed by Prien et al [7]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 108022-16-8 |
References: |
1. |
Lubas, W.A. and Spiro, R.G. Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem. 262 (1987) 3775–3781. [PMID: 3818665] |
2. |
Tulsiani, D.R.P., Coleman, V.P. and Touster, O. Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and endomannosidase (glucosyl mannosidase). Arch. Biochem. Biophys. 277 (1990) 114–121. [DOI] [PMID: 2407194] |
3. |
Hiraizumi, S., Spohr, U. and Spiro, R.G. Ligand affinity chromatographic purification of rat liver Golgi endomannosidase. J. Biol. Chem. 269 (1994) 4697–4700. [PMID: 8106437] |
4. |
Spiro, M.J., Bhoyroo, V.D. and Spiro, R.G. Molecular cloning and expression of rat liver endo-α-mannosidase, an N-linked oligosaccharide processing enzyme. J. Biol. Chem. 272 (1997) 29356–29363. [DOI] [PMID: 9361017] |
5. |
Hamilton, S.R., Li, H., Wischnewski, H., Prasad, A., Kerley-Hamilton, J.S., Mitchell, T., Walling, A.J., Davidson, R.C., Wildt, S. and Gerngross, T.U. Intact α-1,2-endomannosidase is a typical type II membrane protein. Glycobiology 15 (2005) 615–624. [DOI] [PMID: 15677381] |
6. |
Hardt, B., Volker, C., Mundt, S., Salska-Navarro, M., Hauptmann, M. and Bause, E. Human endo-α1,2-mannosidase is a Golgi-resident type II membrane protein. Biochimie 87 (2005) 169–179. [DOI] [PMID: 15760709] |
7. |
Prien, J.M., Ashline, D.J., Lapadula, A.J., Zhang, H. and Reinhold, V.N. The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS. J. Am. Soc. Mass Spectrom. 20 (2009) 539–556. [DOI] [PMID: 19181540] |
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[EC 3.2.1.130 created 1990, modified 2017] |
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EC |
2.4.1.387 | Relevance: 79% |
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 |
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 14553982] |
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[EC 2.4.1.387 created 2022] |
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EC |
2.4.1.287 | Relevance: 78.7% |
Accepted name: |
rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,4/1,5-galactofuranosyltransferase |
Reaction: |
2 UDP-α-D-galactofuranose + α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol = 2 UDP + β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol (overall reaction) (1a) UDP-α-D-galactofuranose + α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol = UDP + β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol (1b) UDP-α-D-galactofuranose + β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol = UDP + β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol |
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For diagram of galactofuranan biosynthesis, click here |
Other name(s): |
arabinogalactan galactofuranosyl transferase 1; GlfT1 |
Systematic name: |
UDP-α-D-galactofuranose:α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-β/4-β-galactofuranosyltransferase (configuration-inverting) |
Comments: |
Isolated from the bacteria Mycobacterium tuberculosis and M. smegmatis, the enzyme has dual β-(1→4) and β-(1→5) transferase action. Involved in the formation of the cell wall in mycobacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mikusová, K., Belánová, M., Korduláková, J., Honda, K., McNeil, M.R., Mahapatra, S., Crick, D.C. and Brennan, P.J. Identification of a novel galactosyl transferase involved in biosynthesis of the mycobacterial cell wall. J. Bacteriol. 188 (2006) 6592–6598. [DOI] [PMID: 16952951] |
2. |
Belánová, M., Dianisková, P., Brennan, P.J., Completo, G.C., Rose, N.L., Lowary, T.L. and Mikusová, K. Galactosyl transferases in mycobacterial cell wall synthesis. J. Bacteriol. 190 (2008) 1141–1145. [DOI] [PMID: 18055597] |
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[EC 2.4.1.287 created 2012, modified 2017] |
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EC |
2.4.1.343 | Relevance: 78.6% |
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 |
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. [DOI] [PMID: 27196310] |
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[EC 2.4.1.343 created 2017] |
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EC |
2.4.1.290 | Relevance: 78.3% |
Accepted name: |
N,N′-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-galactosamine + N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol |
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For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here |
Glossary: |
N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose |
Other name(s): |
PglA |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase |
Comments: |
Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480] |
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[EC 2.4.1.290 created 2012] |
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EC |
2.4.1.261 | Relevance: 78.1% |
Accepted name: |
dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase |
Reaction: |
dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate |
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For diagram of dolichyltetradecasaccharide biosynthesis, click here |
Other name(s): |
ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase |
Systematic name: |
dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting) |
Comments: |
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues: the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [PMID: 19451548] |
2. |
Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956] |
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[EC 2.4.1.261 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.261, modified 2012] |
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EC |
3.2.1.106 | Relevance: 77.8% |
Accepted name: |
mannosyl-oligosaccharide glucosidase |
Reaction: |
Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + β-D-glucopyranose |
Glossary: |
Glc3Man9GlcNAc2 = [α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Glc2Man9GlcNAc2-[protein] = [α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein] |
Other name(s): |
Glc3Man9NAc2 oligosaccharide glucosidase; trimming glucosidase I; CWH41 (gene name); MOGS (gene name); mannosyl-oligosaccharide glucohydrolase |
Systematic name: |
Glc3Man9GlcNAc2-[protein] glucohydrolase (configuration-inverting) |
Comments: |
This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal α-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78413-07-7 |
References: |
1. |
Elting, J.J., Chen, W.W. and Lennarz, J. Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains. J. Biol. Chem. 255 (1980) 2325–2331. [PMID: 7358674] |
2. |
Grinna, L.S. and Robbins, P.W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J. Biol. Chem. 254 (1979) 8814–8818. [PMID: 479161] |
3. |
Kilker, R.D., Saunier, B., Tkacz, J.S. and Herscovics, A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem. 256 (1981) 5299–5603. [PMID: 7014569] |
4. |
Grinna, L.S. and Robbins, P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255 (1980) 2255–2258. [PMID: 7358666] |
5. |
Mark, M.J. and Kornfeld, S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch. Biochem. Biophys. 199 (1980) 249–258. [DOI] [PMID: 7356331] |
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[EC 3.2.1.106 created 1984, modified 2018] |
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EC |
2.4.1.260 | Relevance: 77.8% |
Accepted name: |
dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase |
Reaction: |
dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate |
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For diagram of dolichyltetradecasaccharide biosynthesis, click here |
Other name(s): |
ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl α6-mannosyltransferase; EBS4; Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase |
Systematic name: |
dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting) |
Comments: |
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956] |
2. |
Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21 (2009) 3792–3802. [DOI] [PMID: 20023196] |
3. |
Cipollo, J.F. and Trimble, R.B. The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12 (2002) 749–762. [PMID: 12460943] |
4. |
Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum. Mol. Genet. 11 (2002) 2331–2339. [DOI] [PMID: 12217961] |
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[EC 2.4.1.260 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.160, modified 2012] |
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EC |
2.4.1.383 | Relevance: 77.6% |
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 |
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. [DOI] [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. [DOI] |
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. [DOI] [PMID: 10520265] |
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[EC 2.4.1.383 created 2021] |
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EC |
2.4.1.155 | Relevance: 77.5% |
Accepted name: |
α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] |
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For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here |
Other name(s): |
MGAT5 (gene name); N-acetylglucosaminyltransferase V; α-mannoside β-1,6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-mannoside β1→6-acetylglucosaminyltransferase; UDP-N-acetylglucosamine:α-mannoside-β1,6 N-acetylglucosaminyltransferase; α-1,3(6)-mannosylglycoprotein β-1,6-N-acetylglucosaminyltransferase; GnTV; GlcNAc-T V; UDP-N-acetyl-D-glucosamine:6-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting) |
Comments: |
Requires Mg2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. It catalyses the addition of N-acetylglucosamine in β 1-6 linkage to the α-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83588-90-3 |
References: |
1. |
Cummings, R.D., Trowbridge, I.S. and Kornfeld, S. A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: α-D-mannoside β1,6 N-acetylglucosaminyltransferase. J. Biol. Chem. 257 (1982) 13421–13427. [PMID: 6216250] |
2. |
Hindsgaul, O., Tahir, S.H., Srivastava, O.P. and Pierce, M. The trisaccharide β-D-GlcpNAc-(1→2)-α-D-Manp-(1→6)-β-D-Manp, as its 8-methoxycarbonyloctyl glycoside, is an acceptor selective for N-acetylglucosaminyltransferase V. Carbohydr. Res. 173 (1988) 263–272. [DOI] [PMID: 2834054] |
3. |
Shoreibah, M.G., Hindsgaul, O. and Pierce, M. Purification and characterization of rat kidney UDP-N-acetylglucosamine: α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 2920–2927. [PMID: 1531335] |
4. |
Gu, J., Nishikawa, A., Tsuruoka, N., Ohno, M., Yamaguchi, N., Kangawa, K. and Taniguchi, N. Purification and characterization of UDP-N-acetylglucosamine: α-6-D-mannoside β 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. J. Biochem. 113 (1993) 614–619. [PMID: 8393437] |
5. |
Park, C., Jin, U.H., Lee, Y.C., Cho, T.J. and Kim, C.H. Characterization of UDP-N-acetylglucosamine:α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B. Arch. Biochem. Biophys. 367 (1999) 281–288. [PMID: 10395745] |
6. |
Saito, T., Miyoshi, E., Sasai, K., Nakano, N., Eguchi, H., Honke, K. and Taniguchi, N. A secreted type of β 1,6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity. J. Biol. Chem. 277 (2002) 17002–17008. [PMID: 11872751] |
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[EC 2.4.1.155 created 1986, modified 2001, modified 2018] |
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EC |
5.4.99.66 | Relevance: 77.3% |
Accepted name: |
α-onocerin synthase |
Reaction: |
pre-α-onocerin = α-onocerin |
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For diagram of α-onocerin biosynthesis, click here |
Glossary: |
α-onocerin = 8,14-secogammacera-8(26),14(27)-diene-3β,21α-diol
pre-α-onocerin = (21S)-21,22-epoxypolypoda-8(26)-13,17-trien-3β-ol |
Other name(s): |
LCD |
Systematic name: |
pre-α-onocerin mutase (cyclizing, α-onocerin-forming) |
Comments: |
Isolated from the plant Lycopodium clavatum. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Araki, T., Saga, Y., Marugami, M., Otaka, J., Araya, H., Saito, K., Yamazaki, M., Suzuki, H. and Kushiro, T. Onocerin biosynthesis requires two highly dedicated triterpene cyclases in a fern Lycopodium clavatum. ChemBioChem 17 (2016) 288–290. [DOI] [PMID: 26663356] |
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[EC 5.4.99.66 created 2017] |
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