Enzyme Nomenclature Continued from EC 2.3.3

EC 2.4

Glycosyltransferases

('Glucosyltransferase', 'fructosyltransferase' etc. may be replaced by 'transglucosylase', 'transfructosylase', etc.).

Sections

EC 2.4.1 Hexosyltransferases
EC 2.4.2 Pentosyltransferases
EC 2.4.99 Transferring Other Glycosyl Groups


EC 2.4.1 Hexosyltransferases

Contents

See separate file for EC 2.4.1.51 to EC 2.4.1.100, EC 2.4.1.101 to EC 2.4.1.150, EC 2.4.1.151 to EC 2.4.1.200, EC 2.4.1.201 to EC 2.4.1.250, EC 2.4.1.251 to EC 2.4.1.300 and EC 2.4.1.301 to EC 2.4.1.346.

EC 2.4.1.1 glycogen phosphorylase
EC 2.4.1.2 dextrin dextranase
EC 2.4.1.3 deleted, included in EC 2.4.1.25
EC 2.4.1.4 amylosucrase
EC 2.4.1.5 dextransucrase
EC 2.4.1.6 deleted
EC 2.4.1.7 sucrose phosphorylase
EC 2.4.1.8 maltose phosphorylase
EC 2.4.1.9 inulosucrase
EC 2.4.1.10 levansucrase
EC 2.4.1.11 glycogen(starch) synthase
EC 2.4.1.12 cellulose synthase (UDP-forming)
EC 2.4.1.13 sucrose synthase
EC 2.4.1.14 sucrose-phosphate synthase
EC 2.4.1.15 α,α-trehalose-phosphate synthase (UDP-forming)
EC 2.4.1.16 chitin synthase
EC 2.4.1.17 glucuronosyltransferase
EC 2.4.1.18 1,4-α-glucan branching enzyme
EC 2.4.1.19 cyclomaltodextrin glucanotransferase
EC 2.4.1.20 cellobiose phosphorylase
EC 2.4.1.21 starch synthase (glycosyl-transferring)
EC 2.4.1.22 lactose synthase
EC 2.4.1.23 sphingosine β-galactosyltransferase
EC 2.4.1.24 1,4-α-glucan 6-α-glucosyltransferase
EC 2.4.1.25 4-α-glucanotransferase
EC 2.4.1.26 DNA α-glucosyltransferase
EC 2.4.1.27 DNA β-glucosyltransferase
EC 2.4.1.28 glucosyl-DNA β-glucosyltransferase
EC 2.4.1.29 cellulose synthase (GDP-forming)
EC 2.4.1.30 1,3-β-oligoglucan phosphorylase
EC 2.4.1.31 laminaribiose phosphorylase
EC 2.4.1.32 glucomannan 4-β-mannosyltransferase
EC 2.4.1.33 mannuronan synthase
EC 2.4.1.34 1,3-β-glucan synthase
EC 2.4.1.35 phenol β-glucosyltransferase
EC 2.4.1.36 α,α-trehalose-phosphate synthase (GDP-forming)
EC 2.4.1.37 fucosylglycoprotein 3-α-galactosyltransferase
EC 2.4.1.38 β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase
EC 2.4.1.39 steroid N-acetylglucosaminyltransferase
EC 2.4.1.40 fucosylgalactose α-N-acetylgalactosaminyltransferase
EC 2.4.1.41 polypeptide N-acetylgalactosaminyltransferase
EC 2.4.1.42 deleted, included in EC 2.4.1.17
EC 2.4.1.43 polygalacturonate 4-α-galacturonosyltransferase
EC 2.4.1.44 lipopolysaccharide 3-α-galactosyltransferase
EC 2.4.1.45 now included with EC 2.4.1.47
EC 2.4.1.46 monogalactosyldiacylglycerol synthase
EC 2.4.1.47 N-acylsphingosine galactosyltransferase
EC 2.4.1.48 heteroglycan α-mannosyltransferase
EC 2.4.1.49 cellodextrin phosphorylase
EC 2.4.1.50 procollagen galactosyltransferase

See the following files for:

EC 2.4.1.51 to EC 2.4.1.100
EC 2.4.1.101 to EC 2.4.1.150
EC 2.4.1.151 to EC 2.4.1.200
EC 2.4.1.201 to EC 2.4.1.250
EC 2.4.1.251 to EC 2.4.1.300
EC 2.4.1.301 to EC 2.4.1.346

Entries

EC 2.4.1.1

Accepted name: glycogen 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; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase (ambiguous)

Systematic name: (1→4)-α-D-glucan:phosphate α-D-glucosyltransferase

Comments: This entry covers several enzymes from different sources that act in vivo on different forms of (1→4)-α-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of α-1,4-glucosidic bonds from the non-reducing ends of linear poly(1→4)-α-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an α-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.

Links to other databases: BRENDA, EXPASY, KEGG, PDB, Metacyc, CAS registry number: 9035-74-9

References:

1. 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.

2. Green, A.A. and Cori, G.T. Crystalline muscle phosphorylase. I. Preparation, properties, and molecular weight. J. Biol. Chem. 151 (1943) 21-29.

3. 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]

4. Cowgill, R.W. Lobster muscle phosphorylase: purfication and properties. J. Biol. Chem. 234 (1959) 3146-3153. [PMID: 13812491]

5. 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]

6. 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.

[EC 2.4.1.1 created 1961, modified 2013]

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, KEGG, Metacyc, 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.

[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, KEGG, Metacyc, 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, KEGG, Metacyc, PDB, 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, KEGG, Metacyc, PDB, 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.

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, KEGG, Metacyc, 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.

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.

[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, KEGG, Metacyc, 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 + α-D-glucosyl-(1→2)-[(2→6)-β-D-fructosyl]n = D-glucose + α-D-glucosyl-(1→2)-[(2→6)-β-D-fructosyl]n+1

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:α-D-glucosyl-(1→2)-(2→6)-β-D-fructan 6-β-D-fructosyltransferase

Comments: Some other sugars can act as D-fructosyl acceptors.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, 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]

4. Meng, G. and Futterer, K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat. Struct. Biol. 10 (2003) 935941. [PMID: 14517548]

[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 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, KEGG, Metacyc, PDB, 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, KEGG, Metacyc, PDB, CAS registry number: 9027-19-4

References:

1. Glaser, L. The synthesis of cellulose in cell-free extracts of Acetobacter xylinum. J. Biol. Chem. 232 (1958) 627-636. [PMID: 13549448]

[EC 2.4.1.12 created 1961]

EC 2.4.1.13

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, KEGG, Metacyc, PDB, 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.

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.

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.

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., Muñoz, 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, KEGG, Metacyc, 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, KEGG, Metacyc, 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.

2. Candy, D.J. and Kilby, B.A. The biosynthesis of trehalose in the locust fat body. Biochem. J. 78 (1961) 531-536.

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.

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.

[EC 2.4.1.15 created 1961]

EC 2.4.1.16

Accepted name: chitin synthase

Reaction: UDP-N-acetyl-α-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

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, KEGG, Metacyc, 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.

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, KEGG, Metacyc, 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, KEGG, Metacyc, 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. [PMID: 16522734]

[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 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, KEGG, Metacyc, 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, KEGG, Metacyc, PDB, 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.

[EC 2.4.1.20 created 1965]

EC 2.4.1.21

Accepted name: starch synthase (glycosyl-transferring)

Reaction: ADP-α-D-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-α-D-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, KEGG, Metacyc, 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, p. 122-138.

[EC 2.4.1.21 created 1965]

EC 2.4.1.22

Accepted name: lactose synthase

Reaction: UDP-α-D-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; UDP-galactose:D-glucose 4-β-D-galactosyltransferase

Systematic name: UDP-α-D-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, KEGG, Metacyc, 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.

[EC 2.4.1.22 created 1965]

EC 2.4.1.23

Accepted name: sphingosine β-galactosyltransferase

Reaction: UDP-α-D-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; UDP-galactose:sphingosine 1-β-galactosyltransferase

Systematic name: UDP-α-D-galactose:sphingosine 1-β-galactosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.

[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, KEGG, Metacyc, CAS registry number: 9030-12-0

References:

1. Abdullah, M. and Whelan, W.J. Synthesis of α-1:6-glucosidic linkages by a transglycosylase from potato. Biochem. J. 75 (1960) 12P only.

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, KEGG, Metacyc, 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. [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 only. [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, KEGG, Metacyc, 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.

[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, KEGG, Metacyc, 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.

[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, KEGG, Metacyc, 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.

[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, KEGG, Metacyc, 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, KEGG, Metacyc, 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, KEGG, Metacyc, 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.

[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: GDPmannose:glucomannan 4-β-D-mannosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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: mannuronan synthase

Reaction: GDP-α-D-mannuronate + [(1→4)-β-D-mannuronosyl]n = GDP + [(1→4)-β-D-mannuronosyl]n+1

Glossary: poly[β-(1,4)-D-mannuronate] = mannuronan

Other name(s): mannuronosyl transferase; alginate synthase (incorrect); alg8 (gene name); alg44 (gene name); GDP-D-mannuronate:alginate D-mannuronyltransferase

Systematic name: GDP-α-D-mannuronate:mannuronan D-mannuronatetransferase

Comments: The enzyme catalyses the polymerization of β-D-mannuronate residues into a mannuronan polymer, an intermediate in the biosynthesis of alginate. It is found in brown algae and in alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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]

2. Remminghorst, U. and Rehm, B.H. In vitro alginate polymerization and the functional role of Alg8 in alginate production by Pseudomonas aeruginosa. Appl. Environ. Microbiol. 72 (2006) 298-305. [PMID: 16391057]

3. Oglesby, L.L., Jain, S. and Ohman, D.E. Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization. Microbiology 154 (2008) 1605-1615. [PMID: 18524915]

[EC 2.4.1.33 created 1972, modified 2015]

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, KEGG, Metacyc, 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 (ambiguous); phenol-β-D-glucosyltransferase; UDP glucosyltransferase (ambiguous); UDP-glucose glucosyltransferase (ambiguous); uridine diphosphoglucosyltransferase

Systematic name: UDP-glucose:phenol β-D-glucosyltransferase

Comments: Acts on a wide range of phenols.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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, KEGG, Metacyc, 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-α-D-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; UDP-galactose:α-L-fucosyl-(1→2)-D-galactoside 3-α-D-galactosyltransferase

Systematic name: UDP-α-D-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, KEGG, Metacyc, 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-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase

Reaction: UDP-α-D-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; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase

Systematic name: UDP-α-D-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, KEGG, Metacyc, 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-α-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, KEGG, Metacyc, 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-α-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, KEGG, Metacyc, 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-α-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; polypeptide GalNAc-transferase

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, KEGG, Metacyc, 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 UDP-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, KEGG, Metacyc, 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-α-D-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; UDP-galactose:lipopolysaccharide 3-α-D-galactosyltransferase

Systematic name: UDP-α-D-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, KEGG, Metacyc, 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 Deleted entry: 2-hydroxyacylsphingosine 1-β-galactosyltransferase, now included with EC 2.4.1.47, N-acylsphingosine galactosyltransferase (EC 2.4.1.45 created 1972, deleted 2016)]

EC 2.4.1.46

Accepted name: monogalactosyldiacylglycerol synthase

Reaction: UDP-α-D-galactose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol

For diagram 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; UDP-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase

Systematic name: UDP-α-D-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, KEGG, Metacyc, 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-α-D-galactose + a ceramide = UDP + a β-D-galactosylceramide

Glossary: a ceramide = an N-acylsphingosine

Other name(s): UGT8 (gene name); CGT (gene name); UDP galactose-N-acylsphingosine galactosyltransferase; uridine diphosphogalactose-acylsphingosine galactosyltransferase; UDP-galactose:N-acylsphingosine D-galactosyltransferase; UDP-α-D-galactose:N-acylsphingosine D-galactosyltransferase; 2-hydroxyacylsphingosine 1-β-galactosyltransferase

Systematic name: UDP-α-D-galactose:N-acylsphingosine β-D-galactosyltransferase (configuration-inverting)

Comments: This membrane-bound, endoplasmic reticulum-located enzyme catalyses the last step in the synthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. It has a strong preference for ceramides that contain hydroxylated fatty acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

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]

3. Morell, P., Costantino-Ceccarini, E. and Radin, N.S. The biosynthesis by brain microsomes of cerebrosides containing nonhydroxy fatty acids. Arch. Biochem. Biophys. 141 (1970) 738-748. [PMID: 5497154]

4. 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]

5. Akanuma, H. and Kishimoto, Y. Synthesis of ceramides and cerebrosides containing both α-hydroxy and nonhydroxy fatty acids from lignoceroyl-CoA by rat brain microsomes. J. Biol. Chem. 254 (1979) 1050-1060. [PMID: 762114]

6. Koul, O. and Jungalwala, F.B. UDP-galactose:ceramide galactosyltransferase of rat central-nervous-system myelin. Biochem. J. 194 (1981) 633-637. [PMID: 7306007]

7. Schulte, S. and Stoffel, W. Ceramide UDP-galactosyltransferase from myelinating rat brain: purification, cloning, and expression. Proc. Natl. Acad. Sci. USA 90 (1993) 10265-10269. [PMID: 7694285]

8. Sprong, H., Kruithof, B., Leijendekker, R., Slot, J.W., van Meer, G. and van der Sluijs, P. UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum. J. Biol. Chem. 273 (1998) 25880-25888. [PMID: 9748263]

9. Fewou, S.N., Bussow, H., Schaeren-Wiemers, N., Vanier, M.T., Macklin, W.B., Gieselmann, V. and Eckhardt, M. Reversal of non-hydroxy:α-hydroxy galactosylceramide ratio and unstable myelin in transgenic mice overexpressing UDP-galactose:ceramide galactosyltransferase. J. Neurochem. 94 (2005) 469-481. [PMID: 15998297]

[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, KEGG, Metacyc, 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, KEGG, Metacyc, 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-α-D-galactose + [procollagen]-(2S,5R)-5-hydroxy-L-lysine = UDP + [procollagen]-(2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-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; UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase; UDP-α-D-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase

Systematic name: UDP-α-D-galactose:[procollagen]-(2S,5R)-5-hydroxy-L-lysine 5-β-D-galactosyltransferase (configuration-inverting)

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, KEGG, Metacyc, 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.

3. Schegg, B., Hulsmeier, A.J., Rutschmann, C., Maag, C. and Hennet, T. Core glycosylation of collagen is initiated by two β(1-O)galactosyltransferases. Mol. Cell Biol. 29 (2009) 943-952. [PMID: 19075007]

[EC 2.4.1.50 created 1972, modified 1983]


Continued with EC 2.4.1.51 to EC 2.4.1.100
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