The Enzyme Database

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EC 2.4.1.1     
Accepted name: phosphorylase
Reaction: [(1→4)-α-D-glucosyl]n + phosphate = [(1→4)-α-D-glucosyl]n-1 + α-D-glucose 1-phosphate
For diagram of reaction, click here
Other name(s): muscle phosphorylase a and b; amylophosphorylase; polyphosphorylase; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; glycogen phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase
Systematic name: (1→4)-α-D-glucan:phosphate α-D-glucosyltransferase
Comments: The accepted name should be qualified in each instance by adding the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, glycogen phosphorylase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9035-74-9
References:
1.  Baum, H. and Gilbert, G.A. A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme. Nature 171 (1953) 983–984. [PMID: 13063502]
2.  Chen, G.S. and Segel, I.H. Purification and properties of glycogen phosphorylase from Escherichia coli. Arch. Biochem. Biophys. 127 (1968) 175–186. [PMID: 4878695]
3.  Cowgill, R.W. Lobster muscle phosphorylase: purfication and properties. J. Biol. Chem. 234 (1959) 3146–3153. [PMID: 13812491]
4.  Fischer, E.H., Pocker, A. and Saari, J.C. The structure, function and control of glycogen phosphorylase. In: Campbell, P.N. and Greville, G.D. (Eds), Essays in Biochemistry, vol. 6, Academic Press, London and New York, 1970, pp. 23–68.
5.  Green, A.A. and Cori, G.T. Crystalline muscle phosphorylase. I. Preparation, properties, and molecular weight. J. Biol. Chem. 151 (1943) 21–29.
6.  Hanes, C.S. The breakdown and synthesis of starch by an enzyme from pea seeds. Proc. R. Soc. Lond. B Biol. Sci. 128 (1940) 421–450.
[EC 2.4.1.1 created 1961]
 
 
EC 2.4.1.2     
Accepted name: dextrin dextranase
Reaction: [(1→4)-α-D-glucosyl]n + [(1→6)-α-D-glucosyl]m = [(1→4)-α-D-glucosyl]n-1 + [(1→6)-α-D-glucosyl]m+1
Other name(s): dextrin 6-glucosyltransferase; dextran dextrinase; 1,4-α-D-glucan:1,6-α-D-glucan 6-α-D-glucosyltransferase
Systematic name: (1→4)-α-D-glucan:(1→6)-α-D-glucan 6-α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9032-13-7
References:
1.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
2.  Hehre, E.J. and Hamilton, D.M. Bacterial conversion of dextrin into a polysaccharide with the serological properties of dextran. Proc. Soc. Exp. Biol. Med. 71 (1949) 336–339.
3.  Hehre, E.J. and Hamilton, D.M. The biological synthesis of dextran from dextrins. J. Biol. Chem. 192 (1953) 161–174. [PMID: 14917661]
[EC 2.4.1.2 created 1961]
 
 
EC 2.4.1.3     
Deleted entry:  amylomaltase. Now included with EC 2.4.1.25, 4-α-glucanotransferase
[EC 2.4.1.3 created 1961, deleted 1972]
 
 
EC 2.4.1.4     
Accepted name: amylosucrase
Reaction: sucrose + [(1→4)-α-D-glucosyl]n = D-fructose + [(1→4)-α-D-glucosyl]n+1
Other name(s): sucrose—glucan glucosyltransferase; sucrose-1,4-α-glucan glucosyltransferase; sucrose:1,4-α-D-glucan 4-α-D-glucosyltransferase
Systematic name: sucrose:(1→4)-α-D-glucan 4-α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9032-11-5
References:
1.  Feingold, D.S., Avigad, G. and Hestrin, S. Enzymic synthesis and reactions of a sucrose isomer α-D-galactopyranosyl-β-D-fructofuranoside. J. Biol. Chem. 224 (1957) 295–307. [PMID: 13398406]
2.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
3.  Hehre, E.J., Hamilton, D.M. and Carlson, A.S. Synthesis of a polsaccharide of the starch glycogen class from sucrose by a cell-free, bacterial enzyme system (amylosucrase). J. Biol. Chem. 177 (1949) 267–279.
[EC 2.4.1.4 created 1961]
 
 
EC 2.4.1.5     
Accepted name: dextransucrase
Reaction: sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + [(1→6)-α-D-glucosyl]n+1
Other name(s): sucrose 6-glucosyltransferase; SGE; CEP; sucrose-1,6-α-glucan glucosyltransferase; sucrose:1,6-α-D-glucan 6-α-D-glucosyltransferase
Systematic name: sucrose:(1→6)-α-D-glucan 6-α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9032-14-8
References:
1.  Bailey, R.W. Transglucosidase activity of rumen strains of Streptococcus bovis. 2. Isolation and properties of dextransucrase. Biochem. J. 72 (1959) 42–49. [PMID: 13651133]
2.  Bailey, R.W., Barker, S.A., Bourne, E.J. and Stacey, M. Immunopolysaccharides. Part VI. The isolation and properties of the dextransucrase of Betacoccus arabinosaceous. J. Chem. Soc. (Lond.) (1957) 3530–3536.
3.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
[EC 2.4.1.5 created 1961]
 
 
EC 2.4.1.6     
Deleted entry:  maltose 3-glycosyltransferase
[EC 2.4.1.6 created 1961, deleted 1972]
 
 
EC 2.4.1.7     
Accepted name: sucrose phosphorylase
Reaction: sucrose + phosphate = D-fructose + α-D-glucose 1-phosphate
Other name(s): sucrose glucosyltransferase; disaccharide glucosyltransferase
Systematic name: sucrose:phosphate α-D-glucosyltransferase
Comments: In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose.
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, CAS registry number: 9074-06-0
References:
1.  Doudoroff, M. Disaccharide phosphorylases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 229–236.
2.  Hassid, W.Z. and Doudoroff, M. Enzymic synthesis of sucrose and other disaccharides. Adv. Carbohydr. Chem. 5 (1950) 29–48. [PMID: 14783033]
3.  Silverstein, R., Voet, J., Reed, D. and Abeles, R.H. Purification and mechanism of action of sucrose phosphorylase. J. Biol. Chem. 242 (1967) 1338–1346. [PMID: 4381552]
[EC 2.4.1.7 created 1961]
 
 
EC 2.4.1.8     
Accepted name: maltose phosphorylase
Reaction: maltose + phosphate = D-glucose + β-D-glucose 1-phosphate
Systematic name: maltose:phosphate 1-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9030-19-7
References:
1.  Doudoroff, M. Disaccharide phosphorylases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 229–236.
2.  Fitting, C. and Doudoroff, M. Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis. J. Biol. Chem. 199 (1952) 153–163. [PMID: 12999827]
3.  Putman, E.W., Litt, C.F. and Hassid, W.Z. The structure of D-glucose-D-xylose synthesized by maltose phosphorylase. J. Am. Chem. Soc. 77 (1955) 4351–4353.
4.  Wood, B.J.B. and Rainbow, C. The maltophosphorylase of beer lactobacilli. Biochem. J. 78 (1961) 204–209. [PMID: 13786484]
[EC 2.4.1.8 created 1961]
 
 
EC 2.4.1.9     
Accepted name: inulosucrase
Reaction: sucrose + [(2→1)-β-D-fructosyl]n = glucose + [(2→1)-β-D-fructosyl]n+1
Other name(s): sucrose 1-fructosyltransferase; sucrose:2,1-β-D-fructan 1-β-D-fructosyltransferase
Systematic name: sucrose:(2→1)-β-D-fructan 1-β-D-fructosyltransferase
Comments: Converts sucrose into inulin and D-glucose. Some other sugars can act as D-fructosyl acceptors.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9030-16-4
References:
1.  Bhatia, I.S., Satvanaravana, M.N. and Srinivasan, M. Transfructosidase from Agave cera cruz Mill. Biochem. J. 61 (1955) 171–174. [PMID: 13260192]
2.  Dedonder, R. Les glucides du topinambour. III. Synthèse de glucofructosanes in vitro par des extraits de divers organes de tropinambour. Bull. Soc. Chim. Biol. 34 (1952) 171–182. [PMID: 14935737]
3.  Edelman, J. and Bacon, J.S.D. Transfructosidation in extracts of Helianthus tuberosus L. Biochem. J. 49 (1951) 529–540. [PMID: 14886320]
[EC 2.4.1.9 created 1961]
 
 
EC 2.4.1.10     
Accepted name: levansucrase
Reaction: sucrose + [6)-β-D-fructofuranosyl-(2→]n α-D-glucopyranoside = glucose +[6)-β-D-fructofuranosyl-(2→]n+1 α-D-glucopyranoside
For diagram of reaction, click here
Other name(s): sucrose 6-fructosyltransferase; β-2,6-fructosyltransferase; β-2,6-fructan:D-glucose 1-fructosyltransferase; sucrose:2,6-β-D-fructan 6-β-D-fructosyltransferase; sucrose:(2→6)-β-D-fructan 6-β-D-fructosyltransferase
Systematic name: sucrose:[6)-β-D-fructofuranosyl-(2→]n α-D-glucopyranoside 6-β-D-fructosyltransferase
Comments: Some other sugars can act as D-fructosyl acceptors.
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9030-17-5
References:
1.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
2.  Hestrin, S., Feingold, D.S. and Avigad, G. The mechanism of polysaccharide production from sucrose. 3. Donor-acceptor specificity of levansucrase from Aerobacter levanicum. Biochem. J. 64 (1956) 340–351. [PMID: 13363847]
3.  Reese, E.T. and Avigad, G. Purification of levansucrase by precipitation with levan. Biochim. Biophys. Acta 113 (1966) 79–83. [PMID: 5940635]
[EC 2.4.1.10 created 1961]
 
 
EC 2.4.1.11     
Accepted name: glycogen(starch) synthase
Reaction: UDP-glucose + [(1→4)-α-D-glucosyl]n = UDP + [(1→4)-α-D-glucosyl]n+1
For diagram of reaction, click here
Other name(s): UDP-glucose—glycogen glucosyltransferase; glycogen (starch) synthetase; UDP-glucose-glycogen glucosyltransferase; UDP-glycogen synthase; UDPG-glycogen synthetase; UDPG-glycogen transglucosylase; uridine diphosphoglucose-glycogen glucosyltransferase
Systematic name: UDP-glucose:glycogen 4-α-D-glucosyltransferase
Comments: The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9014-56-6
References:
1.  Algranati, I.D. and Cabib, E. The synthesis of glycogen in yeast. Biochim. Biophys. Acta 43 (1960) 141–142. [PMID: 13682402]
2.  Basu, D.K. and Bachhawat, B.K. Purification of uridine diphosphoglucose-glycogen transglucosylase from sheep brain. Biochim. Biophys. Acta 50 (1961) 123–128. [PMID: 13687710]
3.  Leloir, L.F. and Cardini, C.E. UDPG-glycogen transglucosylase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 317–326.
4.  Leloir, L.F. and Goldemberg, S.H. Synthesis of glycogen from uridine diphosphate glucose in liver. J. Biol. Chem. 235 (1960) 919–923. [PMID: 14415527]
5.  Pitcher, J., Smythe, C. and Cohen, P. Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle. Eur. J. Biochem. 176 (1988) 391–395. [PMID: 2970965]
[EC 2.4.1.11 created 1961]
 
 
EC 2.4.1.12     
Accepted name: cellulose synthase (UDP-forming)
Reaction: UDP-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
Systematic name: UDP-glucose:(1→4)-β-D-glucan 4-β-D-glucosyltransferase
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, IUBMB, KEGG, 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 2.4.1.13     
Accepted name: sucrose synthase
Reaction: NDP-glucose + D-fructose = NDP + sucrose
Other name(s): UDPglucose-fructose glucosyltransferase; sucrose synthetase; sucrose-UDP glucosyltransferase; sucrose-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-fructose glucosyltransferase
Systematic name: NDP-glucose:D-fructose 2-α-D-glucosyltransferase
Comments: Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose [3-9]. Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP-glucose (necessary for starch biosynthesis) [10].
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, CAS registry number: 9030-05-1
References:
1.  Avigad, G. and Milner, Y. UDP-glucose:fructose transglucosylase from sugar beet roots. Methods Enzymol. 8 (1966) 341–345.
2.  Cardini, C.E., Leloir, L.F. and Chiriboga, J. The biosynthesis of sucrose. J. Biol. Chem. 214 (1955) 149–155. [PMID: 14367373]
3.  Delmer, D.P. The purification and properties of sucrose synthetase from etiolated Phaseolus aureus seedlings. J. Biol. Chem. 247 (1972) 3822–3828. [PMID: 4624446]
4.  Murata, T., Sugiyama, T., Minamikawa, T. and Akazawa, T. Enzymic mechanism of starch synthesis in ripening rice grains. Mechanism of the sucrose-starch conversion. Arch. Biochem. Biophys. 113 (1966) 34–44. [PMID: 5941994]
5.  Nakai, T., Konishi, T., Zhang, X.-Q., Chollet, R., Tonouchi, N., Tsuchida, T., Yoshinaga, F., Mori, H., Sakai, F. and Hayashi, T. An increase in apparent affinity for sucrose of mung bean sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11. Plant Cell Physiol. 39 (1998) 1337–1341. [PMID: 10050318]
6.  Porchia, A.C., Curatti, L. and Salerno, G.L. Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence. Planta 210 (1999) 34–40. [PMID: 10592030]
7.  Ross, H.A. and Davies, H.V. Purification and characterization of sucrose synthase from the cotyledons of Vicia fava L. Plant Physiol. 100 (1992) 1008–1013. [PMID: 16653008]
8.  Silvius, J.E. and Snyder, F.W. Comparative enzymic studies of sucrose metabolism in the taproots and fibrous roots of Beta vulgaris L. Plant Physiol. 64 (1979) 1070–1073. [PMID: 16661094]
9.  Tanase, K. and Yamaki, S. Purification and characterization of two sucrose synthase isoforms from Japanese pear fruit. Plant Cell Physiol. 41 (2000) 408–414. [PMID: 10845453]
10.  Baroja-Fernández, E., Muñnoz, F.J., Saikusa, T., Rodríguez-López, M., Akazawa, T. and Pozueta-Romero, J. Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants. Plant Cell Physiol. 44 (2003) 500–509. [PMID: 12773636]
[EC 2.4.1.13 created 1961, modified 2003]
 
 
EC 2.4.1.14     
Accepted name: sucrose-phosphate synthase
Reaction: UDP-glucose + D-fructose 6-phosphate = UDP + sucrose 6F-phosphate
Other name(s): UDP-glucose—fructose-phosphate glucosyltransferase; sucrosephosphate—UDP glucosyltransferase; UDP-glucose-fructose-phosphate glucosyltransferase; SPS; uridine diphosphoglucose-fructose phosphate glucosyltransferase; sucrose 6-phosphate synthase; sucrose phosphate synthetase; sucrose phosphate-uridine diphosphate glucosyltransferase; sucrose phosphate synthase
Systematic name: UDP-glucose:D-fructose-6-phosphate 2-α-D-glucosyltransferase
Comments: Requires Mg2+ or Mn2+ for maximal activity [2]. The enzyme from Synechocystis sp. strain PCC 6803 is not specific for UDP-glucose as it can use ADP-glucose and, to a lesser extent, GDP-glucose as substrates [2]. The enzyme from rice leaves is activated by glucose 6-phosphate but that from cyanobacterial species is not [2]. While the reaction catalysed by this enzyme is reversible, the enzyme usually works in concert with EC 3.1.3.24, sucrose-phosphate phosphatase, to form sucrose, making the above reaction essentially irreversible [3]. The F in sucrose 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9030-06-2
References:
1.  Mendicino, J. Sucrose phosphate synthesis in wheat germ and green leaves. J. Biol. Chem. 235 (1960) 3347–3352. [PMID: 13769376]
2.  Curatti, L., Folco, E., Desplats, P., Abratti, G., Limones, V., Herrera-Estrella, L. and Salerno, G. Sucrose-phosphate synthase from Synechocystis sp. strain PCC 6803: identification of the spsA gene and characterization of the enzyme expressed in Escherichia coli. J. Bacteriol. 180 (1998) 6776–6779. [PMID: 9852031]
3.  Huber, S.C. and Huber, J.L. Role and regulation of sucrose-phosphate synthase in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47 (1996) 431–444. [PMID: 15012296]
4.  Cumino, A., Curatti, L., Giarrocco, L. and Salerno, G.L. Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution. FEBS Lett. 517 (2002) 19–23. [PMID: 12062401]
5.  Chua, T.K., Bujnicki, J.M., Tan, T.C., Huynh, F., Patel, B.K. and Sivaraman, J. The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode. Plant Cell 20 (2008) 1059–1072. [PMID: 18424616]
[EC 2.4.1.14 created 1961, modified 2008]
 
 
EC 2.4.1.15     
Accepted name: α,α-trehalose-phosphate synthase (UDP-forming)
Reaction: UDP-glucose + D-glucose 6-phosphate = UDP + α,α-trehalose 6-phosphate
Other name(s): UDP-glucose—glucose-phosphate glucosyltransferase; trehalosephosphate-UDP glucosyltransferase; UDP-glucose-glucose-phosphate glucosyltransferase; α,α-trehalose phosphate synthase (UDP-forming); phosphotrehalose-uridine diphosphate transglucosylase; trehalose 6-phosphate synthase; trehalose 6-phosphate synthetase; trehalose phosphate synthase; trehalose phosphate synthetase; trehalose phosphate-uridine diphosphate glucosyltransferase; trehalose-P synthetase; transglucosylase; uridine diphosphoglucose phosphate glucosyltransferase
Systematic name: UDP-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase
Comments: See also EC 2.4.1.36 [α,α-trehalose-phosphate synthase (GDP-forming)].
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9030-07-3
References:
1.  Cabib, E. and Leloir, L.F. The biosynthesis of trehalose phosphate. J. Biol. Chem. 231 (1958) 259–275. [PMID: 13538966]
2.  Candy, D.J. and Kilby, B.A. The biosynthesis of trehalose in the locust fat body. Biochem. J. 78 (1961) 531–536. [PMID: 13690400]
3.  Lornitzo, F.A. and Goldman, D.S. Purification and properties of the transglucosylase inhibitor of Mycobacterium tuberculosis. J. Biol. Chem. 239 (1964) 2730–2734. [PMID: 14216421]
4.  Murphy, T.A. and Wyatt, G.R. The enzymes of glycogen and trehalose synthesis in silk moth fat body. J. Biol. Chem. 240 (1965) 1500–1508. [PMID: 14285483]
[EC 2.4.1.15 created 1961]
 
 
EC 2.4.1.16     
Accepted name: chitin synthase
Reaction: UDP-N-acetyl-D-glucosamine + [4)-N-acetyl-β-D-glucosaminyl-(1→]n = UDP + [4)-N-acetyl-β-D-glucosaminyl-(1→]n+1
Other name(s): chitin-UDP N-acetylglucosaminyltransferase; chitin-uridine diphosphate acetylglucosaminyltransferase; chitin synthetase; trans-N-acetylglucosaminosylase; UDP-N-acetyl-D-glucosamine:chitin 4-β-N-acetylglucosaminyl-transferase
Systematic name: UDP-N-acetyl-D-glucosamine:chitin 4-β-N-acetylglucosaminyltransferase
Comments: Converts UDP-N-acetyl-D-glucosamine into chitin and UDP.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9030-18-6
References:
1.  Glaser, L. and Brown, D.H. The synthesis of chitin in cell-free extracts of Neurospora crassa. J. Biol. Chem. 228 (1957) 729–742. [PMID: 13475355]
2.  Sburlati, A. and Cabib, E. Chitin synthetase 2, a presumptive participant in septum formation in Saccharomyces cerevisiae. J. Biol. Chem. 261 (1986) 15147–15152. [PMID: 2945823]
[EC 2.4.1.16 created 1961]
 
 
EC 2.4.1.17     
Accepted name: glucuronosyltransferase
Reaction: UDP-glucuronate + acceptor = UDP + acceptor β-D-glucuronoside
Other name(s): 1-naphthol glucuronyltransferase; 1-naphthol-UDP-glucuronosyltransferase; 17β-hydroxysteroid UDP-glucuronosyltransferase; 3α-hydroxysteroid UDP-glucuronosyltransferase; 4-hydroxybiphenyl UDP-glucuronosyltransferase; 4-methylumbelliferone UDP-glucuronosyltransferase; 4-nitrophenol UDP-glucuronyltransferase; 4-nitrophenol UDPGT; 17-OH steroid UDPGT; 3-OH androgenic UDPGT; bilirubin uridine diphosphoglucuronyltransferase; bilirubin UDP-glucuronosyltransferase; bilirubin monoglucuronide glucuronyltransferase; bilirubin UDPGT; bilirubin glucuronyltransferase; ciramadol UDP-glucuronyltransferase; estriol UDP-glucuronosyltransferase; estrone UDP-glucuronosyltransferase; uridine diphosphoglucuronosyltransferase; uridine diphosphoglucuronate-bilirubin glucuronoside glucuronosyltransferase; uridine diphosphoglucuronate-bilirubin glucuronosyltransferase; uridine diphosphoglucuronate-estriol glucuronosyltransferase; uridine diphosphoglucuronate-estradiol glucuronosyltransferase; uridine diphosphoglucuronate-4-hydroxybiphenyl glucuronosyltransferase; uridine diphosphoglucuronate-1,2-diacylglycerol glucuronosyltransferase; uridine diphosphoglucuronate-estriol 16α-glucuronosyltransferase; uridine diphosphoglucuronosyltransferase; GT; morphine glucuronyltransferase; p-hydroxybiphenyl UDP glucuronyltransferase; p-nitrophenol UDP-glucuronosyltransferase; p-nitrophenol UDP-glucuronyltransferase; p-nitrophenylglucuronosyltransferase; p-phenylphenol glucuronyltransferase; phenyl-UDP-glucuronosyltransferase; PNP-UDPGT; UDP glucuronate-estradiol-glucuronosyltransferase; UDP glucuronosyltransferase; UDP glucuronate-estriol glucuronosyltransferase; UDP glucuronic acid transferase; UDP glucuronyltransferase; UDP-glucuronate-4-hydroxybiphenyl glucuronosyltransferase; UDP-glucuronate-bilirubin glucuronyltransferase; UDP-glucuronosyltransferase; UDP-glucuronyltransferase; UDPGA transferase; UDPGA-glucuronyltransferase; UDPGT; uridine diphosphoglucuronyltransferase; uridine diphosphoglucuronate-bilirubin glucuronosyltransferase; uridine diphosphate glucuronyltransferase; uridine 5′-diphosphoglucuronyltransferase; uridine diphosphoglucuronosyltransferase
Systematic name: UDP-glucuronate β-D-glucuronosyltransferase (acceptor-unspecific)
Comments: This entry denotes a family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines and fatty acids. Some of the activities catalysed were previously listed separately as EC 2.4.1.42, EC 2.4.1.59, EC 2.4.1.61, EC 2.4.1.76, EC 2.4.1.77, EC 2.4.1.84, EC 2.4.1.107 and EC 2.4.1.108. A temporary nomenclature for the various forms, whose delineation is in a state of flux, is suggested in Ref. 1.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9030-08-4
References:
1.  Bock, K.W., Burchell, B., Dutton, G.J., Hanninen, O., Mulder, G.J., Owens, I.S., Siest, G. and Jephly, T.R. UDP-glucuronosyltransferase activities. Guidelines for consistent interim terminology and assay conditions. Biochem. Pharmacol. 32 (1983) 953–955. [PMID: 6404284]
2.  Bock, K.W., Josting, D., Lilienblum, W. and Pfeil, H. Purification of rat-liver microsomal UDP-glucuronyltransferase. Separation of two enzyme forms inducible by 3-methylcholanthrene or phenobarbital. Eur. J. Biochem. 98 (1979) 19–26. [PMID: 111930]
3.  Burchell, B. Identification and purification of multiple forms of UDP-glucuronosyltransferase. Rev. Biochem. Toxicol. 3 (1981) 1–32.
4.  Dutton, G.J. Glucuronidation of Drugs and Other Compounds, C.R.C. Press, Boca Raton, Florida, 1980.
5.  Green, M.D., Falany, C.N., Kirkpatrick, R.B. and Tephly, T.R. Strain differences in purified rat hepatic 3α-hydroxysteroid UDP-glucuronosyltransferase. Biochem. J. 230 (1985) 403–409. [PMID: 3931633]
6.  Jansen, P.L.M. The enzyme-catalyzed formation of bilirubin diglucuronide by a solublized preparation from cat liver microsomes. Biochim. Biophys. Acta 338 (1974) 170–182.
[EC 2.4.1.17 created 1961 (EC 2.4.1.42, EC 2.4.1.59 and EC 2.4.1.61 all created 1972; EC 2.4.1.76, EC 2.4.1.77 and EC 2.4.1.84 all created 1976; EC 2.4.1.107 and EC 2.4.1.108 both created 1983, all incorporated 1984)]
 
 
EC 2.4.1.18     
Accepted name: 1,4-α-glucan branching enzyme
Reaction: Transfers a segment of a (1→4)-α-D-glucan chain to a primary hydroxy group in a similar glucan chain
Other name(s): branching enzyme; amylo-(1,4→1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; glucosan transglycosylase; glycogen branching enzyme; plant branching enzyme; α-1,4-glucan:α-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase
Systematic name: (1→4)-α-D-glucan:(1→4)-α-D-glucan 6-α-D-[(1→4)-α-D-glucano]-transferase
Comments: Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9001-97-2
References:
1.  Barker, S.A., Bourne, E. and Peat, S. The enzymic synthesis and degradation of starch. Part IV. The purification and storage of the Q-enzyme of the potato. J. Chem. Soc. (Lond.) (1949) 1705–1711.
2.  Baum, H. and Gilbert, G.A. A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme. Nature 171 (1953) 983–984. [PMID: 13063502]
3.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
4.  Illingworth Brown, B. and Brown, D.H. α-1,4-Glucan:α-1,4-glucan 6-glycosyltransferase from mammalian muscle. Methods Enzymol. 8 (1966) 395–403.
[EC 2.4.1.18 created 1961]
 
 
EC 2.4.1.19     
Accepted name: cyclomaltodextrin glucanotransferase
Reaction: Cyclizes part of a (1→4)-α-D-glucan chain by formation of a (1→4)-α-D-glucosidic bond
Other name(s): Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferase; γ-cyclodextrin glycosyltransferase; cyclodextrin glycosyltransferase; cyclomaltodextrin glucotransferase; cyclomaltodextrin glycosyltransferase; konchizaimu; α-1,4-glucan 4-glycosyltransferase, cyclizing; BMA; CGTase; neutral-cyclodextrin glycosyltransferase; 1,4-α-D-glucan 4-α-D-(1,4-α-D-glucano)-transferase (cyclizing)
Systematic name: (1→4)-α-D-glucan:(1→4)-α-D-glucan 4-α-D-[(1→4)-α-D-glucano]-transferase (cyclizing)
Comments: Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-α-glucanotransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9030-09-5
References:
1.  DePinto, J.A. and Campbell, L.L. Purification and properties of the amylase of Bacillus macerans. Biochemistry 7 (1968) 114–120. [PMID: 5758537]
2.  French, D., Levine, M.L., Norberg, E., Norden, P., Pazur, J.H. and Wild, G.M. Studies on the Schardinger dextrins. VII. Co-substrate specificity in coupling reactions of Macerans amylase. J. Am. Chem. Soc. 76 (1954) 2387–2390.
3.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
4.  Schwimmer, S. Evidence for the purity of Schardinger dextrinogenase. Arch. Biochem. Biophys. 43 (1953) 108–117. [PMID: 13031665]
[EC 2.4.1.19 created 1961]
 
 
EC 2.4.1.20     
Accepted name: cellobiose phosphorylase
Reaction: cellobiose + phosphate = α-D-glucose 1-phosphate + D-glucose
Systematic name: cellobiose:phosphate α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, CAS registry number: 9030-20-0
References:
1.  Alexander, J.K. Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum. J. Biol. Chem. 243 (1968) 2899–2904. [PMID: 5653182]
2.  Ayers, W.A. Phosphorolysis and synthesis of cellobiose by cell extracts from Ruminococcus flavefaciens. J. Biol. Chem. 234 (1959) 2819–2822. [PMID: 13795349]
[EC 2.4.1.20 created 1965]
 
 
EC 2.4.1.21     
Accepted name: starch synthase
Reaction: ADP-glucose + [(1→4)-α-D-glucosyl]n = ADP + [(1→4)-α-D-glucosyl]n+1
Other name(s): ADP-glucose—starch glucosyltransferase; adenosine diphosphate glucose-starch glucosyltransferase; adenosine diphosphoglucose-starch glucosyltransferase; ADP-glucose starch synthase; ADP-glucose synthase; ADP-glucose transglucosylase; ADP-glucose-starch glucosyltransferase; ADPG starch synthetase; ADPG-starch glucosyltransferase; starch synthetase; ADP-glucose:1,4-α-D-glucan 4-α-D-glucosyltransferase
Systematic name: ADP-glucose:(1→4)-α-D-glucan 4-α-D-glucosyltransferase
Comments: The accepted name varies according to the source of the enzyme and the nature of its synthetic product, e.g. starch synthase, bacterial glycogen synthase. Similar to EC 2.4.1.11 [glycogen(starch) synthase] but the preferred or mandatory nucleoside diphosphate sugar substrate is ADP-glucose. The entry covers starch and glycogen synthases utilizing ADP-glucose.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9030-10-8, 37338-93-5
References:
1.  Chambers, J.C. and Elbein, A.D. Biosynthesis of glucans in mung bean seedlings. Formation of β-(1,4)-glucans from GDP-glucose and β-(1,3)-glucans from UDP-glucose. Arch. Biochem. Biophys. 138 (1970) 620–631. [PMID: 4317490]
2.  Frydman, R.B. and Cardini, C.E. Studies on adenosine diphosphate D-glucose: α-1,4-glucan α-4-glucosyltransferase of sweet-corn endosperm. Biochim. Biophys. Acta 96 (1965) 294–303. [PMID: 14298833]
3.  Greenberg, E. and Preiss, J. Biosynthesis of bacterial glycogen. II. Purification and properties of the adenosine diphosphoglucose:glycogen transglucosylase of arthrobacter species NRRL B1973. J. Biol. Chem. 240 (1965) 2341–2348. [PMID: 14304835]
4.  Leloir, L.F., de Fekete, M.A. and Cardini, C.E. Starch and oligosaccharide synthesis from uridine diphosphate glucose. J. Biol. Chem. 236 (1961) 636–641. [PMID: 13760681]
5.  Preiss, J., Govins, S., Eidels, L., Lammel, C., Greenberg, E., Edelmann, P. and Sabraw, A. Regulatory mechanisms in the biosynthesis of α-1,4-glucans in bacteria and plants. In: Whelan, W.J. and Schultz, J. (Eds), Miami Winter Symposia, vol. 1, North Holland, Utrecht, 1970, pp. 122–138.
[EC 2.4.1.21 created 1965]
 
 
EC 2.4.1.22     
Accepted name: lactose synthase
Reaction: UDP-galactose + D-glucose = UDP + lactose
Other name(s): UDP-galactose—glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase
Systematic name: UDP-galactose:D-glucose 4-β-D-galactosyltransferase
Comments: The enzyme is a complex of two proteins, A and B. In the absence of the B protein (α-lactalbumin), the enzyme catalyses the transfer of galactose from UDP-galactose to N-acetylglucosamine (EC 2.4.1.90 N-acetyllactosamine synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9030-11-9
References:
1.  Fitzgerald, D.K., Brodbeck, U., Kiyosawa, I., Mawal, R., Colvin, B. and Ebner, K.E. α-Lactalbumin and the lactose synthetase reaction. J. Biol. Chem. 245 (1970) 2103–2108. [PMID: 5440844]
2.  Hill, R.L. and Brew, K. Lactose synthetase. Adv. Enzymol. Relat. Areas Mol. Biol. 43 (1975) 411–490. [PMID: 812340]
3.  Watkins, W.M. and Hassid, W.Z. The synthesis of lactose by particulate enzyme preparations from guinea pig and bovine mammary glands. J. Biol. Chem. 237 (1962) 1432–1440. [PMID: 14005251]
[EC 2.4.1.22 created 1965]
 
 
EC 2.4.1.23     
Accepted name: sphingosine β-galactosyltransferase
Reaction: UDP-galactose + sphingosine = UDP + psychosine
Other name(s): psychosine—UDP galactosyltransferase; galactosyl-sphingosine transferase; psychosine-uridine diphosphate galactosyltransferase; UDP-galactose:sphingosine O-galactosyl transferase; uridine diphosphogalactose-sphingosine β-galactosyltransferase; UDP-galactose:sphingosine 1-β-galactotransferase
Systematic name: UDP-galactose:sphingosine 1-β-galactosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9032-90-0
References:
1.  Cleland, W.W. and Kennedy, E.P. The enzymatic synthesis of psychosine. J. Biol. Chem. 235 (1960) 45–51. [PMID: 13810623]
[EC 2.4.1.23 created 1965]
 
 
EC 2.4.1.24     
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, IUBMB, KEGG, 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]
[EC 2.4.1.24 created 1965]
 
 
EC 2.4.1.25     
Accepted name: 4-α-glucanotransferase
Reaction: Transfers a segment of a (1→4)-α-D-glucan to a new position in an acceptor, which may be glucose or a (1→4)-α-D-glucan
Other name(s): disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase
Systematic name: (1→4)-α-D-glucan:(1→4)-α-D-glucan 4-α-D-glycosyltransferase
Comments: This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9032-09-1
References:
1.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337.
2.  Lukomskaya, I.S. Synthesis of oligosaccharides with α-1,6-bonds by enzyme preparations from liver and muscle. Dokl. Akad. Nauk S.S.S.R. 129 (1959) 1172–1175. (in Russian)
3.  Pazur, J.H. and Okada, S. The isolation and mode of action of a bacterial glucanosyltransferase. J. Biol. Chem. 243 (1968) 4732–4738. [PMID: 4972097]
4.  Walker, G.J. and Whelan, W.J. Synthesis of amylose by potato D-enzyme. Nature 183 (1959) 46. [PMID: 13622683]
5.  Whelan, W.H. Enzymic explorations of the structures of starch and glycogen. Biochem. J. 122 (1971) 609–622. [PMID: 5001952]
[EC 2.4.1.25 created 1965 (EC 2.4.1.3 created 1961, incorporated 1972)]
 
 
EC 2.4.1.26     
Accepted name: DNA α-glucosyltransferase
Reaction: Transfers an α-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA
Other name(s): uridine diphosphoglucose-deoxyribonucleate α-glucosyltransferase; UDP-glucose-DNA α-glucosyltransferase; uridine diphosphoglucose-deoxyribonucleate α-glucosyltransferase; T2-HMC-α-glucosyl transferase; T4-HMC-α-glucosyl transferase; T6-HMC-α-glucosyl transferase
Systematic name: UDP-glucose:DNA α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9030-13-1
References:
1.  Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193]
[EC 2.4.1.26 created 1965]
 
 
EC 2.4.1.27     
Accepted name: DNA β-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA
Other name(s): T4-HMC-β-glucosyl transferase; T4-β-glucosyl transferase; T4 phage β-glucosyltransferase; UDP glucose-DNA β-glucosyltransferase; uridine diphosphoglucose-deoxyribonucleate β-glucosyltransferase
Systematic name: UDP-glucose:DNA β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9030-14-2
References:
1.  Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193]
[EC 2.4.1.27 created 1965]
 
 
EC 2.4.1.28     
Accepted name: glucosyl-DNA β-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA
Other name(s): T6-glucosyl-HMC-β-glucosyl transferase; T6-β-glucosyl transferase; uridine diphosphoglucose-glucosyldeoxyribonucleate β-glucosyltransferase
Systematic name: UDP-glucose:D-glucosyl-DNA β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9030-15-3
References:
1.  Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193]
[EC 2.4.1.28 created 1965]
 
 
EC 2.4.1.29     
Accepted name: cellulose synthase (GDP-forming)
Reaction: GDP-glucose + [(1→4)-β-D-glucosyl]n = GDP + [(1→4)-β-D-glucosyl]n+1
Other name(s): cellulose synthase (guanosine diphosphate-forming); cellulose synthetase; guanosine diphosphoglucose-1,4-β-glucan glucosyltransferase; guanosine diphosphoglucose-cellulose glucosyltransferase; GDP-glucose:1,4-β-D-glucan 4-β-D-glucosyltransferase
Systematic name: GDP-glucose:(1→4)-β-D-glucan 4-β-D-glucosyltransferase
Comments: Involved in the synthesis of cellulose. A similar enzyme [EC 2.4.1.12, cellulose synthase (UDP-forming)] utilizes UDP-glucose.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9027-18-3
References:
1.  Chambers, J.C. and Elbein, A.D. Biosynthesis of glucans in mung bean seedlings. Formation of β-(1,4)-glucans from GDP-glucose and β-(1,3)-glucans from UDP-glucose. Arch. Biochem. Biophys. 138 (1970) 620–631. [PMID: 4317490]
2.  Flowers, H.M., Batra, K.K., Kemp, J. and Hassid, W.Z. Biosynthesis of cellulose in vitro from guanosine diphosphate D-glucose with enzymic preparations from Phaseolus aureus and Lupinus albus. J. Biol. Chem. 244 (1969) 4969–4674. [PMID: 5824571]
[EC 2.4.1.29 created 1965]
 
 
EC 2.4.1.30     
Accepted name: 1,3-β-oligoglucan phosphorylase
Reaction: [(1→3)-β-D-glucosyl]n + phosphate = [(1→3)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Other name(s): β-1,3-oligoglucan:orthophosphate glucosyltransferase II; β-1,3-oligoglucan phosphorylase; 1,3-β-D-oligoglucan:phosphate α-D-glucosyltransferase
Systematic name: (1→3)-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: Does not act on laminarin. Differs in specificity from EC 2.4.1.31 (laminaribiose phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-28-6
References:
1.  Maréchal, L.R. β-1,3-Oligoglucan:orthophosphate glucosyltransferases from Euglena gracilis. I. Isolation and some properties of a β-1,3-oligoglucan phosphorylase. Biochim. Biophys. Acta 146 (1967) 417–430. [PMID: 6066291]
2.  Maréchal, L.R. β-1,3-Oligoglucan: orthophosphate glucosyltransferases from Euglena gracilis. II. Comparative studies between laminaribiose- and β-1,3-oligoglucan phosphorylase. Biochim. Biophys. Acta 146 (1967) 431–442. [PMID: 6066292]
[EC 2.4.1.30 created 1972]
 
 
EC 2.4.1.31     
Accepted name: laminaribiose phosphorylase
Reaction: 3-β-D-glucosyl-D-glucose + phosphate = D-glucose + α-D-glucose 1-phosphate
Systematic name: 3-β-D-glucosyl-D-glucose:phosphate α-D-glucosyltransferase
Comments: Also acts on 1,3-β-D-oligoglucans. Differs in specificity from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, CAS registry number: 37257-29-7
References:
1.  Goldemberg, S.H., Maréchal, L.R. and De Souza, B.C. β-1,3-Oligoglucan: orthophosphate glucosyltransferase from Euglena gracilis. J. Biol. Chem. 241 (1966) 45–50. [PMID: 5901055]
2.  Manners, D.J. and Taylor, D.C. Studies on carbohydrate metabolizing enzymes. XVI. Specificity of laminaribiose phosphorylase from Astasia ocellata. Arch. Biochem. Biophys. 121 (1967) 443–451. [PMID: 6057111]
[EC 2.4.1.31 created 1972]
 
 
EC 2.4.1.32     
Accepted name: glucomannan 4-β-mannosyltransferase
Reaction: GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1
Other name(s): GDP-man-β-mannan manosyltransferase; glucomannan-synthase; GDPmannose:glucomannan 1,4-β-D-mannosyltransferase; GDP-mannose:glucomannan 1,4-β-D-mannosyltransferase
Systematic name: GDP-mannose:glucomannan 4-β-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-30-0
References:
1.  Elbein, A.D. Biosynthesis of a cell wall glucomannan in mung bean seedlings. J. Biol. Chem. 244 (1969) 1608–1616. [PMID: 4304230]
[EC 2.4.1.32 created 1972]
 
 
EC 2.4.1.33     
Accepted name: alginate synthase
Reaction: GDP-D-mannuronate + (alginate)n = GDP + (alginate)n+1
Other name(s): mannuronosyl transferase
Systematic name: GDP-D-mannuronate:alginate D-mannuronyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-31-1
References:
1.  Lin, T.-Y. and Hassid, W.Z. Pathway of alginic acid synthesis in the marine brown alga, Fucus gardneri Silva. J. Biol. Chem. 241 (1966) 5284–5297. [PMID: 5954796]
[EC 2.4.1.33 created 1972]
 
 
EC 2.4.1.34     
Accepted name: 1,3-β-glucan synthase
Reaction: UDP-glucose + [(1→3)-β-D-glucosyl]n = UDP + [(1→3)-β-D-glucosyl]n+1
Other name(s): 1,3-β-D-glucan—UDP glucosyltransferase; UDP-glucose—1,3-β-D-glucan glucosyltransferase; callose synthetase; 1,3-β-D-glucan-UDP glucosyltransferase; UDP-glucose-1,3-β-D-glucan glucosyltransferase; paramylon synthetase; UDP-glucose-β-glucan glucosyltransferase; GS-II; (1,3)-β-glucan (callose) synthase; β-1,3-glucan synthase; β-1,3-glucan synthetase; 1,3-β-D-glucan synthetase; 1,3-β-D-glucan synthase; 1,3-β-glucan-uridine diphosphoglucosyltransferase; callose synthase; UDP-glucose-1,3-β-glucan glucosyltransferase; UDP-glucose:(1,3)β-glucan synthase; uridine diphosphoglucose-1,3-β-glucan glucosyltransferase; UDP-glucose:1,3-β-D-glucan 3-β-D-glucosyltransferase
Systematic name: UDP-glucose:(1→3)-β-D-glucan 3-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9037-30-3
References:
1.  Maréchal, L.R. and Goldemberg, S.H. Uridine diphosphate glucose-β-1,3-glucan β-3-glucosyltransferase from Euglena gracilis. J. Biol. Chem. 239 (1964) 3163–3167. [PMID: 14245356]
[EC 2.4.1.34 created 1972]
 
 
EC 2.4.1.35     
Accepted name: phenol β-glucosyltransferase
Reaction: UDP-glucose + a phenol = UDP + an aryl β-D-glucoside
Other name(s): UDPglucosyltransferase; phenol-β-D-glucosyltransferase; UDP glucosyltransferase; UDP-glucose glucosyltransferase; uridine diphosphoglucosyltransferase
Systematic name: UDP-glucose:phenol β-D-glucosyltransferase
Comments: Acts on a wide range of phenols.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9046-69-9
References:
1.  Dutton, G.J. Uridine diphosphate glucose and the synthesis of phenolic glucosides by mollusks. Arch. Biochem. Biophys. 116 (1966) 399–405. [PMID: 5961845]
[EC 2.4.1.35 created 1972]
 
 
EC 2.4.1.36     
Accepted name: α,α-trehalose-phosphate synthase (GDP-forming)
Reaction: GDP-glucose + glucose 6-phosphate = GDP + α,α-trehalose 6-phosphate
Other name(s): GDP-glucose—glucose-phosphate glucosyltransferase; guanosine diphosphoglucose-glucose phosphate glucosyltransferase; trehalose phosphate synthase (GDP-forming)
Systematic name: GDP-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase
Comments: See also EC 2.4.1.15 [α,α-trehalose-phosphate synthase (UDP-forming)].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-32-2
References:
1.  Elbein, A.D. Carbohydrate metabolism in Streptomyces hygroscopicus. I. Enzymatic synthesis of trehalose phosphate from guanosine diphosphate D-glucose-14C. J. Biol. Chem. 242 (1967) 403–406. [PMID: 6022837]
[EC 2.4.1.36 created 1972]
 
 
EC 2.4.1.37     
Accepted name: fucosylgalactoside 3-α-galactosyltransferase
Reaction: UDP-galactose + α-L-fucosyl-(1→2)-D-galactosyl-R = UDP + α-D-galactosyl-(1→3)-[α-L-fucosyl(1→2)]-D-galactosyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
Other name(s): UDP-galactose:O-α-L-fucosyl(1→2)D-galactose α-D-galactosyltransferase; UDPgalactose:glycoprotein-α-L-fucosyl-(1,2)-D-galactose 3-α-D-galactosyltransferase; [blood group substance] α-galactosyltransferase; blood-group substance B-dependent galactosyltransferase; glycoprotein-fucosylgalactoside α-galactosyltransferase; histo-blood group B transferase; histo-blood substance B-dependent galactosyltransferase; UDP-galactose:α-L-fucosyl-1,2-D-galactoside 3-α-D-galactosyltransferase
Systematic name: UDP-galactose:α-L-fucosyl-(1→2)-D-galactoside 3-α-D-galactosyltransferase
Comments: Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37257-33-3
References:
1.  Race, C., Ziderman, D. and Watkins, W.M. An α-D-galactosyltransferase associated with the blood-group B character. Biochem. J. 107 (1968) 733–735. [PMID: 16742598]
[EC 2.4.1.37 created 1972, modified 1999, modified 2002]
 
 
EC 2.4.1.38     
Accepted name: β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase
Reaction: UDP-galactose + N-acetyl-β-D-glucosaminylglycopeptide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminylglycopeptide
Other name(s): UDP-galactose—glycoprotein galactosyltransferase; glycoprotein 4-β-galactosyl-transferase; β-N-acetyl-β1-4-galactosyltransferase; thyroid glycoprotein β-galactosyltransferase; glycoprotein β-galactosyltransferase; thyroid galactosyltransferase; uridine diphosphogalactose-glycoprotein galactosyltransferase; β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase; GalT; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide β-1,4-galactosyltransferase
Systematic name: UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase
Comments: Terminal N-acetyl-β-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by β-1,6-links to galactose residues; lower activity towards residues linked to galactose by β-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37237-43-7
References:
1.  Beyer, T.A., Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Glucosyltransferases and their uses in assessing oligosaccharide structure and structure-function relationship. Adv. Enzymol. 52 (1981) 23–175. [PMID: 6784450]
2.  Blanken, W.M., Hooghwinkel, G.J.M. and van den Eijnden, D.H. Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum β-N-acetyl-D-glucosaminide β1→4 galactosyltransferase. Eur. J. Biochem. 127 (1982) 547–552. [PMID: 6816588]
3.  Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335]
4.  Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid galactosyltransferase. J. Biol. Chem. 243 (1968) 6529–6537. [PMID: 5726898]
[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986]
 
 
EC 2.4.1.39     
Accepted name: steroid N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + estradiol-17α 3-D-glucuronoside = UDP + 17α-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside
Other name(s): hydroxy steroid acetylglucosaminyltransferase; steroid acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-steroid acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:estradiol-17α-3-D-glucuronoside 17α-N-acetylglucosaminyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9033-56-1
References:
1.  Collins, D.C., Jirku, H. and Layne, D.S. Steroid N-acetylglucosaminyl transferase. Localization and some properties of the enzyme in rabbit tissues. J. Biol. Chem. 243 (1968) 2928–2933. [PMID: 5660254]
[EC 2.4.1.39 created 1972]
 
 
EC 2.4.1.40     
Accepted name: glycoprotein-fucosylgalactoside α-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-D-galactosamine + glycoprotein-α-L-fucosyl-(1→2)-D-galactose = UDP + glycoprotein-N-acetyl-α-D-galactosaminyl-(1→3)-[α-L-fucosyl-(1→2)]-D-galactose
Other name(s): A-transferase; histo-blood group A glycosyltransferase (Fucα1→2Galα1→3-N-acetylgalactosaminyltransferase); UDP-GalNAc:Fucα1→2Galα1→3-N-acetylgalactosaminyltransferase; α-3-N-acetylgalactosaminyltransferase; blood-group substance α-acetyltransferase; blood-group substance A-dependent acetylgalactosaminyltransferase; fucosylgalactose acetylgalactosaminyltransferase; histo-blood group A acetylgalactosaminyltransferase; histo-blood group A transferase; UDP-N-acetyl-D-galactosamine:α-L-fucosyl-1,2-D-galactose 3-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:glycoprotein-α-L-fucosyl-(1,2)-D-galactose 3-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:glycoprotein-α-L-fucosyl-(1→2)-D-galactose 3-N-acetyl-D-galactosaminyltransferase
Comments: Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9067-69-0
References:
1.  Kobata, A., Grollman, E.F. and Ginsburg, V. An enzymic basis for blood type A in humans. Arch. Biochem. Biophys. 124 (1968) 609–612. [PMID: 5661629]
2.  Takeya, A., Hosomi, O. and Ishiura, M. Complete purification and characterization of α-3-N-acetylgalactosaminyltransferase encoded by the human blood group A gene. J. Biochem. (Tokyo) 107 (1990) 360–368. [PMID: 2341371]
3.  Yates, A.D., Feeney, J., Donald, A.S.R. and Watkins, W.M. Characterization of a blood-group A-active tetrasaccharide synthesized by a blood-group-B gene-specified glycosyltransferase. Carbohydr. Res. 130 (1984) 251–260. [PMID: 6434182]
[EC 2.4.1.40 created 1972, modified 1999]
 
 
EC 2.4.1.41     
Accepted name: polypeptide N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Other name(s): protein-UDP acetylgalactosaminyltransferase; UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase; UDP-N-acetylgalactosamine:κ-casein polypeptide N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase; glycoprotein acetylgalactosaminyltransferase; polypeptide-N-acetylgalactosamine transferase; UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase; UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase; UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase; ppGalNAc-T
Systematic name: UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase
Comments: Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, κ-casein, apofetuin and some other acceptors of high molecular mass.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9075-15-4
References:
1.  Sugiura, M., Kawasaki, T. and Yamashina, I. Purification and characterization of UDP-GalNAc:polypeptide N-acetylgalactosamine transferase from an ascites hepatoma, AH 66. J. Biol. Chem. 257 (1982) 9501–9507. [PMID: 6809738]
2.  Takeuchi, M., Yoshikawa, M., Sasaki, R. and Chiba, H. Purification and characterization of UDP-N-acetylgalactosamine-κ-casein polypeptide N-acetylgalactosaminyltransferase from mammary-gland of lactating cow. Agric. Biol. Chem. 49 (1985) 1059–1069.
[EC 2.4.1.41 created 1972, modified 1989]
 
 
EC 2.4.1.42     
Deleted entry:  UDP-glucuronate—estriol 17β-D-glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.42 created 1972, deleted 1984]
 
 
EC 2.4.1.43     
Accepted name: polygalacturonate 4-α-galacturonosyltransferase
Reaction: UDP-D-galacturonate + [(1→4)-α-D-galacturonosyl]n = UDP + [(1→4)-α-D-galacturonosyl]n+1
Other name(s): UDP galacturonate-polygalacturonate α-galacturonosyltransferase; uridine diphosphogalacturonate-polygalacturonate α-galacturonosyltransferase; UDP-D-galacturonate:1,4-α-poly-D-galacturonate 4-α-D-galacturonosyltransferase
Systematic name: UDP-D-galacturonate:(1→4)-α-poly-D-galacturonate 4-α-D-galacturonosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-53-5
References:
1.  Villemez, C.L., Swanson, A.L. and Hassid, W.Z. Properties of a polygalacturonic acid-synthesizing enzyme system from Phaseolus aureus seedlings. Arch. Biochem. Biophys. 116 (1966) 446–452. [PMID: 5961848]
[EC 2.4.1.43 created 1972]
 
 
EC 2.4.1.44     
Accepted name: lipopolysaccharide 3-α-galactosyltransferase
Reaction: UDP-galactose + lipopolysaccharide = UDP + 3-α-D-galactosyl-[lipopolysaccharide glucose]
Other name(s): UDP-galactose:lipopolysaccharide α,3-galactosyltransferase; UDP-galactose:polysaccharide galactosyltransferase; uridine diphosphate galactose:lipopolysaccharide α-3-galactosyltransferase; uridine diphosphogalactose-lipopolysaccharide α,3-galactosyltransferase
Systematic name: UDP-galactose:lipopolysaccharide 3-α-D-galactosyltransferase
Comments: Transfers D-galactosyl residues to D-glucose in the partially completed core of lipopolysaccharide [cf. EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase), EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9073-98-7
References:
1.  Endo, A. and Rothfield, L. Studies of a phospholipid-requiring bacterial enzyme. I. Purification and properties of uridine diphosphate galactose: lipopolysaccharide α-3-galactosyl transferase. Biochemistry 8 (1969) 3500–3507. [PMID: 4898284]
2.  Wollin, R., Creeger, E.S., Rothfield, L.I., Stocker, B.A.D. and Lindberg, A.A. Salmonella typhimurium mutants defective in UDP-D-galactose:lipopolysaccharide α-1,6-D-galactosyltransferase. Structural, immunochemical, and enzymologic studies of rfaB mutants. J. Biol. Chem. 258 (1983) 3769–3774. [PMID: 6403519]
[EC 2.4.1.44 created 1972, modified 2002]
 
 
EC 2.4.1.45     
Accepted name: 2-hydroxyacylsphingosine 1-β-galactosyltransferase
Reaction: UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(β-D-galactosyl)-2-(2-hydroxyacyl)sphingosine
Other name(s): uridine diphosphogalactose-2-hydroxyacylsphingosine galactosyltransferase; UDPgalactose-2-hydroxyacylsphingosine galactosyltransferase; UDP-galactose:ceramide galactosyltransferase; UDP-galactose:2-2-hydroxyacylsphingosine galactosyltransferase
Systematic name: UDP-galactose:2-(2-hydroxyacyl)sphingosine 1-β-D-galactosyl-transferase
Comments: Highly specific.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-54-6
References:
1.  Basu, S., Schultz, A., Basu, M. and Roseman, S. Enzymatic synthesis of galactocerebroside by a galactosyltransferase from embryonic chicken brain. J. Biol. Chem. 243 (1971) 4272–4279. [PMID: 5090043]
2.  Morell, P. and Radin, N.S. Synthesis of cerebroside by brain from uridine diphosphate galactose and ceramide containing hydroxy fatty acid. Biochemistry 8 (1969) 506–512. [PMID: 5793706]
[EC 2.4.1.45 created 1972]
 
 
EC 2.4.1.46     
Accepted name: monogalactosyldiacylglycerol synthase
Reaction: UDP-galactose + 1,2-diacyl-sn-glycerol = UDP + 3-β-D-galactosyl-1,2-diacyl-sn-glycerol
For diagram of the biosynthesis of 3-[α-D-galactosyl-(1→6)-β-D-galactosyl]-1,2-diacyl-sn-glycerol, click here
Other name(s): uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose:diacylglycerol galactosyltransferase; MGDG synthase; UDP galactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose-diacylglyceride galactosyltransferase; UDP-galactose:1,2-diacylglycerol 3-β-D-galactosyltransferase; 1β-MGDG; 1,2-diacylglycerol 3-β-galactosyltransferase
Systematic name: UDP-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Comments: This enzyme adds only one galactosyl group to the diacylglycerol; EC 2.4.1.241, digalactosyldiacylglycerol synthase, adds a galactosyl group to the product of the above reaction. There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3). MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis [4].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-55-7
References:
1.  Veerkamp, J.H. Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus after cell-wall inhibition. VI. Biosynthesis of the galactosyldiglycerides. Biochim. Biophys. Acta 348 (1974) 23–34. [PMID: 4838219]
2.  Wenger, D.A., Petipas, J.W. and Pieringer, R.A. The metabolism of glyceride glycolipids. II. Biosynthesis of monogalactosyl diglyceride from uridine diphosphate galactose and diglyceride in brain. Biochemistry 7 (1968) 3700–3707. [PMID: 5681471]
3.  Miège, C., Maréchal, E., Shimojima, M., Awai, K., Block, M.A., Ohta, H., Takamiya, K., Douce, R. and Joyard, J. Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG. Eur. J. Biochem. 265 (1999) 990–1001. [PMID: 10518794]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [PMID: 15590685]
[EC 2.4.1.46 created 1972, modified 2003, modified 2005]
 
 
EC 2.4.1.47     
Accepted name: N-acylsphingosine galactosyltransferase
Reaction: UDP-galactose + N-acylsphingosine = UDP + D-galactosylceramide
Other name(s): UDP galactose-N-acylsphingosine galactosyltransferase; uridine diphosphogalactose-acylsphingosine galactosyltransferase
Systematic name: UDP-galactose:N-acylsphingosine D-galactosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-56-8
References:
1.  Fujino, Y. and Nakano, M. Enzymic synthesis of cerebroside from ceramide and uridine diphosphate galactose. Biochem. J. 113 (1969) 573–575. [PMID: 5807218]
[EC 2.4.1.47 created 1972]
 
 
EC 2.4.1.48     
Accepted name: heteroglycan α-mannosyltransferase
Reaction: GDP-mannose + heteroglycan = GDP + 2(or 3)-α-D-mannosyl-heteroglycan
Other name(s): GDP mannose α-mannosyltransferase; guanosine diphosphomannose-heteroglycan α-mannosyltransferase
Systematic name: GDP-mannose:heteroglycan 2-(or 3-)-α-D-mannosyltransferase
Comments: The acceptor is a heteroglycan primer containing mannose, galactose and xylose. 1,2- and 1,3-mannosyl bonds are formed.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-57-9
References:
1.  Ankel, H., Ankel, E., Schutzbach, J. and Garancis, J.C. Mannosyl transfer in Cryptococcus laurentii. J. Biol. Chem. 245 (1970) 3945–3955. [PMID: 5492958]
[EC 2.4.1.48 created 1972]
 
 
EC 2.4.1.49     
Accepted name: cellodextrin phosphorylase
Reaction: [(1→4)-β-D-glucosyl]n + phosphate = [(1→4)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Other name(s): β-1,4-oligoglucan:orthophosphate glucosyltransferase; 1,4-β-D-oligo-D-glucan:phosphate α-D-glucosyltransferase
Systematic name: (1→4)-β-D-glucan:phosphate α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-58-0
References:
1.  Sheth, K. and Alexander, J.K. Purification and properties of β-1,4-oligoglucan:orthophosphate glucosyltransferase from Clostridium thermocellum. J. Biol. Chem. 244 (1969) 457–464. [PMID: 5773308]
[EC 2.4.1.49 created 1972]
 
 
EC 2.4.1.50     
Accepted name: procollagen galactosyltransferase
Reaction: UDP-galactose + procollagen 5-hydroxy-L-lysine = UDP + procollagen 5-(D-galactosyloxy)-L-lysine
Other name(s): hydroxylysine galactosyltransferase; collagen galactosyltransferase; collagen hydroxylysyl galactosyltransferase; UDP galactose-collagen galactosyltransferase; uridine diphosphogalactose-collagen galactosyltransferase; UDPgalactose:5-hydroxylysine-collagen galactosyltransferase
Systematic name: UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase
Comments: Probably involved in the synthesis of carbohydrate units in complement (cf EC 2.4.1.66 procollagen glucosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9028-07-3
References:
1.  Bosmann, H.B. and Eylar, E.H. Glycoprotein biosynthesis: the biosynthesis of the hydroxylysine-galactose linkage in collagen. Biochem. Biophys. Res. Commun. 33 (1968) 340–346. [PMID: 5722225]
2.  Kivirikko, K.I. and Myllyla, R. In: Hall, D.A. and Jackson, D.S. (Eds), International Review of Connective Tissue Research, vol. 8, Academic Press, New York, 1979, p. 23.
[EC 2.4.1.50 created 1972, modified 1983]
 
 
EC 2.4.1.51     
Deleted entry:  UDP-N-acetylglucosamine—glycoprotein N-acetylglucosaminyltransferase. Now listed as EC 2.4.1.101 (α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase), EC 2.4.1.143 (α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase), EC 2.4.1.144 (β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase) and EC 2.4.1.145 (α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase)
[EC 2.4.1.51 created 1972, deleted 1984]
 
 
EC 2.4.1.52     
Accepted name: poly(glycerol-phosphate) α-glucosyltransferase
Reaction: UDP-glucose + poly(glycerol phosphate) = UDP + O-(α-D-glucosyl)poly(glycerol phosphate)
Other name(s): UDP glucose-poly(glycerol-phosphate) α-glucosyltransferase; uridine diphosphoglucose-poly(glycerol-phosphate) α-glucosyltransferase
Systematic name: UDP-glucose:poly(glycerol-phosphate) α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-60-4
References:
1.  Glaser, L. and Burger, M.M. The synthesis of teichoic acids. 3. Glucosylation of polyglycerophosphate. J. Biol. Chem. 239 (1964) 3187–3191. [PMID: 14245359]
[EC 2.4.1.52 created 1972]
 
 
EC 2.4.1.53     
Accepted name: poly(ribitol-phosphate) β-glucosyltransferase
Reaction: UDP-glucose + poly(ribitol phosphate) = UDP + (β-D-glucosyl)poly(ribitol phosphate)
Other name(s): UDP glucose-poly(ribitol-phosphate) β-glucosyltransferase; uridine diphosphoglucose-poly(ribitol-phosphate) β-glucosyltransferase; UDP-D-glucose polyribitol phosphate glucosyl transferase; UDP-D-glucose:polyribitol phosphate glucosyl transferase
Systematic name: UDP-glucose:poly(ribitol-phosphate) β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-61-5
References:
1.  Chin, T., Burger, M.M. and Glaser, L. Synthesis of teichoic acids. VI. The formation of multiple wall polymers in Bacillus subtilis W-23. Arch. Biochem. Biophys. 116 (1966) 358–367. [PMID: 4960203]
[EC 2.4.1.53 created 1972]
 
 
EC 2.4.1.54     
Accepted name: undecaprenyl-phosphate mannosyltransferase
Reaction: GDP-mannose + undecaprenyl phosphate = GDP + D-mannosyl-1-phosphoundecaprenol
Other name(s): guanosine diphosphomannose-undecaprenyl phosphate mannosyltransferase; GDP mannose-undecaprenyl phosphate mannosyltransferase; GDP-D-mannose:lipid phosphate transmannosylase
Systematic name: GDP-mannose:undecaprenyl-phosphate D-mannosyltransferase
Comments: Requires phosphatidylglycerol.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-62-6
References:
1.  Lahav, M., Chiu, T.H. and Lennarz, W.J. Studies on the biosynthesis of mannan in Micrococcus lysodeikticus. II. The enzymatic synthesis of mannosyl-l-phosphoryl-undecaprenol. J. Biol. Chem. 244 (1969) 5890–5898. [PMID: 5350943]
[EC 2.4.1.54 created 1972]
 
 
EC 2.4.1.55     
Transferred entry: teichoic-acid synthase. Now EC 2.7.8.14, CDP-ribitol ribitolphosphotransferase
[EC 2.4.1.55 created 1972, deleted 1982]
 
 
EC 2.4.1.56     
Accepted name: lipopolysaccharide N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + lipopolysaccharide = UDP + N-acetyl-D-glucosaminyllipopolysaccharide
Other name(s): UDP-N-acetylglucosamine-lipopolysaccharide N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lipopolysaccharide acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:lipopolysaccharide N-acetyl-D-glucosaminyltransferase
Comments: Transfers N-acetylglucosaminyl residues to a D-galactose residue in the partially completed lipopolysaccharide core [cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase), EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-64-8
References:
1.  Osborn, M.J. and D'Ari, L. Enzymatic incorporation of N-acetylglucosamine into cell wall lipopolysaccharide in a mutant strain of Salmonella typhimurium. Biochem. Biophys. Res. Commun. 16 (1964) 568–575. [PMID: 5332855]
[EC 2.4.1.56 created 1972]
 
 
EC 2.4.1.57     
Accepted name: phosphatidylinositol α-mannosyltransferase
Reaction: Transfers one or more α-D-mannose residues from GDP-mannose to positions 2,6 and others in 1-phosphatidyl-myo-inositol
Other name(s): GDP mannose-phosphatidyl-myo-inositol α-mannosyltransferase; GDPmannose:1-phosphatidyl-myo-inositol α-D-mannosyltransferase; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase; phosphatidyl-myo-inositol α-mannosyltransferase
Systematic name: GDP-mannose:1-phosphatidyl-1D-myo-inositol α-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-65-9
References:
1.  Brennan, P. and Ballou, G.E. Phosphatidylmyoinositol monomannoside in Propionibacterium shermanii. Biochem. Biophys. Res. Commun. 30 (1968) 69–75. [PMID: 4295288]
[EC 2.4.1.57 created 1972, modified 2003]
 
 
EC 2.4.1.58     
Accepted name: lipopolysaccharide glucosyltransferase I
Reaction: UDP-glucose + lipopolysaccharide = UDP + D-glucosyl-lipopolysaccharide
Other name(s): UDP-glucose:lipopolysaccharide glucosyltransferase I; lipopolysaccharide glucosyltransferase; uridine diphosphate glucose:lipopolysaccharide glucosyltransferase I; uridine diphosphoglucose-lipopolysaccharide glucosyltransferase
Systematic name: UDP-glucose:lipopolysaccharide glucosyltransferase
Comments: Transfers glucosyl residues to the backbone portion of lipopolysaccharide [cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase, EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9074-00-4
References:
1.  Müller, E., Hinckley, A. and Rothfield, L. Studies of phospholipid-requiring bacterial enzymes. 3. Purification and properties of uridine diphosphate glucose:lipopolysaccharide glucosyltransferase I. J. Biol. Chem. 247 (1972) 2614–2622. [PMID: 4553445]
2.  Rothfield, L., Osborn, M.J. and Horecker, B.L. Biosynthesis of bacterial lipopolysaccharide. II. Incorporation of glucose and galactose catalyzed by particulate and soluble enzymes in salmonella. J. Biol. Chem. 239 (1964) 2788–2795. [PMID: 14217875]
[EC 2.4.1.58 created 1972]
 
 
EC 2.4.1.59     
Deleted entry:  UDP-glucuronate—estradiol glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.59 created 1972, deleted 1984]
 
 
EC 2.4.1.60     
Accepted name: abequosyltransferase
Reaction: CDP-abequose + D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid = CDP + D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid
Other name(s): trihexose diphospholipid abequosyltransferase
Systematic name: CDP-abequose:D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid D-abequosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, 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]
[EC 2.4.1.60 created 1972]
 
 
EC 2.4.1.61     
Deleted entry:  UDP-glucuronate—estriol 16α-glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.61 created 1972, deleted 1984]
 
 
EC 2.4.1.62     
Accepted name: ganglioside galactosyltransferase
Reaction: UDP-galactose + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-(1→4)-β-D-glucosyl-N-acylsphingosine = UDP + D-galactosyl-(1→3)-β-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine
Other name(s): UDP-galactose—ceramide galactosyltransferase; uridine diphosphogalactose-ceramide galactosyltransferase; UDP galactose-LAC Tet-ceramide α-galactosyltransferase; UDP-galactose-GM2 galactosyltransferase; uridine diphosphogalactose-GM2 galactosyltransferase; uridine diphosphate D-galactose:glycolipid galactosyltransferase; UDP-galactose:N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosyl-glucosyl-ceramide galactosyltransferase; UDP-galactose-GM2 ganglioside galactosyltransferase; GM1-synthase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine β-1,3-D-galactosyltransferase
Systematic name: UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-(1→4)-β-D-glucosyl-N-acylsphingosine 3-β-D-galactosyltransferase
Comments: The substrate is also known as GM2.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37217-28-0
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain uridine diphosphate D-galactose: glycolipid galactosyltransferase. J. Biol. Chem. 240 (1965) 4115–4117. [PMID: 5842076]
2.  Yip, G.B. and Dain, J.A. The enzymic synthesis of ganglioside. II. UDP-galactose: N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosyl-glucosyl-ceramide galactosyltransferase in rat brain. Biochim. Biophys. Acta 206 (1970) 252–260. [PMID: 4987145]
3.  Yip, M.C.M. and Dain, J.A. Frog brain uridine diphosphate galactose-N-acetylgalactosaminyl-N-acetylneuraminylgalactosylglucosylceramide galactosyltransferase. Biochem. J. 118 (1970) 247–252. [PMID: 5484669]
[EC 2.4.1.62 created 1972]
 
 
EC 2.4.1.63     
Accepted name: linamarin synthase
Reaction: UDP-glucose + 2-hydroxy-2-methylpropanenitrile = UDP + linamarin
Other name(s): uridine diphosphoglucose-ketone glucosyltransferase; uridine diphosphate-glucose-ketone cyanohydrin β-glucosyltransferase; UDP glucose ketone cyanohydrin glucosyltransferase; UDP-glucose:ketone cyanohydrin β-glucosyltransferase; uridine diphosphoglucose-ketone cyanohydrin glucosyltransferase
Systematic name: UDP-glucose:2-hydroxy-2-methylpropanenitrile β-D-glucosyltransferase
Comments: The enzyme glucosylates the cyanohydrins of butanone and pentan-3-one as well as that of acetone.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-68-2
References:
1.  Hahlbrock, K. and Conn, E.E. The biosynthesis of cyanogenic glycosides in higher plants. I. Purification and properties of a uridine diphosphate-glucose-ketone cyanohydrin β-glucosyltransferase from Linum usitatissimum L. J. Biol. Chem. 245 (1970) 917–922. [PMID: 5417265]
[EC 2.4.1.63 created 1972]
 
 
EC 2.4.1.64     
Accepted name: α,α-trehalose phosphorylase
Reaction: α,α-trehalose + phosphate = D-glucose + β-D-glucose 1-phosphate
For diagram of the reactions of trehalose phosphorylase, click here
Other name(s): trehalose phosphorylase
Systematic name: α,α-trehalose:phosphate β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, CAS registry number: 37205-59-7
References:
1.  Belocopitow, E. and Maréchal, L.R. Trehalose phosphorylase from Euglena gracilis. Biochim. Biophys. Acta 198 (1970) 151–154. [PMID: 5413942]
[EC 2.4.1.64 created 1972]
 
 
EC 2.4.1.65     
Accepted name: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-D-glucosaminyl-R = GDP + β-D-galactosyl-(1→3)-[α-L-fucosyl-(1→4)]-N-acetyl-β-D-glucosaminyl-R
For diagram of reaction, click here
Other name(s): (Lea)-dependent (α-3/4)-fucosyltransferase; α(1,3/1,4) fucosyltransferase III; α-(1→4)-L-fucosyltransferase; α-4-L-fucosyltransferase; β-acetylglucosaminylsaccharide fucosyltransferase; FucT-II; Lewis α-(1→3/4)-fucosyltransferase; Lewis blood group α-(1→3/4)-fucosyltransferase; Lewis(Le) blood group gene-dependent α-(1→3/4)-L-fucosyltransferase; blood group Lewis α-4-fucosyltransferase; blood-group substance Lea-dependent fucosyltransferase; guanosine diphosphofucose-β-acetylglucosaminylsaccharide 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-fucosyltransferase; 3-α-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase; GDP-β-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase; GDP-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase
Comments: This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-α-fucosylation of the GlcNAc in β-D-Gal-(1→3)-β-GlcNAc sequences (with some activity also as 3-α-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-α- and 4-α-fucosyltransferase activities.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-69-3
References:
1.  Prieels, J.-P., Monnom, D., Dolmans, M., Beyer, T.A. and Hill, R.L. Co-purification of the Lewis blood group N-acetylglucosaminide α1→4 fucosyltransferase and an N-acetylglucosaminide α1→3 fucosyltransferase from human milk. J. Biol. Chem. 256 (1981) 10456–10463. [PMID: 7287719]
2.  Rasko, D.A., Wang, G., Palcic, M.M. and Taylor, D.E. Cloning and characterization of the α(1,3/4) fucosyltransferase of Helicobacter pylori. J. Biol. Chem. 275 (2000) 4988–4994. [PMID: 10671538]
3.  Wilson, I.B.H. Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase. Glycoconj. J. 18 (2001) 439–447. [PMID: 12084979]
4.  Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893–21900. [PMID: 12676935]
[EC 2.4.1.65 created 1972, modified 2001, modified twice 2002]
 
 
EC 2.4.1.66     
Accepted name: procollagen glucosyltransferase
Reaction: UDP-glucose + (2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] = UDP + (2S,5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine-[procollagen]
Other name(s): galactosylhydroxylysine glucosyltransferase; collagen glucosyltransferase; collagen hydroxylysyl glucosyltransferase; galactosylhydroxylysyl glucosyltransferase; UDP-glucose-collagenglucosyltransferase; uridine diphosphoglucose-collagen glucosyltransferase; UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen D-glucosyltransferase
Systematic name: UDP-glucose:(2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] D-glucosyltransferase
Comments: Probably involved in the synthesis of carbohydrate units in complement (cf. EC 2.4.1.50 procollagen galactosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9028-08-4
References:
1.  Bosmann, H.B. and Eylar, E.H. Attachment of carbohydrate to collagen. Isolation, purification and properties of the glucosyl transferase. Biochem. Biophys. Res. Commun. 30 (1968) 89–94. [PMID: 5637038]
2.  Bosmann, H.B. and Eylar, E.H. Collagen-glucosyl transferase in fibriblasts transformed by oncogenic viruses. Nature 218 (1968) 582–583. [PMID: 4968368]
3.  Butler, W.T. and Cunningham, L.W. Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen. J. Biol. Chem. 241 (1966) 3882–3888. [PMID: 4288358]
4.  Kivirikko, K.I. and Myllyla, R. In: Hall, D.A. and Jackson, D.S. (Eds), International Review of Connective Tissue Research, vol. 8, Academic Press, New York, 1979, p. 23.
[EC 2.4.1.66 created 1972]
 
 
EC 2.4.1.67     
Accepted name: galactinol—raffinose galactosyltransferase
Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + raffinose = myo-inositol + stachyose
For diagram of stachyose biosynthesis, click here
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): galactinol-raffinose galactosyltransferase; stachyose synthetase; α-D-galactosyl-(1→3)-myo-inositol:raffinose galactosyltransferase
Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:raffinose galactosyltransferase
Comments: This enzyme also catalyses galactosyl transfer from stachyose to raffinose (shown by labelling) [4]. For synthesis of the substrate, see EC 2.4.1.123, inositol 3-α-galactosyltransferase. See also EC 2.4.1.82, galactinol—sucrose galactosyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-70-6
References:
1.  Tanner, W. Die Biosynthese der Stachyose. Ber. Dtsch. Bot. Ges. 80 (1967) 111.
2.  Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of stachyose. Eur. J. Biochem. 4 (1968) 233–239. [PMID: 5655499]
3.  Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [PMID: 4774118]
4.  Kandler, O. and Hopf, H. Occurrence, metabolism and function of oligosaccharides. In: Preiss, J. (Ed.), The Biochemistry of Plant, vol. 3, Academic Press, New York, 1980, pp. 221–270.
[EC 2.4.1.67 created 1972, modified 2003]
 
 
EC 2.4.1.68     
Accepted name: glycoprotein 6-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-[α-L-fucosyl-(1→6)]-N-acetyl-β-D-glucosaminyl}asparagine
For diagram of the reactions of mannosyl-glycoprotein fucosyl and xylosyl transferases, click here
Other name(s): GDP-fucose—glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase; GDP-L-fucose-glycoprotein fucosyltransferase; glycoprotein fucosyltransferase; guanosine diphosphofucose-glycoprotein fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of 4-N-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyltransferase; FucT; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyltransferase
Comments: This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-α-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-β-L-fucose to form an α1,6-linkage rather than an α1,3-linkage.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9033-08-3
References:
1.  Longmore, G.D. and Schachter, H. Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-β-D-glucoside (Fuc → Asn-linked GlcNAc) 6-α-L-fucosyltransferase in a Golgi-rich fraction from porcine liver. Carbohydr. Res. 100 (1982) 365–392. [PMID: 7083256]
2.  Voynow, J.A., Scanlin, T.F. and Glick, M.C. A quantitative method for GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase activity with lectin affinity chromatography. Anal. Biochem. 168 (1988) 367–373. [PMID: 3364733]
3.  Uozumi, N., Yanagidani, S., Miyoshi, E., Ihara, Y., Sakuma, T., Gao, C.-X., Teshima, T., Fujii, S., Shiba, T. and Taniguchi, N. Purification and cDNA cloning of porcine brain GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase. J. Biol. Chem. 271 (1996) 27810–27817. [PMID: 8910378]
[EC 2.4.1.68 created 1972, modified 2002]
 
 
EC 2.4.1.69     
Accepted name: galactoside 2-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Glossary: lactotetraosylceramide = β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
III2-α-fucosyllactotetraosylceramide = α-L-fucosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): blood group H α-2-fucosyltransferase; guanosine diphosphofucose-galactoside 2-L-fucosyltransferase; α-(1→2)-L-fucosyltransferase; α-2-fucosyltransferase; α-2-L-fucosyltransferase; blood-group substance H-dependent fucosyltransferase; guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase; guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase; guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase; H-gene-encoded β-galactoside α1→2fucosyltransferase; secretor-type β-galactoside α1→2fucosyltransferase; β-galactoside α1→2fucosyltransferase; GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 2-α-L-fucosyltransferase
Comments: Free lactose can act as acceptor. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. The action on glycolipid was previously listed as EC 2.4.1.89.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 56093-23-3
References:
1.  Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956–2962. [PMID: 804484]
2.  Beyer, T.A. and Hill, R.L. Enzymatic properties of the β-galactoside α 1 leads to 2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5373–5379. [PMID: 7372640]
3.  Beyer, T.A., Sadler, J.E. and Hill, R.L. Purification to homogeneity of H blood group β-galactoside α 1 leads to 2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5364–5372. [PMID: 6246105]
4.  Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351–353.
[EC 2.4.1.69 created 1972 (EC 2.4.1.89 created 1976, incorporated 1984), modified 2002]
 
 
EC 2.4.1.70     
Accepted name: poly(ribitol-phosphate) N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + poly(ribitol phosphate) = UDP + (N-acetyl-D-glucosaminyl)poly(ribitol phosphate)
Other name(s): UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase
Comments: Involved in the synthesis of teichoic acids.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-71-7
References:
1.  Nathenson, S.G., Ishimoto, N. and Strominger, J.L. UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases from Staphylococcus aureus. Methods Enzymol. 8 (1966) 426–429.
[EC 2.4.1.70 created 1972]
 
 
EC 2.4.1.71     
Accepted name: arylamine glucosyltransferase
Reaction: UDP-glucose + an arylamine = UDP + an N-D-glucosylarylamine
Other name(s): UDP glucose-arylamine glucosyltransferase; uridine diphosphoglucose-arylamine glucosyltransferase
Systematic name: UDP-glucose:arylamine N-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37277-72-8
References:
1.  Frear, D.S. Herbicide metabolism in plants. I. Purification and properties of UDP-glucose:arylamine N-glucosyl-transferase from soybean. Phytochemistry 7 (1968) 381–390.
[EC 2.4.1.71 created 1972]
 
 
EC 2.4.1.72     
Transferred entry: 1,4-β-xylan synthase. Now EC 2.4.2.24, 1,4-β-D-xylan synthase
[EC 2.4.1.72 created 1972, deleted 1976]
 
 
EC 2.4.1.73     
Accepted name: lipopolysaccharide glucosyltransferase II
Reaction: UDP-glucose + lipopolysaccharide = UDP + α-D-glucosyl-lipopolysaccharide
Other name(s): uridine diphosphoglucose-galactosylpolysaccharide glucosyltransferase
Systematic name: UDP-glucose:galactosyl-lipopolysaccharide α-D-glucosyltransferase
Comments: Transfers glucosyl residues to the D-galactosyl-D-glucosyl side-chains in the partially completed core of lipopolysaccharides. cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase), EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 51004-27-4
References:
1.  Edstrom, R.D. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. VI. Enzymatic transfer of galactose, glucose, N-acetylglucosamine, and colitose into the polymer. J. Biol. Chem. 242 (1967) 3581–3588. [PMID: 5341482]
[EC 2.4.1.73 created 1972]
 
 
EC 2.4.1.74     
Accepted name: glycosaminoglycan galactosyltransferase
Reaction: UDP-galactose + glycosaminoglycan = UDP + D-galactosylglycosaminoglycan
Other name(s): uridine diphosphogalactose-mucopolysaccharide galactosyltransferase
Systematic name: UDP-galactose:glycosaminoglycan D-galactosyltransferase
Comments: Involved in the biosynthesis of galactose-containing glycosaminoglycan of Dictyostelium discoideum.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 51004-28-5
References:
1.  Sussman, M. and Osborn, M.J. UDP-glucose polysaccharide transferase in the cellular slime mold Dictyostelium discoideum: appearance and dissappearance of activity during cell differentiation. Proc. Natl. Acad. Sci. USA 52 (1964) 81–87.
[EC 2.4.1.74 created 1972, modified 1980]
 
 
EC 2.4.1.75     
Deleted entry: UDP-galacturonosyltransferase. Insufficient evidence to conclude that this is a different enzyme from EC 2.4.1.43, polygalacturonate 4-α-galacturonosyltransferase
[EC 2.4.1.75 created 1976, deleted 2005]
 
 
EC 2.4.1.76     
Deleted entry:  UDP-glucuronate—bilirubin glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.76 created 1976, deleted 1984]
 
 
EC 2.4.1.77     
Deleted entry:  UDP-glucuronate—bilirubin-glucuronoside glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.77 created 1976, deleted 1984]
 
 
EC 2.4.1.78     
Accepted name: phosphopolyprenol glucosyltransferase
Reaction: UDP-glucose + polyprenyl phosphate = UDP + polyprenylphosphate-glucose
Other name(s): uridine diphosphoglucose-polyprenol monophosphate glucosyltransferase; UDP-glucose:polyprenol monophosphate glucosyltransferase
Systematic name: UDP-glucose:phosphopolyprenol D-glucosyltransferase
Comments: Ficaprenyl phosphate is the best substrate; other polyprenols can also act as substrates, but more slowly.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 55576-46-0
References:
1.  Jankowski, W., Mankowski, T. and Chojnacki, T. Formation of polyprenol monophosphate glucose in Shigella flexneri. Biochim. Biophys. Acta 337 (1974) 153–162. [PMID: 4373050]
[EC 2.4.1.78 created 1976]
 
 
EC 2.4.1.79     
Accepted name: globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-D-galactosamine + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of reaction, click here
Glossary: globotriaosylceramide = Pk antigen = α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
globotetraosylceramide = globoside = P antigen = β-N-acetyl-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgalactosamine:globotriaosylceramide β-3-N-acetylgalactosaminyltransferase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase; globoside synthase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide β-N-acetyl-D-galactosaminyltransferase; β3GalNAc-T1; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3III-β-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-β-N-acetyl-D-galactosaminyltransferase
Comments: Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted ’3′ in the systematic name, see GL-5.3.4.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 62213-46-1
References:
1.  Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917]
2.  Ishibashi, T., Kijimoto, S. and Makita, A. Biosynthesis of globoside and Forssman hapten from trihexosylceramide and properties of β-N-acetyl-galactosaminyltransferase of guinea pig kidney. Biochim. Biophys. Acta 337 (1974) 92–106. [PMID: 4433547]
3.  Taniguchi, N. and Makita, A. Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide β-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen. J. Biol. Chem. 259 (1984) 5637–5642. [PMID: 6425294]
4.  Okajima, T., Nakamura, Y., Uchikawa, M., Haslam, D.B., Numata, S.I., Furukawa, K., Urano, T. and Furukawa, K. Expression cloning of human globoside synthase cDNAs. Identification of β3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase. J. Biol. Chem. 275 (2000) 40498–40503. [PMID: 10993897]
[EC 2.4.1.79 created 1976, modified 2006]
 
 
EC 2.4.1.80     
Accepted name: ceramide glucosyltransferase
Reaction: UDP-glucose + an N-acylsphingosine = UDP + a D-glucosyl-N-acylsphingosine
For diagram of reaction, click here
Other name(s): UDP-glucose:ceramide glucosyltransferase; ceramide:UDP-Glc glucosyltransferase; uridine diphosphoglucose-ceramide glucosyltransferase; ceramide:UDP-glucose glucosyltransferase; glucosylceramide synthase
Systematic name: UDP-glucose:N-acylsphingosine D-glucosyltransferase
Comments: Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37237-44-8
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388–1394. [PMID: 4631392]
[EC 2.4.1.80 created 1976]
 
 
EC 2.4.1.81     
Accepted name: flavone 7-O-β-glucosyltransferase
Reaction: UDP-glucose + 5,7,3′,4′-tetrahydroxyflavone = UDP + 7-O-β-D-glucosyl-5,7,3′,4′-tetrahydroxyflavone
For diagram of the biosynthesis of apigenin derivatives, click here and of luteolin derivatives, click here
Other name(s): UDP-glucose-apigenin β-glucosyltransferase; UDP-glucose-luteolin β-D-glucosyltransferase; uridine diphosphoglucose-luteolin glucosyltransferase; uridine diphosphoglucose-apigenin 7-O-glucosyltransferase; UDP-glucosyltransferase
Systematic name: UDP-glucose:5,7,3′,4′-tetrahydroxyflavone 7-O-β-D-glucosyltransferase
Comments: A number of flavones, flavanones and flavonols can function as acceptors. Different from EC 2.4.1.91 (flavonol 3-O-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37332-50-6
References:
1.  Sutter, A., Ortmann, R. and Grisebach, H. Purification and properties of an enzyme from cell suspension cultures of parsley catalyzing the transfer of D-glucose from UDP-D-glucose to flavonoids. Biochim. Biophys. Acta 258 (1972) 71–87. [PMID: 5058406]
[EC 2.4.1.81 created 1976]
 
 
EC 2.4.1.82     
Accepted name: galactinol—sucrose galactosyltransferase
Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + sucrose = myo-inositol + raffinose
For diagram of stachyose biosynthesis, click here
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): 1-α-D-galactosyl-myo-inositol:sucrose 6-α-D-galactosyltransferase; α-D-galactosyl-(1→3)-myo-inositol:sucrose 6-α-D-galactosyltransferase; raffinose synthase; RafS
Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:sucrose 6-α-D-galactosyltransferase
Comments: 4-Nitrophenyl α-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-α-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 62213-45-0
References:
1.  Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [PMID: 4774118]
2.  Lehle, L., Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of raffinose. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 1494–1498. [PMID: 5491608]
[EC 2.4.1.82 created 1976, modified 2003]
 
 
EC 2.4.1.83     
Accepted name: dolichyl-phosphate β-D-mannosyltransferase
Reaction: GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate
Other name(s): GDP-Man:DolP mannosyltransferase; dolichyl mannosyl phosphate synthase; dolichyl-phospho-mannose synthase; GDP-mannose:dolichyl-phosphate mannosyltransferase; guanosine diphosphomannose-dolichol phosphate mannosyltransferase; dolichol phosphate mannose synthase; dolichyl phosphate mannosyltransferase; dolichyl-phosphate mannose synthase; GDP-mannose-dolichol phosphate mannosyltransferase; GDP-mannose-dolichylmonophosphate mannosyltransferase; mannosylphosphodolichol synthase; mannosylphosphoryldolichol synthase
Systematic name: GDP-mannose:dolichyl-phosphate β-D-mannosyltransferase
Comments: Acts only on long-chain polyprenyl phosphates and α-dihydropolyprenyl phosphates that are larger than C35.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 62213-44-9
References:
1.  Babczinski, P., Haselbeck, A. and Tanner, W. Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme. Eur. J. Biochem. 105 (1980) 509–515. [PMID: 6989607]
2.  Bretthauer, R.K., Wu, S. and Irwin, W.E. Enzymatic transfer of mannose from guanosine diphosphate mannose to dolichol phosphate in yeast (Hansenula holstii). A possible step in mannan synthesis. Biochim. Biophys. Acta 304 (1973) 736–747. [PMID: 4726855]
3.  Haselbeck, A. Purification of GDP mannose:dolichyl-phosphate O-β-D-mannosyltransferase from Saccharomyces cerevisiae. Eur. J. Biochem. 181 (1989) 663–668. [PMID: 2659345]
4.  Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives. Eur. J. Biochem. 105 (1980) 517–523. [PMID: 6445267]
5.  Richards, J.B. and Hemming, F.W. The transfer of mannose from guanosine diphosphate mannose to dolichol phosphate and protein by pig liver endoplasmic reticulum. Biochem. J. 130 (1972) 77–93. [PMID: 4655455]
[EC 2.4.1.83 created 1976, modified 1983]
 
 
EC 2.4.1.84     
Deleted entry:  UDP-glucuronate—1,2-diacylglycerol glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.84 created 1976, deleted 1984]
 
 
EC 2.4.1.85     
Accepted name: cyanohydrin β-glucosyltransferase
Reaction: UDP-D-glucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile β-D-glucoside
For diagram of dhurrin biosynthesis, click here
Glossary: dhurrin = (S)-4-hydroxymandelonitrile β-D-glucoside
Other name(s): uridine diphosphoglucose-p-hydroxymandelonitrile glucosyltransferase; UDP-glucose-p-hydroxymandelonitrile glucosyltransferase; uridine diphosphoglucose-cyanohydrin glucosyltransferase; uridine diphosphoglucose:aldehyde cyanohydrin β-glucosyltransferase; UDP-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase; UGT85B1; UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase
Systematic name: UDP-D-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase
Comments: Acts on a wide range of substrates in vitro, including cyanohydrins, terpenoids, phenolics, hexanol derivatives and plant hormones, in a regiospecific manner [3]. This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.41, tyrosine N-monooxygenase and EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase. This reaction prevents the disocciation and release of toxic hydrogen cyanide [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 55354-52-4
References:
1.  Reay, P.F. and Conn, E.E. The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin β-glucosyltransferase from sorghum seedlings. J. Biol. Chem. 249 (1974) 5826–5830. [PMID: 4416442]
2.  Jones, P.R., Møller, B.L. and Hoj, P.B. The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity. J. Biol. Chem. 274 (1999) 35483–35491. [PMID: 10585420]
3.  Hansen, K.S., Kristensen, C., Tattersall, D.B., Jones, P.R., Olsen, C.E., Bak, S. and Møller, B.L. The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor. Phytochemistry 64 (2003) 143–151. [PMID: 12946413]
4.  Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222–1231. [PMID: 12114576]
5.  Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779–1784. [PMID: 15665094]
[EC 2.4.1.85 created 1976, modified 2005]
 
 
EC 2.4.1.86     
Accepted name: glucosaminylgalactosylglucosylceramide β-galactosyltransferase
Reaction: UDP-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Glossary: lactotriosylceramide = N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
lactotetraosylceramide = β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): uridine diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide galactosyltransferase; GalT-4; paragloboside synthase; glucosaminylgalactosylglucosylceramide 4-β-galactosyltransferase; lactotriaosylceramide 4-β-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-glucosylceramide β-D-galactosyltransferase; UDP-Gal:LcOse3Cer(β 1-4)galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-D-galactosyltransferase
Systematic name: UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9073-46-5
References:
1.  Basu, M. and Basu, S. Enzymatic synthesis of a tetraglycosylceramide by a galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 247 (1972) 1489–1495. [PMID: 4335001]
2.  Basu, M., Presper, K.A., Basu, S., Hoffman, L.M. and Brooks, S.E. Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum. Proc. Natl. Acad. Sci. USA 76 (1979) 4270–4274. [PMID: 291963]
[EC 2.4.1.86 created 1976]
 
 
EC 2.4.1.87     
Accepted name: N-acetyllactosaminide 3-α-galactosyltransferase
Reaction: UDP-galactose + β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R = UDP + α-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
Other name(s): α-galactosyltransferase; UDP-Gal:β-D-Gal(1,4)-D-GlcNAc α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α-1,3-D-galactosyltransferase; UDP-Gal:Galβ1→4GlcNAc-R α1→3-galactosyltransferase; UDP-galactose-acetyllactosamine α-D-galactosyltransferase; UDPgalactose:β-D-galactosyl-β-1,4-N-acetyl-D-glucosaminyl-glycopeptide α-1,3-D-galactosyltransferase; glucosaminylglycopeptide α-1,3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine α1→3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine galactosyltransferase; uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide galactosyltransferase; β-D-galactosyl-N-acetylglucosaminylglycopeptide α-1,3-galactosyltransferase; UDP-galactose:N-acetyllactosaminide 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-1,4-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase
Systematic name: UDP-galactose:β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and N-acetyllactosamine (β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine), but not on 2′-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 128449-51-4
References:
1.  Basu, M. and Basu, S. Enzymatic synthesis of a blood group B-related pentaglycosylceramide by an α-galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 248 (1973) 1700–1706. [PMID: 4632915]
2.  Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335]
3.  Blake, D.A. and Goldstein, I.J. An α-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (α-D-galactose-(1→3)-N-acetyllactosamine). J. Biol. Chem. 256 (1981) 5387–5393. [PMID: 6787040]
[EC 2.4.1.87 created 1976, modified 1989, modified 2002 (EC 2.4.1.124 created 1984, incorporated 2002; EC 2.4.1.151 created 1984, incorporated 2002)]
 
 
EC 2.4.1.88     
Accepted name: globoside α-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-D-galactosaminyl-(1→3)-D-galactosyl-(1→4)-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-D-galactosaminyl-(1→3)-N-acetyl-D-galactosaminyl-(1→3)-D-galactosyl-(1→4)-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide
Other name(s): uridine diphosphoacetylgalactosamine-globoside α-acetylgalactosaminyltransferase; Forssman synthase; globoside acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide α-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-(1→3)-D-galactosyl-(1→4)-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide α-N-acetyl-D-galactosaminyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 52037-97-5
References:
1.  Kijimoto, S., Ishibashi, T. and Makita, A. Biosynthesis of Forssman hapten from globoside by α-N-acetylgalactosaminyltransferase of guinea pig tissues. Biochem. Biophys. Res. Commun. 56 (1974) 177–184. [PMID: 4823436]
[EC 2.4.1.88 created 1976]
 
 
EC 2.4.1.89     
Deleted entry:  Galactosylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase - now included with EC 2.4.1.69 galactoside 2-α-L-fucosyltransferase
[EC 2.4.1.89 created 1976, deleted 1984]
 
 
EC 2.4.1.90     
Accepted name: N-acetyllactosamine synthase
Reaction: UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Other name(s): UDP-galactose—N-acetylglucosamine β-D-galactosyltransferase; uridine diphosphogalactose-acetylglucosamine galactosyltransferase; β-1,4-galactosyltransferase; acetyllactosamine synthetase; lactosamine synthase; lactosamine synthetase; lactose synthetase A protein; N-acetyllactosamine synthetase; UDP-galactose N-acetylglucosamine β-4-galactosyltransferase; UDP-galactose-acetylglucosamine galactosyltransferase; UDP-galactose-N-acetylglucosamine β-1,4-galactosyltransferase; UDP-galactose-N-acetylglucosamine galactosyltransferase; β1-4-galactosyltransferase; UDP-Gal:N-acetylglucosamine β1-4-galactosyltransferase; β1-4GalT; NAL synthetase; UDP-β-1,4-galactosyltransferase; Gal-T; UDP-galactose:N-acetylglucosaminide β1-4-galactosyltransferase; UDPgalactose:N-acetylglucosaminyl(β1-4)galactosyltransferase; β-N-acetylglucosaminide β1-4-galactosyltransferase
Systematic name: UDP-galactose:N-acetyl-D-glucosamine 4-β-D-galactosyltransferase
Comments: The reaction is catalysed by a component of EC 2.4.1.22 (lactose synthase), which is identical with EC 2.4.1.38 (β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase), and by an enzyme from the Golgi apparatus of animal tissues. Formerly listed also as EC 2.4.1.98.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9054-94-8
References:
1.  Deshmukh, D.S., Bear, W.D. and Soifer, D. Isolation and characterization of an enriched Golgi fraction from rat brain. Biochim. Biophys. Acta 542 (1978) 284–295. [PMID: 99178]
2.  Helting, T. and Erbing, B. Galactosyl transfer in mouse mastocytoma: purification and properties of N-acetyllactosamine synthetase. Biochim. Biophys. Acta 293 (1973) 94–104. [PMID: 4631039]
3.  Hill, R.L. and Brew, K. Lactose synthetase. Adv. Enzymol. Relat. Areas Mol. Biol. 43 (1975) 411–490. [PMID: 812340]
4.  Humphreys-Beher, M.G. Isolation and characterization of UDP-galactose:N-acetylglucosamine 4 β-galactosyltransferase activity induced in rat parotid glands treated with isoproterenol. J. Biol. Chem. 259 (1984) 5797–5802. [PMID: 6201486]
5.  Schachter, H., Jabbal, I., Hudgin, R.L., Pinteric, L., McGuire, E.J. and Roseman, S. Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction. J. Biol. Chem. 245 (1970) 1090–1100. [PMID: 4392041]
[EC 2.4.1.90 created 1976 (EC 2.4.1.98 created 1980, incorporated 1984)]
 
 
EC 2.4.1.91     
Accepted name: flavonol 3-O-glucosyltransferase
Reaction: UDP-glucose + a flavonol = UDP + a flavonol 3-O-β-D-glucoside
For diagram of kaempferol biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-glycoside derivatives, click here
Other name(s): GTI; uridine diphosphoglucose-flavonol 3-O-glucosyltransferase; UDP-glucose:flavonol 3-O-glucosyltransferase; UDPG:flavonoid-3-O-glucosyltransferase
Systematic name: UDP-glucose:flavonol 3-O-D-glucosyltransferase
Comments: Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81 (flavone 7-O-β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 50812-18-5
References:
1.  Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587–599.
2.  Sutter, A. and Grisebach, H. UDP-glucose: flavonol 3-O-glucosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 309 (1973) 289–295. [PMID: 4731963]
[EC 2.4.1.91 created 1976]
 
 
EC 2.4.1.92     
Accepted name: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-D-galactosamine + 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide = UDP + 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminosyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
Glossary: ganglioside GM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminosyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
ganglioside GM3 = 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
ganglioside GD3 = 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→8)-O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
ganglioside GD2 = 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→8)-O-(N-acetyl-α-neuraminosyl)-(2→3)-O-[2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
ganglioside SM3 = 1-O-[4-O-(3-O-sulfo-β-D-galactopyranosyl)-β-D-glucopyranosyl]-ceramide
ganglioside SM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-3-O-sulfo-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
Other name(s): uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase; ganglioside GM2 synthase; ganglioside GM3 acetylgalactosaminyltransferase; GM2 synthase; UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 1,4-β-N-acetyl-D-galactosaminyltransferase acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase; GM2/GD2-synthase; β-1,4N-aetylgalactosaminyltransferase; asialo-GM2 synthase; GalNAc-T; UDP-N-acetyl-D-galactosamine:(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 4-β-N-acetyl-D-galactosaminyltransferase
Comments: This enzyme catalyses the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. Asialo-GM3 [3] and lactosylceramide [2] are also substrates, but glycoproteins and oligosaccharides are not substrates.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 67338-98-1
References:
1.  Dicesare, J.L. and Dain, J.A. The enzymic synthesis of ganglioside. IV. UDP-N-acetylgalactosamine: (N-acetylneuraminyl)-galactosylglucosyl ceramide N-acetylgalactosaminyltransferase in rat brain. Biochim. Biophys. Acta 231 (1971) 385–393. [PMID: 5554906]
2.  Pohlentz, G., Klein, D., Schwarzmann, G., Schmitz, D. and Sandhoff, K. Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases are single enzymes in Golgi vesicles from rat liver. Proc. Natl. Acad. Sci. USA 85 (1988) 7044–7048. [PMID: 3140234]
3.  Kazuya, I.-P., Hidari, J.K., Ichikawa, S., Furukawa, K., Yamasaki, M. and Hirabayashi, Y. β1-4N-Acetylgalactosaminyltransferase can synthesize both asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and in vivo: isolation and characterization of a β1-4N-acetylgalactosaminyltransferase cDNA clone from rat ascites hepatoma cell line AH7974F. Biochem. J. 303 (1994) 957–965. [PMID: 7980468]
4.  Hashimoto, Y., Sekine, M., Iwasaki, K. and Suzuki, A. Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver. J. Biol. Chem. 268 (1993) 25857–25864. [PMID: 8245020]
5.  Nagai, K. and Ishizuka, I. Biosynthesis of monosulfogangliotriaosylceramide and GM2 by N-acetylgalactosaminyltransferase from rat brain. J. Biochem. (Tokyo) 101 (1987) 1115–1127. [PMID: 3115968]
6.  Furukawa, K., Takamiya, K. and Furukawa, K. β1,4-N-Acetylgalactosaminyltransferase—GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides. Biochim. Biophys. Acta 1573 (2002) 356–362. [PMID: 12417418]
7.  Yamashita, T., Wu, Y.P., Sandhoff, R., Werth, N., Mizukami, H., Ellis, J.M., Dupree, J.L., Geyer, R., Sandhoff, K. and Proia, R.L. Interruption of ganglioside synthesis produces central nervous system degeneration and altered axon-glial interactions. Proc. Natl. Acad. Sci. USA 102 (2005) 2725–2730. [PMID: 15710896]
[EC 2.4.1.92 created 1976, modified 2006]
 
 
EC 2.4.1.93     
Transferred entry: inulin fructotransferase (depolymerizing, difructofuranose-1,2′:2,3′-dianhydride-forming). Now EC 4.2.2.18, inulin fructotransferase (DFA-III-forming). The enzyme was wrongly classified as a transferase rather than a lyase
[EC 2.4.1.93 created 1976, deleted 2004]
 
 
EC 2.4.1.94     
Accepted name: protein N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + protein = UDP + N4-(N-acetyl-D-glucosaminyl)-protein
Other name(s): uridine diphosphoacetylglucosamine-protein acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; O-GlcNAc transferase
Systematic name: UDP-N-acetyl-D-glucosamine:protein β-N-acetyl-D-glucosaminyl-transferase
Comments: The acceptor is the asparagine residue in a sequence of the form Asn-Xaa-Thr or Asn-Xaa-Ser.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 72319-34-7
References:
1.  Khalkhali, Z. and Marshall, R.D. Glycosylation of ribonuclease A catalysed by rabbit liver extracts. Biochem. J. 146 (1975) 299–307. [PMID: 1156375]
2.  Khalkhali, Z. and Marshall, R.D. UDP-N-acetyl-D-glucosamine-asparagine sequon N-acetyl-β-D-glucosaminyl-transferase-activity in human serum. Carbohydr. Res. 49 (1976) 455–473. [PMID: 986874]
3.  Khalkhali, Z., Marshall, R.D., Reuvers, F., Habets-Willems, C. and Boer, P. Glycosylation in vitro of an asparagine sequon catalysed by preparations of yeast cell membranes. Biochem. J. 160 (1976) 37–41. [PMID: 795426]
[EC 2.4.1.94 created 1978]
 
 
EC 2.4.1.95     
Accepted name: bilirubin-glucuronoside glucuronosyltransferase
Reaction: 2 bilirubin-glucuronoside = bilirubin + bilirubin-bisglucuronoside
Other name(s): bilirubin monoglucuronide transglucuronidase; bilirubin glucuronoside glucuronosyltransferase
Systematic name: bilirubin-glucuronoside:bilirubin-glucuronoside D-glucuronosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 71822-22-5
References:
1.  Jansen, P.L.M., Chowdhury, J.R., Fischberg, E.B. and Arias, I.M. Enzymatic conversion of bilirubin monoglucuronide to diglucuronide by rat liver plasma membranes. J. Biol. Chem. 252 (1977) 2710–2716. [PMID: 15996]
[EC 2.4.1.95 created 1978]
 
 
EC 2.4.1.96     
Accepted name: sn-glycerol-3-phosphate 1-galactosyltransferase
Reaction: UDP-galactose + sn-glycerol 3-phosphate = UDP + 1-O-α-D-galactosyl-sn-glycerol 3-phosphate
Other name(s): isofloridoside-phosphate synthase; UDP-Gal:sn-glycero-3-phosphoric acid 1-α-galactosyl-transferase; UDPgalactose:sn-glycerol-3-phosphate α-D-galactosyltransferase; uridine diphosphogalactose-glycerol phosphate galactosyltransferase; glycerol 3-phosphate 1α-galactosyltransferase
Systematic name: UDP-galactose:sn-glycerol-3-phosphate 1-α-D-galactosyltransferase
Comments: The product is hydrolysed by a phosphatase to isofloridoside, which is involved in osmoregulation (cf. EC 2.4.1.137 sn-glycerol-3-phosphate 2-α-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9076-70-4
References:
1.  Kauss, H. and Quader, H. In vitro activation of a galactosyl transferase involved in the osmotic regulation of Ochromonas. Plant Physiol. 58 (1976) 295–298. [PMID: 16659666]
2.  Kauss, H. and Schubert, B. `First demonstration of UDP-gal:sn-glycero-3-phosphoric acid 1α-galactosyl-transferase and its possible role in osmoregulation. FEBS Lett. 19 (1971) 131–135. [PMID: 11946194]
[EC 2.4.1.96 created 1978]
 
 
EC 2.4.1.97     
Accepted name: 1,3-β-D-glucan phosphorylase
Reaction: [(1→3)-β-D-glucosyl]n + phosphate = [(1→3)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Other name(s): laminarin phosphoryltransferase; 1,3-β-D-glucan:orthophosphate glucosyltransferase;1,3-β-D-glucan:phosphate α-D-glucosyltransferase
Systematic name: (1→3)-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: Acts on a range of β-1,3-oligoglucans, and on glucans of laminarin type. Different from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.31 (laminaribiose phosphorylase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37340-31-1
References:
1.  Albrecht, G.J. and Kauss, H. Purification, crystallization and properties of a β-(1→3)-glucan phosphorylase from Ochromonas malhamensis. Phytochemistry 10 (1971) 1293–1298.
[EC 2.4.1.97 created 1978]
 
 
EC 2.4.1.98     
Deleted entry:  UDP-galactose—N-acetylglucosamine β-D-galactosyl-transferase. Now included with EC 2.4.1.90, N-acetyllactosamine synthase
[EC 2.4.1.98 created 1980, deleted 1984]
 
 
EC 2.4.1.99     
Accepted name: sucrose:sucrose fructosyltransferase
Reaction: 2 sucrose = D-glucose + β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside
Other name(s): SST; sucrose:sucrose 1-fructosyltransferase; sucrose-sucrose 1-fructosyltransferase; sucrose 1F-fructosyltransferase; sucrose:sucrose 1F-β-D-fructosyltransferase
Systematic name: sucrose:sucrose 1′-β-D-fructosyltransferase
Comments: For definition of the prime in the systematic name, see 2-Carb-36.2.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 73379-56-3
References:
1.  Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017–1020.
2.  Lüscher, M., Hochstrasser, U., Vogel, G., Aeschbacher, R., Galati, V., Nelson, C.J., Boller, T. and Wiemken, A. Cloning and functional analysis of sucrose:sucrose 1-fructosyltransferase from tall fescue. Plant Physiol. 124 (2000) 1217–1228. [PMID: 11080298]
[EC 2.4.1.99 created 1981, modified 2004]
 
 
EC 2.4.1.100     
Accepted name: 2,1-fructan:2,1-fructan 1-fructosyltransferase
Reaction: [β-D-fructosyl-(2→1)-]m + [β-D-fructosyl-(2→1)-]n = [β-D-fructosyl-(2→1)-]m-1 + [β-D-fructosyl-(2→1)-]n+1
Other name(s): 1,2-β-D-fructan 1F-fructosyltransferase; fructan:fructan fructosyl transferase; FFT; 1,2-β-fructan 1F-fructosyltransferase; 1,2-β-D-fructan:1,2-β-D-fructan 1F-β-D-fructosyltransferase; fructan:fructan 1-fructosyl transferase; 2,1-β-D-fructan:2,1-β-D-fructan 1-β-D-fructosyltransferase
Systematic name: (2→1)-β-D-fructan:(2→1)-β-D-fructan 1-β-D-fructosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 73379-55-2
References:
1.  Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017–1020.
2.  Vergauwen, R., Van Laere, A. and Van den Ende, W. Properties of fructan:fructan 1-fructosyltransferases from chicory and globe thistle, two asteracean plants storing greatly different types of inulin. Plant Physiol. 133 (2003) 391–401. [PMID: 12970504]
[EC 2.4.1.100 created 1981, modified 2004]
 
 
EC 2.4.1.101     
Accepted name: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + 3-(α-D-mannosyl)-β-D-mannosyl-R = UDP + 3-(2-[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R
For diagram of the reactions of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): 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
Systematic name: UDP-N-acetyl-D-glucosamine:3-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts before N-acetylglucosaminyltransferases II, III, IV, V and VI (click here for diagram).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, 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.  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. [PMID: 6170335]
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.  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]
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. [PMID: 11032794]
[EC 2.4.1.101 created 1983, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984)]
 
 
EC 2.4.1.102     
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R = UDP + β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; β6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-mucin β-(1→6)-acetylglucosaminyltransferase; core 2 acetylglucosaminyltransferase; core 6-β-GlcNAc-transferase A; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R) 6-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase), EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [PMID: 6226356]
2.  Williams, D., Longmore, G., Matta, K.L. and Schachter, H. Mucin synthesis. II. Substrate specificity and product identification studies on canine submaxillary gland UDP-GlcNAc:Gal β1-3GalNAc(GlcNAc→GalNAc) β6-N-acetylglucosaminyltransferase. J. Biol. Chem. 255 (1980) 11253–11261. [PMID: 6449508]
3.  Williams, D. and Schachter, H. Mucin synthesis. I. Detection in canine submaxillary glands of an N-acetylglucosaminyltransferase which acts on mucin substrates. J. Biol. Chem. 255 (1980) 11247–11252. [PMID: 6449507]
[EC 2.4.1.102 created 1983]
 
 
EC 2.4.1.103     
Accepted name: alizarin 2-β-glucosyltransferase
Reaction: UDP-glucose + 1,2-dihydroxy-9,10-anthraquinone = UDP + 1-hydroxy-2-(β-D-glucosyloxy)-9,10-anthraquinone
Glossary: alizarin = 1,2-dihydroxy-9,10-anthraquinone
Other name(s): uridine diphosphoglucose-alizarin glucosyltransferase
Systematic name: UDP-glucose:1,2-dihydroxy-9,10-anthraquinone 2-O-β-D-glucosyltransferase
Comments: Acts on other hydroxy- and dihydroxy-derivatives of 9,10-anthraquinone.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 74506-41-5
References:
1.  Mateju, J., Cudlin, J., Steinerova, N., Blumauerova, M. and Vanek, Z. Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens. Folia Microbiol. 24 (1979) 205–210. [PMID: 38193]
[EC 2.4.1.103 created 1983]
 
 
EC 2.4.1.104     
Accepted name: o-dihydroxycoumarin 7-O-glucosyltransferase
Reaction: UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin
Other name(s): uridine diphosphoglucose-o-dihydroxycoumarin 7-O-glucosyltransferase; UDP-glucose:o-dihydroxycoumarin glucosyltransferase
Systematic name: UDP-glucose:7,8-dihydroxycoumarin 7-O-β-D-glucosyltransferase
Comments: Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 74114-37-7
References:
1.  Ibrahim, R.K. and Boulay, B. Purification and some properties of UDP-glucose:o-hydroxycoumarin 7-O-glucosyltransferase from tobacco cell cultures. Plant Sci. Lett. 18 (1980) 177–184.
[EC 2.4.1.104 created 1983]
 
 
EC 2.4.1.105     
Accepted name: vitexin β-glucosyltransferase
Reaction: UDP-glucose + vitexin = UDP + vitexin 2′′-O-β-D-glucoside
For diagram of the biosynthesis of vitexin and isovitexin derivatives, click here
Other name(s): uridine diphosphoglucose-vitexin 2′′-glucosyltransferase
Systematic name: UDP-glucose:vitexin 2′′-O-β-D-glucosyltransferase
Comments: Vitexin is a flavonoid from Cannabis sativa (hemp) and some populations of Silene alba.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 76828-68-7
References:
1.  Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2′′-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935–1937.
[EC 2.4.1.105 created 1983]
 
 
EC 2.4.1.106     
Accepted name: isovitexin β-glucosyltransferase
Reaction: UDP-glucose + isovitexin = UDP + isovitexin 2′′-O-β-D-glucoside
For diagram of the biosynthesis of vitexin and isovitexin derivatives, click here
Other name(s): uridine diphosphoglucose-isovitexin 2′′-glucosyltransferase
Systematic name: UDP-glucose:isovitexin 2′′-O-β-D-glucosyltransferase
Comments: Isovitexin is a flavonoid from petals of Silene alba.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 72102-99-9
References:
1.  Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2′′-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935–1937.
[EC 2.4.1.106 created 1983]
 
 
EC 2.4.1.107     
Deleted entry:  UDP-glucuronate—testosterone glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.107 created 1983, deleted 1984]
 
 
EC 2.4.1.108     
Deleted entry:  UDP-glucuronate—phenol glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.108 created 1983, deleted 1984]
 
 
EC 2.4.1.109     
Accepted name: dolichyl-phosphate-mannose-protein mannosyltransferase
Reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein
Other name(s): dolichol phosphomannose-protein mannosyltransferase; protein O-D-mannosyltransferase
Systematic name: dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase
Comments: The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain α-dihydropolyprenyl derivatives, larger than C35.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 74315-99-4
References:
1.  Babczinski, P., Haselbeck, A. and Tanner, W. Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme. Eur. J. Biochem. 105 (1980) 509–515. [PMID: 6989607]
2.  Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives. Eur. J. Biochem. 105 (1980) 517–523. [PMID: 6445267]
[EC 2.4.1.109 created 1983]
 
 
EC 2.4.1.110     
Accepted name: tRNA-queuosine β-mannosyltransferase
Reaction: GDP-mannose + tRNAAsp-queuosine = GDP + tRNAAsp-O-5′′-β-D-mannosylqueuosine
Systematic name: GDP-mannose:tRNAAsp-queuosine O-5′′-β-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9055-06-5
References:
1.  Okada, N. and Nishimura, S. Enzymatic synthesis of Q nucleoside containing mannose in the anticodon of tRNA: isolation of a novel mannosyltransferase from a cell-free extract of rat liver. Nucleic Acids Res. 4 (1977) 2931–2938. [PMID: 20603]
[EC 2.4.1.110 created 1984]
 
 
EC 2.4.1.111     
Accepted name: coniferyl-alcohol glucosyltransferase
Reaction: UDP-glucose + coniferyl alcohol = UDP + coniferin
Other name(s): uridine diphosphoglucose-coniferyl alcohol glucosyltransferase; UDP-glucose coniferyl alcohol glucosyltransferase
Systematic name: UDP-glucose:coniferyl-alcohol 4′-β-D-glucosyltransferase
Comments: Sinapyl alcohol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 61116-23-2
References:
1.  Ibrahim, R.K. and Grisebach, H. Purification and properties of UDP-glucose: coniferyl alcohol glucosyltransferase from suspension cultures of Paul's scarlet rose. Arch. Biochem. Biophys. 176 (1976) 700–708. [PMID: 10853]
[EC 2.4.1.111 created 1984]
 
 
EC 2.4.1.112     
Deleted entry: α-1,4-glucan-protein synthase (UDP-forming). The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase
[EC 2.4.1.112 created 1984, deleted 2007]
 
 
EC 2.4.1.113     
Accepted name: α-1,4-glucan-protein synthase (ADP-forming)
Reaction: ADP-glucose + protein = ADP + α-D-glucosyl-protein
Other name(s): ADP-glucose:protein glucosyltransferase; adenosine diphosphoglucose-protein glucosyltransferase
Systematic name: ADP-glucose:protein 4-α-D-glucosyltransferase
Comments: The enzyme builds up α-1,4-glucan chains covalently bound to protein, thus acting as an initiator of glycogen synthesis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 67053-99-0
References:
1.  Barengo, R. and Krisman, C.R. Initiation of glycogen biosynthesis in Escherichia coli. Studies of the properties of the enzymes involved. Biochim. Biophys. Acta 540 (1978) 190–196. [PMID: 418819]
[EC 2.4.1.113 created 1984]
 
 
EC 2.4.1.114     
Accepted name: 2-coumarate O-β-glucosyltransferase
Reaction: UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-β-D-glucosyl-2-hydroxycinnamate
Other name(s): uridine diphosphoglucose-o-coumarate glucosyltransferase; UDPG:o-coumaric acid O-glucosyltransferase
Systematic name: UDP-glucose:trans-2-hydroxycinnamate O-β-D-glucosyltransferase
Comments: Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 73665-97-1
References:
1.  Kleinhofs, A., Haskins, F.A. and Gorz, H.J. trans-o-Hydroxylcinnamic acid glucosylation in cell-free extracts of Melilotus alba. Phytochemistry 6 (1967) 1313–1318.
2.  Poulton, J.E., McRee, B.E. and Conn, E.E. Intracellular localization of two enzymes involved in coumarin biosynthesis in Melilotus alba. Plant Physiol. 65 (1980) 171–175. [PMID: 16661155]
[EC 2.4.1.114 created 1984]
 
 
EC 2.4.1.115     
Accepted name: anthocyanidin 3-O-glucosyltransferase
Reaction: UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-β-D-glucoside
For diagram of anthocyanin biosynthesis, click here
Other name(s): uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase; UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-glucosyltransferase; UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase; 3-GT
Systematic name: UDP-D-glucose:anthocyanidin 3-O-β-D-glucosyltransferase
Comments: The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.11.19, leucocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 65607-32-1
References:
1.  Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1045–1058. [PMID: 751640]
2.  Ford, C.M., Boss, P.K. and Høj, P.B. Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273 (1998) 9224–9233. [PMID: 9535914]
3.  Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276 (2001) 25797–25803. [PMID: 11316805]
[EC 2.4.1.115 created 1984 (EC 2.4.1.233 created 2004, incorporated 2005), modified 2005]
 
 
EC 2.4.1.116     
Accepted name: cyanidin 3-O-rutinoside 5-O-glucosyltransferase
Reaction: UDP-glucose + cyanidin-3-O-β-L-rhamnosyl-(1→6)-β-D-glucoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside
For diagram of anthocyanidin glycoside biosynthesis, click here
Glossary: cyanidin 3-O-rutinoside = cyanidin-3-O-β-L-rhamnosyl-(1→6)-β-D-glucoside
Other name(s): uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase;
Systematic name: UDP-glucose:cyanidin-3-O-β-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase
Comments: Also acts on pelargonidin-3-rutinoside. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin-3-glucoside.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 70248-66-7
References:
1.  Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059–1071. [PMID: 751641]
[EC 2.4.1.116 created 1984 (EC 2.4.1.235 created 2004, incorporated 2006), modified 2006]
 
 
EC 2.4.1.117     
Accepted name: dolichyl-phosphate β-glucosyltransferase
Reaction: UDP-glucose + dolichyl phosphate = UDP + dolichyl β-D-glucosyl phosphate
Other name(s): polyprenyl phosphate:UDP-D-glucose glucosyltransferase; UDP-glucose dolichyl-phosphate glucosyltransferase; uridine diphosphoglucose-dolichol glucosyltransferase; UDP-glucose:dolichol phosphate glucosyltransferase; UDP-glucose:dolicholphosphoryl glucosyltransferase; UDP-glucose:dolichyl monophosphate glucosyltransferase; UDP-glucose:dolichyl phosphate glucosyltransferase
Systematic name: UDP-glucose:dolichyl-phosphate β-D-glucosyltransferase
Comments: Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 71061-42-2
References:
1.  Behrens, N.H. and Leloir, L.F. Dolichol monophosphate glucose: an intermediate in glucose transfer in liver. Proc. Natl Acad. Sci. USA 66 (1970) 153–159. [PMID: 5273893]
2.  Herscovics, A., Bugge, B. and Jeanloz, R.W. Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. J. Biol. Chem. 252 (1977) 2271–2277. [PMID: 849929]
3.  Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase. J. Biol. Chem. 254 (1979) 4814–4819. [PMID: 438216]
[EC 2.4.1.117 created 1984]
 
 
EC 2.4.1.118     
Accepted name: cytokinin 7-β-glucosyltransferase
Reaction: UDP-glucose + an N6-alkylaminopurine = UDP + an N6-alkylaminopurine-7-β-D-glucoside
Glossary: zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
Other name(s): uridine diphosphoglucose-zeatin 7-glucosyltransferase; cytokinin 7-glucosyltransferase; UDP-glucose:zeatin 7-glucosyltransferase
Systematic name: UDP-glucose:N6-alkylaminopurine 7-glucosyltransferase
Comments: Acts on a range of N6-substituted adenines, including zeatin and N6-benzylaminopurine, but not N6-benzyladenine. With some acceptors, 9-β-D-glucosides are also formed.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 72103-03-8
References:
1.  Entsch, B. and Letham, D.S. Enzymic glucosylation of the cytokinin, 6-benzylaminopurine. Plant Sci. Lett. 14 (1979) 205–212.
2.  Entsch, B., Parker, C.W., Letham, D.S. and Summons, R.E. Preparation and characterization, using high-performance liquid chromatography, of an enzyme forming glucosides of cytokinins. Biochim. Biophys. Acta 570 (1979) 124–139. [PMID: 486500]
[EC 2.4.1.118 created 1984]
 
 
EC 2.4.1.119     
Accepted name: dolichyl-diphosphooligosaccharide—protein glycotransferase
Reaction: dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
Other name(s): dolichyldiphosphooligosaccharide-protein glycosyltransferase; asparagine N-glycosyltransferase; dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase; dolichylpyrophosphodiacetylchitobiose-protein glycosyltransferase; oligomannosyltransferase; oligosaccharide transferase; dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase
Systematic name: dolichyl-diphosphooligosaccharide:protein-L-asparagine oligopolysaccharidotransferase
Comments: Transfers the glucosyl-mannosyl-glucosamine polysaccharide side-chains of glycoproteins to an asparagine residue in the sequence Asn-Xaa-Ser or Asn-Xaa-Thr in the nascent polypeptide chains of the protein moiety.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 75302-32-8
References:
1.  Das, R.C. and Heath, E.C. Dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase; solubilization, purification, and properties. Proc. Natl. Acad. Sci. USA 77 (1980) 3811–3815. [PMID: 6933437]
[EC 2.4.1.119 created 1984]
 
 
EC 2.4.1.120     
Accepted name: sinapate 1-glucosyltransferase
Reaction: UDP-glucose + sinapate = UDP + 1-sinapoyl-D-glucose
Other name(s): uridine diphosphoglucose-sinapate glucosyltransferase; UDP-glucose:sinapic acid glucosyltransferase; uridine 5′-diphosphoglucose-hydroxycinnamic acid acylglucosyltransferase
Systematic name: UDP-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, IUBMB, KEGG, 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, IUBMB, KEGG, 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: glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase
Reaction: UDP-galactose + glycoprotein N-acetyl-D-galactosamine = UDP + glycoprotein D-galactosyl-(1→3)-N-acetyl-D-galactosamine
Other name(s): uridine diphosphogalactose-mucin β-(1→3)-galactosyltransferase
Systematic name: UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase
Comments: The non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins can act as acceptors.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, 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. [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]
[EC 2.4.1.122 created 1984]
 
 
EC 2.4.1.123     
Accepted name: inositol 3-α-galactosyltransferase
Reaction: UDP-galactose + myo-inositol = UDP + O-α-D-galactosyl-(1→3)-1D-myo-inositol
For diagram of stachyose biosynthesis, click here
Glossary: galactinol = 3-O-α-D-galactosyl-1D-myo-inositol
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
Systematic name: UDP-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, IUBMB, KEGG, 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: sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + [(1→6)-α-D-glucosyl]n+1
Other name(s): water-soluble-glucan synthase; GTF-S; 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
Systematic name: sucrose:(1→6)-α-D-glucan 3(6)-α-D-glucosyltransferase
Comments: Also transfers glucosyl residues to the 3-position on glucose residues in glucans, producing a highly-branched 1,6-α-D-glucan.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, 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. [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. [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. [PMID: 2937877]
[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, IUBMB, KEGG, 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
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, IUBMB, KEGG, 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, IUBMB, KEGG, 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, IUBMB, KEGG, 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. [PMID: 11320055]
[EC 2.4.1.129 created 1984, modified 2002]
 
 
EC 2.4.1.130     
Accepted name: dolichyl-phosphate-mannose—glycolipid α-mannosyltransferase
Reaction: Transfers an α-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide
Other name(s): dolichol phosphomannose-oligosaccharide-lipid mannosyltransferase; oligomannosylsynthase
Systematic name: dolichyl-phosphate-D-mannose:glycolipid α-D-mannosyltransferase
Comments: Four of the nine mannosyl residues in the main membrane lipid-linked oligosaccharide of the structure Glc3Man9GlcNAc2 are produced by the action of this enzyme.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 77967-76-1
References:
1.  Rearick, J.I., Fujimoto, K. and Kornfeld, S. Identification of the mannosyl donors involved in the synthesis of lipid-linked oligosaccharides. J. Biol. Chem. 256 (1981) 3762–3769. [PMID: 6163773]
[EC 2.4.1.130 created 1984]
 
 
EC 2.4.1.131     
Accepted name: glycolipid 2-α-mannosyltransferase
Reaction: Transfers an α-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an α-(1→2)-D-mannosyl-D-mannose linkage
Other name(s): guanosine diphosphomannose-oligosaccharide-lipid mannosyltransferase; GDP-mannose-oligosaccharide-lipid mannosyltransferase; oligosaccharide-lipid mannosyltransferase; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase
Systematic name: GDP-mannose:glycolipid 2-α-D-mannosyltransferase
Comments: The two 1,2-linked mannosyl residues in the mammalian lipid-linked oligosaccharide of the structure Glc3Man9GlcNAc2 are produced by the action of this enzyme.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 74506-43-7
References:
1.  Schutzbach, J.S., Springfield, J.D. and Jensen, J.W. The biosynthesis of oligosaccharide-lipids. Formation of an α-1,2-mannosyl-mannose linkage. J. Biol. Chem. 255 (1980) 4170–4175. [PMID: 6154707]
[EC 2.4.1.131 created 1984]
 
 
EC 2.4.1.132     
Accepted name: glycolipid 3-α-mannosyltransferase
Reaction: Transfers an α-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an α-(1→3)-D-mannosyl-D-mannose linkage
Other name(s): mannosyltransferase II; guanosine diphosphomannose-oligosaccharide-lipid II mannosyltransferase; GDP-mannose-oligosaccharide-lipid mannosyltransferase II; GDP-mannose:glycolipid 1,3-α-D-mannosyltransferase
Systematic name: GDP-mannose:glycolipid 3-α-D-mannosyltransferase
Comments: The 1,3-linked mannosyl residue in the mammalian lipid-linked oligosaccharide of the structure Glc3Man9GlcNAc2 is produced by this enzyme.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 81181-76-2
References:
1.  Jensen, J.W. and Schutzbach, J.S. The biosynthesis of oligosaccharide-lipids. Partial purification and characterization of mannosyltransferase II. J. Biol. Chem. 256 (1981) 12899–12904. [PMID: 7309740]
[EC 2.4.1.132 created 1984]
 
 
EC 2.4.1.133     
Accepted name: xylosylprotein 4-β-galactosyltransferase
Reaction: UDP-galactose + O-β-D-xylosylprotein = UDP + 4-β-D-galactosyl-O-β-D-xylosylprotein
For diagram of the early stages of heparan and chondroitin biosynthesis, click here
Other name(s): UDP-D-galactose:D-xylose galactosyltransferase; UDP-D-galactose:xylose galactosyltransferase; galactosyltransferase I; uridine diphosphogalactose-xylose galactosyltransferase
Systematic name: UDP-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 52227-72-2
References:
1.  Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200–5207. [PMID: 1150655]
2.  Okajima, T., Yoshida, K., Kondo, T. and Furukawa, K. Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 274 (1999) 22915–22918. [PMID: 10438455]
[EC 2.4.1.133 created 1984, modified 2002]
 
 
EC 2.4.1.134     
Accepted name: galactosylxylosylprotein 3-β-galactosyltransferase
Reaction: UDP-galactose + 4-β-D-galactosyl-O-β-D-xylosylprotein = UDP + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein
For diagram of the early stages of heparan and chondroitin biosynthesis, click here
Other name(s): galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase
Systematic name: UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 56626-21-2, 56626-19-8
References:
1.  Robinson, J.A. and Robinson, H.C. Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II. Biochem. J. 227 (1985) 805–814. [PMID: 3924029]
2.  Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200–5207. [PMID: 1150655]
3.  Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6). J. Biol. Chem. 276 (2001) 48189–48195. [PMID: 11551958]
[EC 2.4.1.134 created 1984, modified 2002]
 
 
EC 2.4.1.135     
Accepted name: galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase
Reaction: UDP-glucuronate + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein = UDP + 3-β-D-glucuronosyl-3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein
For diagram of the early stages of heparan and chondroitin biosynthesis, click here
Other name(s): glucuronosyltransferase I; uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-protein D-glucuronosyltransferase
Systematic name: UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein D-glucuronosyltransferase
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 227184-75-0
References:
1.  Helting, J. and Roden, L. Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region. J. Biol. Chem. 244 (1969) 2799–2805. [PMID: 5770003]
2.  Helting, T. Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma. J. Biol. Chem. 247 (1972) 4327–4332. [PMID: 4260846]
3.  Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, S., Kawasaki, T. and Sugahara, K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273 (1998) 6615–6618. [PMID: 9506957]
[EC 2.4.1.135 created 1984, modified 2002]
 
 
EC 2.4.1.136     
Accepted name: gallate 1-β-glucosyltransferase
Reaction: UDP-glucose + gallate = UDP + 1-galloyl-β-D-glucose
Other name(s): UDP-glucose—vanillate 1-glucosyltransferase; UDPglucose:vanillate 1-O-glucosyltransferase; UDPglucose:gallate glucosyltransferase
Systematic name: UDP-glucose:gallate β-D-glucosyltransferase
Comments: A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. Vanillin is the best acceptor investigated.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 89700-30-1
References:
1.  Gross, G.G. Synthesis of β-glucogallin from UDP-glucose and gallic acid by an enzyme preparation from oak leaves. FEBS Lett. 148 (1982) 67–70.
2.  Gross, G.G. Partial-purification and properties of UDP-glucose-vanillate 1-O-glucosyl transferase from oak leaves. Phytochemistry 22 (1983) 2179–2182.
[EC 2.4.1.136 created 1984]
 
 
EC 2.4.1.137     
Accepted name: sn-glycerol-3-phosphate 2-α-galactosyltransferase
Reaction: UDP-galactose + sn-glycerol 3-phosphate = UDP + 2-(α-D-galactosyl)-sn-glycerol 3-phosphate
Other name(s): floridoside-phosphate synthase; UDP-galactose:sn-glycerol-3-phosphate-2-D-galactosyl transferase; FPS; UDP-galactose, sn-3-glycerol phosphate:1→2′ galactosyltransferase; floridoside phosphate synthetase; floridoside phosphate synthase
Systematic name: UDP-galactose:sn-glycerol-3-phosphate 2-α-D-galactosyltransferase
Comments: The product is hydrolysed by a phosphatase to floridoside (cf. EC 2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 80747-34-8
References:
1.  Gray, N.C.C. and Strickland, K.P. The purification and characterization of a phospholipase A2 activity from the 106,000 x g pellet (microsomal fraction) of bovine brain acting on phosphatidylinositol. Can. J. Biochem. 60 (1982) 108–117. [PMID: 7083039]
[EC 2.4.1.137 created 1984]
 
 
EC 2.4.1.138     
Accepted name: mannotetraose 2-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + (1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-α-D-mannosyl-D-mannose = UDP + (1→3)-α-D-mannosyl-(1→2)-(N-acetyl-α-D-glucosaminyl-α-D-mannosyl)-(1→2)-α-D-mannosyl-D-mannose
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-D-glucosamine:α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-D-mannose α-N-acetyl-D-glucosaminyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, 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]
[EC 2.4.1.138 created 1984]
 
 
EC 2.4.1.139     
Accepted name: maltose synthase
Reaction: 2 α-D-glucose 1-phosphate + H2O = maltose + 2 phosphate
Systematic name: α-D-glucose-1-phosphate:α-D-glucose-1-phosphate 4-α-D-glucosyltransferase (dephosphorylating)
Comments: Neither free phosphate nor maltose 1-phosphate is an intermediate in the reaction.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 81669-74-1
References:
1.  Schilling, N. Characterization of maltose biosynthesis from α-D-glucose-1-phosphate in Spinacia oleracea L. Planta 154 (1982) 87–93.
[EC 2.4.1.139 created 1984]
 
 
EC 2.4.1.140     
Accepted name: alternansucrase
Reaction: Transfers alternately an α-D-glucosyl residue from sucrose to the 6-position and the 3-position of the non-reducing terminal residue of an α-D-glucan, thus producing a glucan having alternating α-(1→6)- and α-(1→3)-linkages
Other name(s): sucrose-1,6(3)-α-glucan 6(3)-α-glucosyltransferase; sucrose:1,6-, 1,3-α-D-glucan 3-α- and 6-α-D-glucosyltransferase; sucrose:1,6(1,3)-α-D-glucan 6(3)-α-D-glucosyltransferase
Systematic name: sucrose:(1→6)[(1→3)]-α-D-glucan 6(3)-α-D-glucosyltransferase
Comments: The product, which has quite different properties from other dextrans, has been called alternan.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 100630-46-4
References:
1.  Cote, G.L. and Robyt, J.F. Isolation and partial characterization of an extracellular glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that synthesizes an alternating (1→6), (1→3)-α-D-glucan. Carbohydr. Res. 101 (1982) 57–74. [PMID: 7060056]
[EC 2.4.1.140 created 1984, modified 2003]
 
 
EC 2.4.1.141     
Accepted name: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N′-diacetylchitobiosyl-diphosphodolichol
Other name(s): UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase; uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase; N,N′-diacetylchitobiosylpyrophosphoryldolichol synthase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol N-acetyl-D-glucosaminyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 75536-54-8
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [PMID: 6215245]
2.  Turco, S.J. and Heath, E.C. Glucuronosyl-N-acetylglucosaminyl pyrophosphoryldolichol. Formation in SV40-transformed human lung fibroblasts and biosynthesis in rat lung microsomal preparations. J. Biol. Chem. 252 (1977) 2918–2928. [PMID: 192724]
[EC 2.4.1.141 created 1984]
 
 
EC 2.4.1.142     
Accepted name: chitobiosyldiphosphodolichol β-mannosyltransferase
Reaction: GDP-mannose + chitobiosyldiphosphodolichol = GDP + β-(1→4)-D-mannosylchitobiosyldiphosphodolichol
Other name(s): guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
Systematic name: GDP-mannose:chitobiosyldiphosphodolichol β-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 83380-85-2
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [PMID: 6215245]
2.  Takahashi, T., Honda, R. and Nishikawa, Y. Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1. Glycobiology 10 (2000) 321–327. [PMID: 10704531]
[EC 2.4.1.142 created 1984, modified 2001]
 
 
EC 2.4.1.143     
Accepted name: α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + 6-(α-D-mannosyl)-β-D-mannosyl-R = UDP + 6-(2-[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R
For diagram of the reactions of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): N-acetylglucosaminyltransferase II; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mannoside α1→6-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-1,6-mannosylglycoprotein β-1-2-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-D-mannoside β1-2-acetylglucosaminyltransferase; UDP-GlcNAc:mannoside α1-6 acetylglucosaminyltransferase; α-1,6-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTII
Systematic name: UDP-N-acetyl-D-glucosamine:6-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts after N-acetylglucosaminyltransferase I but before N-acetylglucosaminyltransferases III, IV, V and VI (click here for diagram).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 105913-04-0
References:
1.  Bendiak, B. and Schacter, H. Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:α-D-mannoside β1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem. 262 (1987) 5775–5783. [PMID: 2952644]
2.  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]
3.  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]
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.  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]
6.  Bendiak, B. and Schachter, H. Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:α-D-mannoside β-1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem. 262 (1987) 5784–5790. [PMID: 2952644]
[EC 2.4.1.143 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984)]
 
 
EC 2.4.1.144     
Accepted name: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-mannosyl-R = UDP + 4-(N-acetyl-β-D-glucosaminyl)-β-D-mannosyl-R
For diagram of reaction, click here
Other name(s): N-acetylglucosaminyltransferase III; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase III; β-1,4-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIII
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor (click here for diagram). The action of this enzyme probably prevents further attachment of N-acetylglucosamine residues to the growing carbohydrate chain.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 83744-93-8
References:
1.  Narasimhan, S. Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide β4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β1-4 linkage to the β-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J. Biol. Chem. 257 (1982) 10235–10242. [PMID: 6213618]
2.  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]
[EC 2.4.1.144 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984)]
 
 
EC 2.4.1.145     
Accepted name: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R = UDP + 3-(2,4-bis[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R
For diagram of reaction, click here
Other name(s): N-acetylglucosaminyltransferase IV; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; β-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase IV; α-1,3-mannosylglycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIV
Systematic name: UDP-N-acetyl-D-glucosamine:3-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor (click here for diagram). The best acceptor for this enzyme is probably the same as that favoured by EC 2.4.1.144, β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 86498-16-0
References:
1.  Gleeson, P.A. and Schachter, H. Control of glycoprotein synthesis. J. Biol. Chem. 258 (1983) 6162–6173. [PMID: 6222042]
[EC 2.4.1.145 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984)]
 
 
EC 2.4.1.146     
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-galactosyl-(1→3)-[N-acetyl-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase (elongating); elongation 3β-GalNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to -D-galactose of β-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→3)-[N-acetyl-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 87927-99-9
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [PMID: 6226356]
[EC 2.4.1.146 created 1984]
 
 
EC 2.4.1.147     
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-β-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-β-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase; mucin core 3 β3-GlcNAc-transferase; Core 3β-GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 87927-96-6
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [PMID: 6226356]
[EC 2.4.1.147 created 1984]
 
 
EC 2.4.1.148     
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→3)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-mucin β(1→6)-acetylglucosaminyltransferase B; core 4 β6-GalNAc-transferase; core 6β-GalNAc-transferase B; UDP-N-acetyl-D-glucosamine:O-oligosaccharide-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of N-acetyl-β-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R 6-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [PMID: 6226356]
[EC 2.4.1.148 created 1984]
 
 
EC 2.4.1.149     
Accepted name: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R
Other name(s): uridine diphosphoacetylglucosamine-acetyllactosaminide β1→3-acetylglucosaminyltransferase; poly-N-acetyllactosamine extension enzyme; Galβ1→4GlcNAc-R β1→3 N-acetylglucosaminyltransferase; UDP-GlcNAc:GalR, β-D-3-N-acetylglucosaminyltransferase; N-acetyllactosamine β(1-3)N-acetylglucosaminyltransferase; UDP-GlcNAc:Galβ1→4GlcNAcβ-Rβ1→3-N-acetylglucosaminyltransferase; GnTE; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosamine β-1,3-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine 3-β-N-acetyl-D-glucosaminyltransferase
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and other glycoproteins and oligosaccharides.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 85638-39-7
References:
1.  Takeya, A., Hosomi, O. and Kogure, T. The presence of N-acetyllactosamine and lactose: β (1-3)N-acetylglucosaminyltransferase activity in human urine. Jpn. J. Med. Sci. Biol. 38 (1985) 1–8. [PMID: 3160874]
2.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
[EC 2.4.1.149 created 1984]
 
 
EC 2.4.1.150     
Accepted name: N-acetyllactosaminide β-1,6-N-acetylglucosaminyl-transferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→6)-β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R
Other name(s): N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-GlcNAc:Gal-R, β-D-6-N-acetylglucosaminyltransferasel UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminide 6-β-N-acetyl-D-glucosaminyltransferase
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 85638-40-0
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
[EC 2.4.1.150 created 1984]
 
 
EC 2.4.1.151     
Transferred entry: N-acetyllactosaminide α-1,3-galactosyltransferase. Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase
[EC 2.4.1.151 created 1984, deleted 2002]
 
 
EC 2.4.1.152     
Accepted name: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + (1→4)-β-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + (1→4)-β-D-galactosyl-[α-(1→3)-L-fucosyl]-N-acetyl-D-glucosaminyl-R
For diagram of reaction, click here
Other name(s): Lewis-negative α-3-fucosyltransferase; plasma α-3-fucosyltransferase; guanosine diphosphofucose-glucoside α1→3-fucosyltransferase; galactoside 3-fucosyltransferase; GDP-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:(1→4)-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase
Comments: Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 39279-34-0
References:
1.  Johnson, P.H., Yates, A.D. and Watkins, W.M. Human salivary fucosyltransferase: evidence for two distinct α-3-L-fucosyltransferase activities one of which is associated with the Lewis blood Le gene. Biochem. Biophys. Res. Commun. 100 (1981) 1611–1618. [PMID: 7295318]
2.  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]
3.  Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893–21900. [PMID: 12676935]
[EC 2.4.1.152 created 1984, modified 2002]
 
 
EC 2.4.1.153     
Accepted name: dolichyl-phosphate α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UDP + dolichyl N-acetyl-α-D-glucosaminyl phosphate
Other name(s): uridine diphosphoacetylglucosamine-dolichol phosphate acetylglucosaminyltransferase; dolichyl phosphate acetylglucosaminyltransferase; dolichyl phosphate N-acetylglucosaminyltransferase; UDP-N-acetylglucosamine-dolichol phosphate N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Links to other databases: