The Enzyme Database

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EC 2.4.1.12     
Accepted name: cellulose synthase (UDP-forming)
Reaction: UDP-α-D-glucose + [(1→4)-β-D-glucosyl]n = UDP + [(1→4)-β-D-glucosyl]n+1
Other name(s): UDP-glucose—β-glucan glucosyltransferase; UDP-glucose-cellulose glucosyltransferase; GS-I; β-1,4-glucosyltransferase; uridine diphosphoglucose-1,4-β-glucan glucosyltransferase; β-1,4-glucan synthase; β-1,4-glucan synthetase; β-glucan synthase; 1,4-β-D-glucan synthase; 1,4-β-glucan synthase; glucan synthase; UDP-glucose-1,4-β-glucan glucosyltransferase; uridine diphosphoglucose-cellulose glucosyltransferase; UDP-glucose:1,4-β-D-glucan 4-β-D-glucosyltransferase; UDP-glucose:(1→4)-β-D-glucan 4-β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:(1→4)-β-D-glucan 4-β-D-glucosyltransferase (configuration-inverting)
Comments: Involved in the synthesis of cellulose. A similar enzyme utilizes GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-19-4
References:
1.  Glaser, L. The synthesis of cellulose in cell-free extracts of Acetobacter xylinum. J. Biol. Chem. 232 (1958) 627–636. [PMID: 13549448]
[EC 2.4.1.12 created 1961]
 
 
EC 2.4.1.120     
Accepted name: sinapate 1-glucosyltransferase
Reaction: UDP-α-D-glucose + sinapate = UDP + 1-O-sinapoyl-β-D-glucose
Glossary: sinapate = (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate
Other name(s): uridine diphosphoglucose-sinapate glucosyltransferase; UDP-glucose:sinapic acid glucosyltransferase; uridine 5′-diphosphoglucose-hydroxycinnamic acid acylglucosyltransferase; UDP-glucose:sinapate D-glucosyltransferase
Systematic name: UDP-α-D-glucose:sinapate D-glucosyltransferase
Comments: Some other hydroxycinnamates, including 4-coumarate, ferulate and caffeate, can act as acceptors, but more slowly. Only glucose esters, not glucosides, are formed (cf. EC 2.4.1.126 hydroxycinnamate 4-β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 74082-53-4
References:
1.  Strack, D. Enzymatic synthesis of 1-sinapoylglucose from free sinapic acid and UDP-glucose by a cell free system from Raphanus sativus seedlings. Z. Naturforsch. C: Biosci. 35 (1980) 204–208.
[EC 2.4.1.120 created 1984]
 
 
EC 2.4.1.121     
Accepted name: indole-3-acetate β-glucosyltransferase
Reaction: UDP-glucose + (indol-3-yl)acetate = UDP + 1-O-(indol-3-yl)acetyl-β-D-glucose
Other name(s): uridine diphosphoglucose-indoleacetate glucosyltransferase; UDPG-indol-3-ylacetyl glucosyl transferase; UDP-glucose:indol-3-ylacetate glucosyltransferase; indol-3-ylacetylglucose synthase; UDP-glucose:indol-3-ylacetate glucosyl-transferase; IAGlu synthase; IAA-glucose synthase; UDP-glucose:indole-3-acetate β-D-glucosyltransferase
Systematic name: UDP-glucose:(indol-3-yl)acetate β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74082-56-7
References:
1.  Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of 1-O-indol-3-ylacetyl-β-D-glucose and indol-3-ylacetyl-myo-inositol. Biochem. J. 207 (1982) 273–281. [PMID: 6218801]
[EC 2.4.1.121 created 1984]
 
 
EC 2.4.1.122     
Accepted name: N-acetylgalactosaminide β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-galactosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R
Other name(s): glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase; uridine diphosphogalactose-mucin β-(1→3)-galactosyltransferase; UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase; UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase; wbnJ (gene name); wbiP (gene name); C1GALT1 (gene name); UDP-α-D-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-galactosaminyl-R β-1,3-galactosyltransferase (configuration-inverting)
Comments: The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97089-61-7
References:
1.  Hesford, F.J., Berger, E.G. and van den Eijnden, D.H. Identification of the product formed by human erythrocyte galactosyltransferase. Biochim. Biophys. Acta 659 (1981) 302–311. [DOI] [PMID: 6789880]
2.  Mendicino, J., Sivakami, S., Davila, M. and Chandrasekaran, E.V. Purification and properties of UDP-gal:N-acetylgalactosaminide mucin:β1,3-galactosyltransferase from swine trachea mucosa. J. Biol. Chem. 257 (1982) 3987–3994. [PMID: 6801057]
3.  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]
4.  Ju, T., Brewer, K., D'Souza, A., Cummings, R.D. and Canfield, W.M. Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277 (2002) 178–186. [DOI] [PMID: 11677243]
5.  Yi, W., Perali, R.S., Eguchi, H., Motari, E., Woodward, R. and Wang, P.G. Characterization of a bacterial β-1,3-galactosyltransferase with application in the synthesis of tumor-associated T-antigen mimics. Biochemistry 47 (2008) 1241–1248. [DOI] [PMID: 18179256]
6.  Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]
[EC 2.4.1.122 created 1984 (EC 2.4.1.307 created 2013, incorporated 2016), modified 2016]
 
 
EC 2.4.1.123     
Accepted name: inositol 3-α-galactosyltransferase
Reaction: UDP-α-D-galactose + myo-inositol = UDP + O-α-D-galactosyl-(1→3)-1D-myo-inositol
For diagram of stachyose biosynthesis, click here
Glossary: O-α-D-galactosyl-(1→3)-1D-myo-inositol = galactinol
Other name(s): UDP-D-galactose:inositol galactosyltransferase; UDP-galactose:myo-inositol 1-α-D-galactosyltransferase; UDPgalactose:myo-inositol 1-α-D-galactosyltransferase; galactinol synthase; inositol 1-α-galactosyltransferase; uridine diphosphogalactose-inositol galactosyltransferase; GolS; UDP-galactose:myo-inositol 3-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:myo-inositol 3-α-D-galactosyltransferase
Comments: An enzyme from plants involved in the formation of raffinose and stachyose [cf. EC 2.4.1.67 (galactinol—raffinose galactosyltransferase) and EC 2.4.1.82 (galactinol—sucrose galactosyltransferase)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79955-89-8
References:
1.  Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C. Partial characterization of the galactinol forming enzyme from leaves of Cucumis sativus L. Plant Sci. Lett. 23 (1981) 25–33.
[EC 2.4.1.123 created 1984, modified 2003]
 
 
EC 2.4.1.124      
Transferred entry: N-acetyllactosamine 3-α-galactosyltransferase. Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase
[EC 2.4.1.124 created 1984, deleted 2002]
 
 
EC 2.4.1.125     
Accepted name: sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase
Reaction: (1) sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + [(1→6)-α-D-glucosyl]n+1
(2) sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + (1→3)-α-D-glucosyl-[(1→6)-α-D-glucosyl]n
Other name(s): water-soluble-glucan synthase (misleading); GTF-I; GTF-S; GTF-SI; sucrose-1,6-α-glucan 3(6)-α-glucosyltransferase; sucrose:1,6-α-D-glucan 3-α- and 6-α-glucosyltransferase; sucrose:1,6-, 1,3-α-D-glucan 3-α- and 6-α-D-glucosyltransferase; sucrose:1,6-α-D-glucan 3(6)-α-D-glucosyltransferase; gtfB (gene name); gtfC (gene name); gtfD (gene name)
Systematic name: sucrose:(1→6)-α-D-glucan 3(6)-α-D-glucosyltransferase
Comments: The enzyme was characterized from the dental caries bacterium Streptococcus mutans. It transfers glucosyl residues from sucrose to either the 6- or the 3-positions of glucose residues in glucans, producing a highly-branched extracellular D-glucan polymers that promote attachment of the bacteria to teeth. Three types of the enzyme have been described; the insoluble polymers produced by GTF-I and GTF-SI contain 85% α(1→3) bonds and 15% α(1→6) bonds, while the soluble polymers produced by GTF-S contain only 30% of α(1→3) bonds and 70% α(1→6) bonds. cf. EC 2.4.1.5, dextransucrase [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81725-87-3
References:
1.  Mukasa, H., Shimamura, A. and Tsumori, H. Purification and characterization of basic glucosyltransferase from Streptococcus mutans serotype c. Biochim. Biophys. Acta 719 (1982) 81–89. [DOI] [PMID: 6216919]
2.  Shimamura, A., Tsumori, H. and Mukasa, H. Purification and properties of Streptococcus mutans extracellular glucosyltransferase. Biochim. Biophys. Acta 702 (1982) 72–80. [DOI] [PMID: 6461359]
3.  Tsumori, H., Shimamura, A. and Mukasa, H. Purification and properties of extracellular glucosyltransferase synthesizing 1,6-, 1,3-α-D-glucan from Streptococcus mutans serotype a. J. Gen. Microbiol. 131 (1985) 3347–3353. [DOI] [PMID: 2937877]
4.  Fujiwara, T., Tamesada, M., Bian, Z., Kawabata, S., Kimura, S. and Hamada, S. Deletion and reintroduction of glucosyltransferase genes of Streptococcus mutans and role of their gene products in sucrose dependent cellular adherence. Microb Pathog 20 (1996) 225–233. [DOI] [PMID: 8737492]
5.  Monchois, V., Willemot, R.M. and Monsan, P. Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol. Rev. 23 (1999) 131–151. [DOI] [PMID: 10234842]
6.  Ito, K., Ito, S., Shimamura, T., Weyand, S., Kawarasaki, Y., Misaka, T., Abe, K., Kobayashi, T., Cameron, A.D. and Iwata, S. Crystal structure of glucansucrase from the dental caries pathogen Streptococcus mutans. J. Mol. Biol. 408 (2011) 177–186. [DOI] [PMID: 21354427]
[EC 2.4.1.125 created 1984]
 
 
EC 2.4.1.126     
Accepted name: hydroxycinnamate 4-β-glucosyltransferase
Reaction: UDP-glucose + trans-4-hydroxycinnamate = UDP + 4-O-β-D-glucosyl-4-hydroxycinnamate
Other name(s): uridine diphosphoglucose-hydroxycinnamate glucosyltransferase; UDP-glucose-hydroxycinnamate glucosyltransferase; hydroxycinnamoyl glucosyltransferase
Systematic name: UDP-glucose:trans-4-hydroxycinnamate 4-O-β-D-glucosyltransferase
Comments: Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120 sinapate 1-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77848-85-2
References:
1.  Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K. Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from tomato fruits. Z. Naturforsch. C: Biosci. 35 (1980) 967–972.
[EC 2.4.1.126 created 1984]
 
 
EC 2.4.1.127     
Accepted name: monoterpenol β-glucosyltransferase
Reaction: UDP-glucose + (-)-menthol = UDP + (-)-menthyl O-β-D-glucoside
For diagram of menthol biosynthesis, click here
Other name(s): uridine diphosphoglucose-monoterpenol glucosyltransferase; UDPglucose:monoterpenol glucosyltransferase
Systematic name: UDP-glucose:(-)-menthol O-β-D-glucosyltransferase
Comments: (+)-Neomenthol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78990-64-4
References:
1.  Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K. Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from tomato fruits. Z. Naturforsch. C: Biosci. 35 (1980) 967–972.
[EC 2.4.1.127 created 1984]
 
 
EC 2.4.1.128     
Accepted name: scopoletin glucosyltransferase
Reaction: UDP-glucose + scopoletin = UDP + scopolin
Other name(s): uridine diphosphoglucose-scopoletin glucosyltransferase; UDP-glucose:scopoletin glucosyltransferase; SGTase
Systematic name: UDP-glucose:scopoletin O-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81210-69-7
References:
1.  Hino, F., Okazaki, M. and Miura, Y. Effect of 2,4-dichlorophenoxyacetic acid on glucosylation of scopoletin to scopolin in tobacco tissue-culture. Plant Physiol. 69 (1982) 810–813. [PMID: 16662301]
[EC 2.4.1.128 created 1984]
 
 
EC 2.4.1.129     
Accepted name: peptidoglycan glycosyltransferase
Reaction: [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
Glossary: Mur2Ac = N-acetylmuramic acid
Other name(s): PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase
Systematic name: [poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-04-2
References:
1.  Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018–5022. [PMID: 6802846]
2.  Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079–1093. [PMID: 9841666]
3.  van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25. [DOI] [PMID: 11320055]
[EC 2.4.1.129 created 1984, modified 2002]
 
 


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