The Enzyme Database

Displaying entries 51-100 of 160.

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EC 2.4.1.98      
Deleted entry:  UDP-galactoseN-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 2.4.1.122     
Accepted name: N-acetylgalactosaminide β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-galactosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R
Other name(s): glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase; uridine diphosphogalactose-mucin β-(1→3)-galactosyltransferase; UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase; UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase; wbnJ (gene name); wbiP (gene name); C1GALT1 (gene name); UDP-α-D-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-galactosaminyl-R β-1,3-galactosyltransferase (configuration-inverting)
Comments: The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97089-61-7
References:
1.  Hesford, F.J., Berger, E.G. and van den Eijnden, D.H. Identification of the product formed by human erythrocyte galactosyltransferase. Biochim. Biophys. Acta 659 (1981) 302–311. [DOI] [PMID: 6789880]
2.  Mendicino, J., Sivakami, S., Davila, M. and Chandrasekaran, E.V. Purification and properties of UDP-gal:N-acetylgalactosaminide mucin:β1,3-galactosyltransferase from swine trachea mucosa. J. Biol. Chem. 257 (1982) 3987–3994. [PMID: 6801057]
3.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
4.  Ju, T., Brewer, K., D'Souza, A., Cummings, R.D. and Canfield, W.M. Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277 (2002) 178–186. [DOI] [PMID: 11677243]
5.  Yi, W., Perali, R.S., Eguchi, H., Motari, E., Woodward, R. and Wang, P.G. Characterization of a bacterial β-1,3-galactosyltransferase with application in the synthesis of tumor-associated T-antigen mimics. Biochemistry 47 (2008) 1241–1248. [DOI] [PMID: 18179256]
6.  Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]
[EC 2.4.1.122 created 1984 (EC 2.4.1.307 created 2013, incorporated 2016), modified 2016]
 
 
EC 2.4.1.123     
Accepted name: inositol 3-α-galactosyltransferase
Reaction: UDP-α-D-galactose + myo-inositol = UDP + O-α-D-galactosyl-(1→3)-1D-myo-inositol
For diagram of stachyose biosynthesis, click here
Glossary: O-α-D-galactosyl-(1→3)-1D-myo-inositol = galactinol
Other name(s): UDP-D-galactose:inositol galactosyltransferase; UDP-galactose:myo-inositol 1-α-D-galactosyltransferase; UDPgalactose:myo-inositol 1-α-D-galactosyltransferase; galactinol synthase; inositol 1-α-galactosyltransferase; uridine diphosphogalactose-inositol galactosyltransferase; GolS; UDP-galactose:myo-inositol 3-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:myo-inositol 3-α-D-galactosyltransferase
Comments: An enzyme from plants involved in the formation of raffinose and stachyose [cf. EC 2.4.1.67 (galactinol—raffinose galactosyltransferase) and EC 2.4.1.82 (galactinol—sucrose galactosyltransferase)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79955-89-8
References:
1.  Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C. Partial characterization of the galactinol forming enzyme from leaves of Cucumis sativus L. Plant Sci. Lett. 23 (1981) 25–33.
[EC 2.4.1.123 created 1984, modified 2003]
 
 
EC 2.4.1.133     
Accepted name: xylosylprotein 4-β-galactosyltransferase
Reaction: UDP-α-D-galactose + [protein]-3-O-(β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
For diagram of heparan and chondroitin biosynthesis (early stages), click here
Other name(s): UDP-D-galactose:D-xylose galactosyltransferase; UDP-D-galactose:xylose galactosyltransferase; galactosyltransferase I; uridine diphosphogalactose-xylose galactosyltransferase; UDP-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase; UDP-α-D-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase; UDP-α-D-galactose:O-β-D-xylosyl-[protein] 4-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:[protein]-3-O-(β-D-xylosyl)-L-serine 4-β-D-galactosyltransferase (configuration-inverting)
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, KEGG, MetaCyc, 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. [DOI] [PMID: 10438455]
[EC 2.4.1.133 created 1984, modified 2002]
 
 
EC 2.4.1.134     
Accepted name: galactosylxylosylprotein 3-β-galactosyltransferase
Reaction: UDP-α-D-galactose + [protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
For diagram of heparan and chondroitin biosynthesis (early stages), click here
Other name(s): galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase; UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase; UDP-α-D-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:[protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine (configuration-inverting)
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, KEGG, MetaCyc, 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. [DOI] [PMID: 11551958]
[EC 2.4.1.134 created 1984, modified 2002]
 
 
EC 2.4.1.137     
Accepted name: sn-glycerol-3-phosphate 2-α-galactosyltransferase
Reaction: UDP-α-D-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; UDP-galactose:sn-glycerol-3-phosphate 2-α-D-galactosyltransferase
Systematic name: UDP-α-D-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, KEGG, MetaCyc, 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 2.4.1.146     
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] = UDP + 3-O-{N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Glossary: core 2 = 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
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 β-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; 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; B3GNT3 (gene name)
Systematic name: UDP-N-acetyl-α-D-glucosamine:3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] 3-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 2 structure of O-glycans.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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. [DOI] [PMID: 6226356]
2.  Shiraishi, N., Natsume, A., Togayachi, A., Endo, T., Akashima, T., Yamada, Y., Imai, N., Nakagawa, S., Koizumi, S., Sekine, S., Narimatsu, H. and Sasaki, K. Identification and characterization of three novel β 1,3-N-acetylglucosaminyltransferases structurally related to the β 1,3-galactosyltransferase family. J. Biol. Chem. 276 (2001) 3498–3507. [PMID: 11042166]
[EC 2.4.1.146 created 1984, modified 2018]
 
 
EC 2.4.1.149     
Accepted name: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-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; β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine 3-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R 3-β N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on glycoproteins, glycolipids, and oligosaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-39-7
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]
2.  Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026]
3.  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]
[EC 2.4.1.149 created 1984 (EC 2.4.1.163 created 1989, incorporated 2016), modified 2016]
 
 
EC 2.4.1.156     
Accepted name: indolylacetyl-myo-inositol galactosyltransferase
Reaction: UDP-α-D-galactose + (indol-3-yl)acetyl-myo-inositol = UDP + 5-O-(indol-3-yl)acetyl-myo-inositol D-galactoside
Other name(s): uridine diphosphogalactose-indolylacetylinositol galactosyltransferase; indol-3-ylacetyl-myo-inositol galactoside synthase; UDP-galactose:indol-3-ylacetyl-myo-inositol 5-O-D-galactosyltransferase; UDP-galactose:(indol-3-yl)acetyl-myo-inositol 5-O-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:(indol-3-yl)acetyl-myo-inositol 5-O-D-galactosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85537-80-0
References:
1.  Corcuera, L.J., Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of indol-3-ylacetyl-myo-inositol galactoside. Biochem. J. 207 (1982) 283–290. [PMID: 7159382]
[EC 2.4.1.156 created 1986]
 
 
EC 2.4.1.167     
Accepted name: sucrose 6F-α-galactosyltransferase
Reaction: UDP-α-D-galactose + sucrose = UDP + 6F-α-D-galactosylsucrose
Other name(s): uridine diphosphogalactose-sucrose 6F-α-galactosyltransferase; UDPgalactose:sucrose 6fru-α-galactosyltransferase; sucrose 6F-α-galactotransferase; UDP-galactose:sucrose 6F-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:sucrose 6F-α-D-galactosyltransferase
Comments: The enzyme is involved in the synthesis of the trisaccharide planteose and higher analogues in the seeds of Plantago and Sesamum species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 92480-04-1
References:
1.  Hopf, H., Spanfelner, M. and Kandler, O. Planteose synthesis in seeds of Sesamum indicum L. Z. Pflanzenphysiol. 114 (1984) 485–492.
[EC 2.4.1.167 created 1989]
 
 
EC 2.4.1.173     
Accepted name: sterol 3β-glucosyltransferase
Reaction: UDP-glucose + a sterol = UDP + a sterol 3-β-D-glucoside
Other name(s): UDPG:sterol glucosyltransferase; UDP-glucose-sterol β-glucosyltransferase; sterol:UDPG glucosyltransferase; UDPG-SGTase; uridine diphosphoglucose-poriferasterol glucosyltransferase; uridine diphosphoglucose-sterol glucosyltransferase; sterol glucosyltransferase; sterol-β-D-glucosyltransferase; UDP-glucose-sterol glucosyltransferase
Systematic name: UDP-glucose:sterol 3-O-β-D-glucosyltransferase
Comments: Not identical with EC 2.4.1.192 (nuatigenin 3β-glucosyltransferase) or EC 2.4.1.193 (sarsapogenin 3β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123940-38-5, 9075-00-7
References:
1.  Duperon, R. and Duperon, P. Intracellular-localization of UDP-glucose-sterol glucosyl transferase and UDP-galactose-sterol galactosyl transferase activities in the leaves of tomato (Solanum lycopersicon L, Solanaceae). C.R. Acad. Sci. Paris, Ser. 3 304 (1987) 235–238.
2.  Kalinowska, M. and Wojciechowski, Z.A. Enzymatic-synthesis of nuatigenin 3-β-D-glucoside in oat (Avena sativa) leaves. Phytochemistry 25 (1986) 2525–2529.
3.  Kalinowska, M. and Wojciechowski, Z.A. Subcellular-localization of UDPG-nuatigenin glucosyltransferase in oat leaves. Phytochemistry 26 (1987) 353–357.
4.  Murakami-Murofushi, K. and Ohta, J. Expression of UDP-glucose: poriferasterol glucosyltransferase in the process of differentiation of a true slime mold, Physarum polycephalum. Biochim. Biophys. Acta 992 (1989) 412–415. [DOI] [PMID: 2528379]
5.  Wojciechowski, Z.A., Zimowski, J. and Tyski, S. Enzymatic synthesis of steryl 3β-D-monoglucosides in the slime mold Physarum polycephalum. Phytochemistry 16 (1977) 911–914.
[EC 2.4.1.173 created 1989]
 
 
EC 2.4.1.179     
Accepted name: lactosylceramide β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-R = UDP + β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-R
For diagram of glycolipid biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): uridine diphosphogalactose-lactosylceramide β1→3-galactosyltransferase; UDP-galactose:D-galactosyl-1,4-β-D-glucosyl-R β-1,3-galactosyltransferase; UDP-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase; UDP-α-D-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase
Comments: R may be an oligosaccharide or a glycolipid; lactose can also act as acceptor, but more slowly. Involved in the elongation of oligosaccharide chains, especially in glycolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 106769-64-6
References:
1.  Bailly, P., Piller, F. and Cartron, J.-P. Characterization and specific assay for a galactoside β-3-galactosyltransferase of human kidney. Eur. J. Biochem. 173 (1988) 417–422. [DOI] [PMID: 3129295]
[EC 2.4.1.179 created 1989]
 
 
EC 2.4.1.184     
Accepted name: galactolipid galactosyltransferase
Reaction: 2 a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[β-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Glossary: a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = monogalactosyldiacylglycerol
Other name(s): galactolipid-galactolipid galactosyltransferase; galactolipid:galactolipid galactosyltransferase; interlipid galactosyltransferase; GGGT; DGDG synthase (ambiguous); digalactosyldiacylglycerol synthase (ambiguous); 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:mono-3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; SFR2 (gene name)
Systematic name: 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol β-D-galactosyltransferase
Comments: The enzyme converts monogalactosyldiacylglycerol to digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol. All residues are connected by β linkages. The activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants, which is performed by EC 2.4.1.46, monogalactosyldiacylglycerol synthase, and EC 2.4.1.241, digalactosyldiacylglycerol synthase. Note that the β,β-digalactosyldiacylglycerol formed by this enzyme is different from the more common α,β-digalactosyldiacylglycerol formed by EC 2.4.1.241. The enzyme provides an important mechanism for the stabilization of the chloroplast membranes during freezing and drought stress.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66676-74-2
References:
1.  Dorne, A.-J., Block, M.A., Joyard, J. and Douce, R. The galactolipid-galactolipid galactosyltransferase is located on the outer surface of the outer-membrane of the chloroplast envelope. FEBS Lett. 145 (1982) 30–34.
2.  Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A., Dorne, A.-J. and Douce, R. Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer envelope membrane of spinach chloroplasts. Biochim. Biophys. Acta 877 (1986) 281–289.
3.  Heemskerk, J.W.M., Jacobs, F.H.H. and Wintermans, J.F.G.M. UDPgalactose-independent synthesis of monogalactosyldiacylglycerol. An enzymatic activity of the spinach chloroplast envelope. Biochim. Biophys. Acta 961 (1988) 38–47. [DOI]
4.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
5.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
6.  Fourrier, N., Bedard, J., Lopez-Juez, E., Barbrook, A., Bowyer, J., Jarvis, P., Warren, G. and Thorlby, G. A role for SENSITIVE TO FREEZING2 in protecting chloroplasts against freeze-induced damage in Arabidopsis. Plant J. 55 (2008) 734–745. [DOI] [PMID: 18466306]
7.  Moellering, E.R., Muthan, B. and Benning, C. Freezing tolerance in plants requires lipid remodeling at the outer chloroplast membrane. Science 330 (2010) 226–228. [DOI] [PMID: 20798281]
[EC 2.4.1.184 created 1990, modified 2005, modified 2015]
 
 
EC 2.4.1.205     
Accepted name: galactogen 6β-galactosyltransferase
Reaction: UDP-α-D-galactose + galactogen = UDP + (1→6)-β-D-galactosylgalactogen
Other name(s): uridine diphosphogalactose-galactogen galactosyltransferase; 1,6-D-galactosyltransferase; β-(1-6)-D-galactosyltransferase; UDP-galactose:galactogen β-1,6-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:galactogen 6-β-D-galactosyltransferase
Comments: Galactogen from Helix pomatia is the most effective acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 88273-54-5
References:
1.  Goudsmit, E.M., Ketchum, P.A., Grossens, M.K. and Blake, D.A. Biosynthesis of galactogen: identification of a β-(1→6)-D-galactosyltransferase in Helix pomatia albumen glands. Biochim. Biophys. Acta 992 (1989) 289–297. [DOI] [PMID: 2505854]
[EC 2.4.1.205 created 1992]
 
 
EC 2.4.1.228     
Accepted name: lactosylceramide 4-α-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of globotetraosylceramide biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-galactose; UDP-galactose:lactosylceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl(1↔1)ceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase
Comments: For explanation of superscript II in systematic name, see 2-carb.37.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52725-57-2
References:
1.  Bailly, P., Piller, F., Cartron, J.P., Leroy, Y. and Fournet, B. Identification of UDP-galactose: lactose (lactosylceramide) α-4 and β-3 galactosyltransferases in human kidney. Biochem. Biophys. Res. Commun. 141 (1986) 84–91. [DOI] [PMID: 3099784]
2.  Steffensen, R., Carlier, K., Wiels, J., Levery, S.B., Stroud, M., Cedergren, B., Nilsson Sojka, B., Bennett, E.P., Jersild, C. and Clausen, H. Cloning and expression of the histo-blood group Pk UDP-galactose: Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase. Molecular genetic basis of the p phenotype. J. Biol. Chem. 275 (2000) 16723–16729. [DOI] [PMID: 10747952]
3.  Kojima, Y., Fukumoto, S., Furukawa, K., Okajima, T., Wiels, J., Yokoyama, K., Suzuki, Y., Urano, T., Ohta, M. and Furukawa, K. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J. Biol. Chem. 275 (2000) 15152–15156. [DOI] [PMID: 10748143]
[EC 2.4.1.228 created 2002]
 
 
EC 2.4.1.230     
Accepted name: kojibiose phosphorylase
Reaction: 2-α-D-glucosyl-D-glucose + phosphate = D-glucose + β-D-glucose 1-phosphate
Systematic name: 2-α-D-glucosyl-D-glucose:phosphate β-D-glucosyltransferase
Comments: The enzyme from Thermoanaerobacter brockii can act with α-1,2-oligoglucans, such as selaginose, as substrate, but more slowly. The enzyme is inactive when dissaccharides with linkages other than α-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 206566-36-1
References:
1.  Chaen, H., Yamamoto, T., Nishimoto, T., Nakada, T., Fukuda, S., Sugimoto, T., Kurimoto, M. and Tsujisaka, Y. Purification and characterization of a novel phosphorylase, kojibiose phosphorylase, from Thermoanaerobium brockii. J. Appl. Glycosci. 46 (1999) 423–429.
2.  Chaen, H., Nishimoto, T., Nakada, T., Fukuda, S., Kurimoto, M. and Tsujisaka, Y. Enzymatic synthesis of kojioligosaccharides using kojibiose phosphorylase. J. Biosci. Bioeng. 92 (2001) 177–182. [DOI] [PMID: 16233080]
[EC 2.4.1.230 created 2003]
 
 
EC 2.4.1.234     
Accepted name: kaempferol 3-O-galactosyltransferase
Reaction: UDP-α-D-galactose + kaempferol = UDP + kaempferol 3-O-β-D-galactoside
For diagram of kaempferol biosynthesis, click here
Other name(s): F3GalTase; UDP-galactose:kaempferol 3-O-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:kaempferol 3-O-β-D-galactosyltransferase
Comments: Acts on the endogenous flavonols kaempferol and quercetin, to a lesser extent on myricetin and fisetin, and weakly on galangin and isorhamnetin. The reaction can occur equally well in both directions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Miller, K.D., Guyon, V., Evans, J.N., Shuttleworth, W.A. and Taylor, L.P. Purification, cloning, and heterologous expression of a catalytically efficient flavonol 3-O-galactosyltransferase expressed in the male gametophyte of Petunia hybrida. J. Biol. Chem. 274 (1999) 34011–34019. [DOI] [PMID: 10567367]
[EC 2.4.1.234 created 2004]
 
 
EC 2.4.1.241     
Accepted name: digalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): DGD1; DGD2; DGDG synthase (ambiguous); UDP-galactose-dependent DGDG synthase; UDP-galactose-dependent digalactosyldiacylglycerol synthase; UDP-galactose:MGDG galactosyltransferase; UDP-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol 6-α-galactosyltransferase
Comments: Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalysed by EC 2.4.1.46, monogalactosyldiacylglyerol synthase. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids [3]. The enzyme has been localized to the outer side of chloroplast envelope membranes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69913-00-4
References:
1.  Kelly, A.A. and Dörmann, P. DGD2, an Arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J. Biol. Chem. 277 (2002) 1166–1173. [DOI] [PMID: 11696551]
2.  Härtel, H., Dörmann, P. and Benning, C. DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis. Proc. Natl. Acad. Sci. USA 97 (2000) 10649–10654. [DOI] [PMID: 10973486]
3.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC 2.4.1.241 created 2005]
 
 
EC 2.4.1.244     
Accepted name: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-glucosaminyl group = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group
Glossary: N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosamine = N,N′-diacetyllactosediamine
Other name(s): β1,4-N-acetylgalactosaminyltransferase III; β4GalNAc-T3; β1,4-N-acetylgalactosaminyltransferase IV; β4GalNAc-T4; UDP-N-acetyl-D-galactosamine:N-acetyl-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase
Comments: The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-β-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sato, T., Gotoh, M., Kiyohara, K., Kameyama, A., Kubota, T., Kikuchi, N., Ishizuka, Y., Iwasaki, H., Togayachi, A., Kudo, T., Ohkura, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of a novel human β1,4-N-acetylgalactosaminyltransferase, β4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, GalNAc β1-4GlcNAc. J. Biol. Chem. 278 (2003) 47534–47544. [DOI] [PMID: 12966086]
2.  Gotoh, M., Sato, T., Kiyohara, K., Kameyama, A., Kikuchi, N., Kwon, Y.D., Ishizuka, Y., Iwai, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of β1,4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine. FEBS Lett. 562 (2004) 134–140. [DOI] [PMID: 15044014]
[EC 2.4.1.244 created 2006]
 
 
EC 2.4.1.245     
Accepted name: α,α-trehalose synthase
Reaction: NDP-α-D-glucose + D-glucose = α,α-trehalose + NDP
Glossary: NDP = a nucleoside diphosphate
Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase
Systematic name: NDP-α-D-glucose:D-glucose 1-α-D-glucosyltransferase
Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890–47897. [DOI] [PMID: 15364950]
2.  Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429–436. [DOI] [PMID: 15737605]
3.  Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N. and da Costa, M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 190 (2008) 7939–7946. [DOI] [PMID: 18835983]
4.  Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H. and Siebers, B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 190 (2008) 355–369. [DOI] [PMID: 18483808]
[EC 2.4.1.245 created 2008, modified 2013]
 
 
EC 2.4.1.247     
Accepted name: β-D-galactosyl-(1→4)-L-rhamnose phosphorylase
Reaction: β-D-galactosyl-(1→4)-L-rhamnose + phosphate = L-rhamnose + α-D-galactose 1-phosphate
Other name(s): D-galactosyl-β1→4-L-rhamnose phosphorylase; GalRhaP
Systematic name: β-D-galactosyl-(1→4)-L-rhamnose:phosphate 1-α-D-galactosyltransferase
Comments: The enzyme from Clostridium phytofermentans is also active towards towards β-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose in this order. Differs from 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211) in being active towards L-rhamnose and inactive towards N-acetyl hexosamine derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1236189-79-9
References:
1.  Nakajima, M., Nishimoto, M. and Kitaoka, M. Characterization of three β-galactoside phosphorylases from Clostridium phytofermentans: discovery of D-galactosyl-β1→4-L-rhamnose phosphorylase. J. Biol. Chem. 284 (2009) 19220–19227. [DOI] [PMID: 19491100]
[EC 2.4.1.247 created 2009]
 
 
EC 2.4.1.272     
Accepted name: soyasapogenol B glucuronide galactosyltransferase
Reaction: UDP-α-D-galactose + soyasapogenol B 3-O-β-D-glucuronide = UDP + soyasaponin III
For diagram of soyasapogenol biosynthesis, click here
Glossary: soyasaponin III = 3β-(2-O-β-D-galactopyranosyl-β-D-glucopyranosyloxyuronic acid)olean-12-ene-22β,24-diol
Other name(s): UDP-galactose:SBMG-galactosyltransferase; UGT73P2; GmSGT2 (gene name); UDP-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase
Comments: Part of the biosynthetic pathway for soyasaponins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584 (2010) 2258–2264. [DOI] [PMID: 20350545]
[EC 2.4.1.272 created 2011]
 
 
EC 2.4.1.274     
Accepted name: glucosylceramide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of glycolipid biosynthesis, click here
Other name(s): lactosylceramide synthase; uridine diphosphate-galactose:glucosyl ceramide β 1-4 galactosyltransferase; UDP-Gal:glucosylceramide β1→4galactosyltransferase; GalT-2 (misleading); UDP-galactose:β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase
Comments: Involved in the synthesis of several different major classes of glycosphingolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chatterjee, S. and Castiglione, E. UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. Biochim. Biophys. Acta 923 (1987) 136–142. [DOI] [PMID: 3099851]
2.  Trinchera, M., Fiorilli, A. and Ghidoni, R. Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase. Biochemistry 30 (1991) 2719–2724. [PMID: 1900430]
3.  Chatterjee, S., Ghosh, N. and Khurana, S. Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney. J. Biol. Chem. 267 (1992) 7148–7153. [PMID: 1551920]
4.  Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273 (1998) 13570–13577. [DOI] [PMID: 9593693]
5.  Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. cDNA cloning and expression of human lactosylceramide synthase. Biochim. Biophys. Acta 1438 (1999) 301–304. [DOI] [PMID: 10320813]
[EC 2.4.1.274 created 2011]
 
 
EC 2.4.1.275     
Accepted name: neolactotriaosylceramide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of neolactotetraosylceramide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide
Other name(s): β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect)
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331–29340. [DOI] [PMID: 9792633]
[EC 2.4.1.275 created 2011, modified 2013]
 
 
EC 2.4.1.280     
Accepted name: N,N′-diacetylchitobiose phosphorylase
Reaction: N,N′-diacetylchitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-α-D-glucosamine 1-phosphate
Glossary: N,N′-diacetylchitobiose = N-acetyl-D-glucosaminyl-β-(1→4)-N-acetyl-D-glucosamine
Other name(s): chbP (gene name)
Systematic name: N,N′-diacetylchitobiose:phosphate N-acetyl-D-glucosaminyltransferase
Comments: The enzyme is specific for N,N′-diacetylchitobiose and does not phosphorylate other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Park, J.K., Keyhani, N.O. and Roseman, S. Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N′-diacetylchitobiose phosphorylase. J. Biol. Chem. 275 (2000) 33077–33083. [DOI] [PMID: 10913116]
2.  Honda, Y., Kitaoka, M. and Hayashi, K. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio. Biochem. J. 377 (2004) 225–232. [DOI] [PMID: 13678418]
3.  Hidaka, M., Honda, Y., Kitaoka, M., Nirasawa, S., Hayashi, K., Wakagi, T., Shoun, H. and Fushinobu, S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (α/α)6 barrel fold. Structure 12 (2004) 937–947. [DOI] [PMID: 15274915]
[EC 2.4.1.280 created 2012]
 
 
EC 2.4.1.294     
Accepted name: cyanidin 3-O-galactosyltransferase
Reaction: UDP-α-D-galactose + cyanidin = UDP + cyanidin 3-O-β-D-galactoside
For diagram of cyanidin galactoside biosynthesis, click here
Glossary: cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): UDP-galactose:cyanidin galactosyltransferase
Systematic name: UDP-α-D-galactose:cyanidin 3-O-galactosyltransferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397–403. [PMID: 8717136]
[EC 2.4.1.294 created 2013]
 
 
EC 2.4.1.303     
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbbD; WbbD β3Gal-transferase; UDP-Gal:GlcNAc-R β1,3-galactosyltransferase; UDP-Gal:GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase; UDP-Gal:GlcNAc-R galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-β-galactosyltransferase (configuration-inverting)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O7:K1 (VW187). Requires Mn2+. cf. EC 2.4.1.343, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Riley, J.G., Menggad, M., Montoya-Peleaz, P.J., Szarek, W.A., Marolda, C.L., Valvano, M.A., Schutzbach, J.S. and Brockhausen, I. The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal: GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase involved in the biosynthesis of O7-specific lipopolysaccharide. Glycobiology 15 (2005) 605–613. [DOI] [PMID: 15625181]
2.  Brockhausen, I., Riley, J.G., Joynt, M., Yang, X. and Szarek, W.A. Acceptor substrate specificity of UDP-Gal: GlcNAc-R β1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1. Glycoconj. J. 25 (2008) 663–673. [DOI] [PMID: 18536883]
[EC 2.4.1.303 created 2013, modified 2017]
 
 
EC 2.4.1.304     
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→4)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfeD; UDP-Gal:GlcNAc-R 1,4-Gal-transferase; UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,4-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn2+ or to a lesser extent by Mg2+, Ca2+, Ni2+ or Pb2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xu, C., Liu, B., Hu, B., Han, Y., Feng, L., Allingham, J.S., Szarek, W.A., Wang, L. and Brockhausen, I. Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis. J. Bacteriol. 193 (2011) 449–459. [DOI] [PMID: 21057010]
[EC 2.4.1.304 created 2013]
 
 
EC 2.4.1.307      
Deleted entry: UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. Now included in EC 2.4.1.122, glycoprotein-N-acetylgalactosamine β-1,3-galactosyltransferase
[EC 2.4.1.307 created 2013, deleted 2016]
 
 
EC 2.4.1.309     
Accepted name: UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-(α-L-Fuc-(1→2))-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbnI
Systematic name: UDP-α-D-galactose:α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,3-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040–2041. [DOI] [PMID: 15713070]
2.  Yi, W., Zhu, L., Guo, H., Li, M., Li, J. and Wang, P.G. Formation of a new O-polysaccharide in Escherichia coli O86 via disruption of a glycosyltransferase gene involved in O-unit assembly. Carbohydr. Res. 341 (2006) 2254–2260. [DOI] [PMID: 16839526]
3.  Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]
[EC 2.4.1.309 created 2013]
 
 
EC 2.4.1.315     
Accepted name: diglucosyl diacylglycerol synthase (1,6-linking)
Reaction: (1) UDP-α-D-glucose + 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
(2) UDP-α-D-glucose + 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
Other name(s): monoglucosyl diacylglycerol (1→6) glucosyltransferase; MGlcDAG (1→6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name)
Systematic name: UDP-α-D-glucose:1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol 6-glucosyltransferase
Comments: The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose [1]. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo [3]. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1′-sn-glycerol) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jorasch, P., Wolter, F.P., Zahringer, U. and Heinz, E. A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29 (1998) 419–430. [DOI] [PMID: 9720862]
2.  Jorasch, P., Warnecke, D.C., Lindner, B., Zahringer, U. and Heinz, E. Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols. Eur. J. Biochem. 267 (2000) 3770–3783. [DOI] [PMID: 10848996]
3.  Andres, E., Martinez, N. and Planas, A. Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: potential target against mycoplasma infections. J. Biol. Chem. 286 (2011) 35367–35379. [DOI] [PMID: 21835921]
[EC 2.4.1.315 created 2014]
 
 
EC 2.4.1.325     
Accepted name: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Reaction: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)
Systematic name: dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase
Comments: Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509–6516. [DOI] [PMID: 11673418]
[EC 2.4.1.325 created 2014]
 
 
EC 2.4.1.343     
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): wclR (gene name)
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-galactosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O3. Requires a divalent metal ion (Mn2+, Mg2+ or Fe2+). cf. EC 2.4.1.303, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, C., Liu, B., Xu, Y., Utkina, N., Zhou, D., Danilov, L., Torgov, V., Veselovsky, V. and Feng, L. Biochemical characterization of the novel α-1, 3-galactosyltransferase WclR from Escherichia coli O3. Carbohydr. Res. 430 (2016) 36–43. [DOI] [PMID: 27196310]
[EC 2.4.1.343 created 2017]
 
 
EC 2.4.1.344     
Accepted name: type 2 galactoside α-(1,2)-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase (ambiguous); α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); H-gene-encoded β-galactoside α(1→2)fucosyltransferase; β-galactoside α(1→2)fucosyltransferase (ambiguous); GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT1 (gene name); FUT2 (gene name)
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)
Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956–2962. [PMID: 804484]
2.  Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351–353.
3.  Ernst, L.K., Rajan, V.P., Larsen, R.D., Ruff, M.M. and Lowe, J.B. Stable expression of blood group H determinants and GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264 (1989) 3436–3447. [PMID: 2464598]
4.  Larsen, R.D., Ernst, L.K., Nair, R.P. and Lowe, J.B. Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc. Natl. Acad. Sci. USA 87 (1990) 6674–6678. [DOI] [PMID: 2118655]
[EC 2.4.1.344 created 2017]
 
 
EC 2.4.1.375     
Accepted name: rhamnogalacturonan I galactosyltransferase
Reaction: Transfer of a β-galactosyl residue in a β-(1→4) linkage from UDP-α-D-galactose to rhamnosyl residues within the rhamnogalacturonan I backbone.
Glossary: rhamnogalacturonan I backbone = [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n
Systematic name: UDP-α-D-galactose:[rhamnogalacturonan I]-α-L-rhamnosyl β-1,4-galactosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the plant Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan I, one of the components of pectin in plant cell wall. It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 9.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Matsumoto, N., Takenaka, Y., Wachananawat, B., Kajiura, H., Imai, T. and Ishimizu, T. Rhamnogalacturonan I galactosyltransferase: Detection of enzyme activity and its hyperactivation. Plant Physiol. Biochem. 142 (2019) 173–178. [DOI] [PMID: 31299599]
[EC 2.4.1.375 created 2020]
 
 
EC 2.4.1.384     
Accepted name: NDP-glycosyltransferase
Reaction: an NDP-glycose + an acceptor = a glycosylated acceptor + NDP
Other name(s): yjiC (gene name)
Systematic name: NDP-glycose:acceptor glycosyltransferase
Comments: The enzyme, characterized from the bacterium Bacillus licheniformis DSM-13, is an extremely promiscuous glycosyltransferase. It can accept ADP-, GDP-, CDP-, TDP-, or UDP-activated glycose molecules as donors, and can glycosylate a large number of substrates, catalysing O-, N-, or S-glycosylation. While D-glucose is the primarily reported sugar being transferred, the enzyme has been shown to transfer D-galactose, 2-deoxy-D-glucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, L-fucose, L-rhamnose, D-glucuronate, and D-viosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pandey, R.P., Parajuli, P., Koirala, N., Park, J.W. and Sohng, J.K. Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by YjiC. Appl. Environ. Microbiol. 79 (2013) 6833–6838. [DOI] [PMID: 23974133]
2.  Pandey, R.P., Gurung, R.B., Parajuli, P., Koirala, N., Tuoi le, T. and Sohng, J.K. Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids. Carbohydr. Res. 393 (2014) 26–31. [DOI] [PMID: 24893262]
3.  Pandey, R.P., Parajuli, P., Shin, J.Y., Lee, J., Lee, S., Hong, Y.S., Park, Y.I., Kim, J.S. and Sohng, J.K. Enzymatic biosynthesis of novel resveratrol glucoside and glycoside derivatives. Appl. Environ. Microbiol. 80 (2014) 7235–7243. [DOI] [PMID: 25239890]
4.  Parajuli, P., Pandey, R.P., Koirala, N., Yoon, Y.J., Kim, B.G. and Sohng, J.K. Enzymatic synthesis of epothilone A glycosides. AMB Express 4:31 (2014). [DOI] [PMID: 24949266]
5.  Pandey, R.P., Parajuli, P., Gurung, R.B. and Sohng, J.K. Donor specificity of YjiC glycosyltransferase determines the conjugation of cytosolic NDP-sugar in in vivo glycosylation reactions. Enzyme Microb. Technol. 91 (2016) 26–33. [DOI] [PMID: 27444326]
6.  Bashyal, P., Thapa, S.B., Kim, T.S., Pandey, R.P. and Sohng, J.K. Exploring the nucleophilic N- and S-glycosylation capacity of Bacillus licheniformis YjiC enzyme. J. Microbiol. Biotechnol. 30 (2020) 1092–1096. [DOI] [PMID: 32238768]
[EC 2.4.1.384 created 2021]
 
 
EC 2.4.2.41     
Accepted name: xylogalacturonan β-1,3-xylosyltransferase
Reaction: Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a β-1,3-D-xylosyl-D-galactose linkage.
Other name(s): xylogalacturonan xylosyltransferase; XGA xylosyltransferase
Systematic name: UDP-D-xylose:xylogalacturonan 3-β-D-xylosyltransferase
Comments: Involved in plant cell wall synthesis. The enzyme from Arabidopsis thaliana also transfers D-xylose from UDP-D-xylose onto oligogalacturonide acceptors. The enzyme did not show significant activity with UDP-glucose, UDP-galactose, or UDP-N-acetyl-D-glucosamine as sugar donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jensen, J.K., Sorensen, S.O., Harholt, J., Geshi, N., Sakuragi, Y., Moller, I., Zandleven, J., Bernal, A.J., Jensen, N.B., Sorensen, C., Pauly, M., Beldman, G., Willats, W.G. and Scheller, H.V. Identification of a xylogalacturonan xylosyltransferase involved in pectin biosynthesis in Arabidopsis. Plant Cell 20 (2008) 1289–1302. [DOI] [PMID: 18460606]
[EC 2.4.2.41 created 2009]
 
 
EC 2.4.99.4     
Accepted name: β-galactoside α-2,3-sialyltransferase
Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R
Other name(s): CMP-N-acetylneuraminate:β-D-galactoside α-2,3-N-acetylneuraminyl-transferase
Systematic name: CMP-N-acetylneuraminate:β-D-galactoside α-(2→3)-N-acetylneuraminyl-transferase
Comments: The acceptor is Galβ1,3GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid. Lactose can also act as acceptor. May be identical with EC 2.4.99.2 monosialoganglioside sialyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 71124-51-1
References:
1.  Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198]
2.  Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Purification to homogeneity of a β-galactoside α2→3 sialyltransferase and partial purification of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 4434–4442. [PMID: 438196]
[EC 2.4.99.4 created 1984, modified 1986]
 
 
EC 2.4.99.9     
Accepted name: lactosylceramide α-2,3-sialyltransferase
Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis (pathway to GM2), click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): cytidine monophosphoacetylneuraminate-lactosylceramide α2,3- sialyltransferase; CMP-acetylneuraminate-lactosylceramide-sialyltransferase; CMP-acetylneuraminic acid:lactosylceramide sialyltransferase; CMP-sialic acid:lactosylceramide-sialyltransferase; cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase; ganglioside GM3 synthetase; GM3 synthase; GM3 synthetase; SAT 1; CMP-N-acetylneuraminate:lactosylceramide α-2,3-N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide α-(2→3)-N-acetylneuraminyltransferase
Systematic name: CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-(2→3)-N-acetylneuraminyltransferase
Comments: Lactose cannot act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-90-1
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]
2.  Fishman, P.H., Bradley, R.M. and Henneberry, R.C. Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase. Arch. Biochem. Biophys. 172 (1976) 618–626. [DOI] [PMID: 4022]
3.  Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172]
[EC 2.4.99.9 created 1984, modified 1986]
 
 
EC 2.5.1.5     
Accepted name: galactose-6-sulfurylase
Reaction: Eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues
Glossary: porphyran = is a linear polysaccharide produced by the red algae Porphyra. Its backbone is composed of about 30% agarose repeating units (alternating D-galactose and 3,6-anhydro-α-L-galactopyranose residues joined by α-(1→3)- and β-(1→4)-linkages), with the remaining residues being 3-linked β-D-galactopyranose and 4-linked α-L-galactopyranose-6-sulfate.
Other name(s): porphyran sulfatase; galactose-6-sulfatase; galactose 6-sulfatase
Systematic name: D-galactose-6-sulfate:alkyltransferase (cyclizing)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-36-8
References:
1.  Rees, D.A. Enzymic desulphation of porphyran. Biochem. J. 80 (1961) 449–453. [PMID: 13740282]
2.  Rees, D.A. Enzymic synthesis of 3:6-anhydro-L-galactose within porphyran from L-galactose 6-sulphate units. Biochem. J. 81 (1961) 347–352. [PMID: 16748934]
[EC 2.5.1.5 created 1965]
 
 
EC 2.6.1.59     
Accepted name: dTDP-4-amino-4,6-dideoxygalactose transaminase
Reaction: dTDP-4-amino-4,6-dideoxy-α-D-galactose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-α-D-galactose + L-glutamate
For diagram of dTDP-Fuc3NAc, dTDP-Fuc4NAc and dTDP-Fuc3NMe2 biosynthesis, click here
Glossary: dTDP-4-dehydro-6-deoxy-α-D-galactose = dTDP-4-dehydro-6-deoxy-α-D-glucose
Other name(s): thymidine diphosphoaminodideoxygalactose aminotransferase; thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase; WecE; dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase; dTDP-4,6-dideoxy-α-D-galactose:2-oxoglutarate aminotransferase
Systematic name: dTDP-4-amino-4,6-dideoxy-α-D-galactose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72560-97-5
References:
1.  Ohashi, H., Matsuhashi, M. and Matsuhashi, S. Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. IV. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Pasteurella pseudotuberculosis. J. Biol. Chem. 246 (1971) 2325–2330. [PMID: 4928644]
2.  Hwang, B.Y., Lee, H.J., Yang, Y.H., Joo, H.S. and Kim, B.G. Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12. Chem. Biol. 11 (2004) 915–925. [DOI] [PMID: 15271350]
[EC 2.6.1.59 created 1978]
 
 
EC 2.6.1.90     
Accepted name: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose transaminase
Reaction: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-α-D-galactopyranose + L-glutamate
For diagram of dTDP-Fuc3NAc and dTDP-Fuc4NAc biosynthesis, click here
Glossary: dTDP-3-dehydro-6-deoxy-D-galactopyranose = dTDP-6-deoxy-D-xylo-hexopyranos-3-ulose
Other name(s): dTDP-6-deoxy-D-xylohex-3-uloseaminase; FdtB; TDP-3-keto-6-deoxy-D-galactose-3-aminotransferase; RavAMT; TDP-3-keto-6-deoxy-D-galactose 3-aminotransferase; TDP-3-dehydro-6-deoxy-D-galactose 3-aminotransferase
Systematic name: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-α-D-galactose. The reaction occurs in the reverse direction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pfoestl, A., Hofinger, A., Kosma, P. and Messner, P. Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-α-D-galactose in Aneurinibacillus thermoaerophilus L420-91T. J. Biol. Chem. 278 (2003) 26410–26417. [DOI] [PMID: 12740380]
[EC 2.6.1.90 created 2011]
 
 
EC 2.7.1.6     
Accepted name: galactokinase
Reaction: ATP + α-D-galactose = ADP + α-D-galactose 1-phosphate
Other name(s): galactokinase (phosphorylating); ATP:D-galactose-1-phosphotransferase
Systematic name: ATP:α-D-galactose 1-phosphotransferase
Comments: Part of the Leloir pathway for galactose metabolism. The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-α-D-galactosamine [4-6].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-53-9
References:
1.  Cardini, C.E. and Leloir, L.F. Enzymic phosphorylation of galactosamine and galactose. Arch. Biochem. Biophys. 45 (1953) 55–64. [DOI] [PMID: 13058412]
2.  Neufeld, E.F., Feingold, D.S. and Hassid, W.Z. Phosphorylation of D-galactose and L-arabinose by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 906–909. [PMID: 14426659]
3.  Wilkinson, J.F. The pathway of the adaptive fermentation of galactose by yeast. Biochem. J. 44 (1949) 460–467. [PMID: 16748546]
4.  Yang, J., Fu, X., Jia, Q., Shen, J., Biggins, J.B., Jiang, J., Zhao, J., Schmidt, J.J., Wang, P.G. and Thorson, J.S. Studies on the substrate specificity of Escherichia coli galactokinase. Org. Lett. 5 (2003) 2223–2226. [DOI] [PMID: 12816414]
5.  Timson, D.J. and Reece, R.J. Sugar recognition by human galactokinase. BMC Biochem. 4:16 (2003). [DOI] [PMID: 14596685]
6.  Thoden, J.B., Timson, D.J., Reece, R.J. and Holden, H.M. Molecular structure of human galactokinase: implications for type II galactosemia. J. Biol. Chem. 280 (2005) 9662–9670. [DOI] [PMID: 15590630]
[EC 2.7.1.6 created 1961]
 
 
EC 2.7.1.46     
Accepted name: L-arabinokinase
Reaction: ATP + L-arabinose = ADP + β-L-arabinose 1-phosphate
For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here
Other name(s): L-arabinokinase (phosphorylating)
Systematic name: ATP:L-arabinose 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-99-9
References:
1.  Neufeld, E.F., Feingold, D.S. and Hassid, W.Z. Phosphorylation of D-galactose and L-arabinose by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 906–909. [PMID: 14426659]
[EC 2.7.1.46 created 1965]
 
 
EC 2.7.1.52     
Accepted name: fucokinase
Reaction: ATP + L-fucose = ADP + β-L-fucose 1-phosphate
For diagram of GDP-L-fucose and GDP-mannose biosynthesis, click here
Other name(s): fucokinase (phosphorylating); fucose kinase; L-fucose kinase; L-fucokinase; ATP:6-deoxy-L-galactose 1-phosphotransferase; ATP:L-fucose 1-phosphotransferase
Systematic name: ATP:β-L-fucose 1-phosphotransferase
Comments: Requires a divalent cation for activity, with Mg2+ and Fe2+ giving rise to the highest enzyme activity. Forms part of a salvage pathway for reutilization of L-fucose. Can also phosphorylate D-arabinose, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-00-5
References:
1.  Ishihara, H., Massaro, D.J. and Heath, E.C. The metabolism of L-fucose. 3. The enzymatic synthesis of β-L-fucose 1-phosphate. J. Biol. Chem. 243 (1968) 1103–1109. [PMID: 5646161]
2.  Butler, W. and Serif, G.S. Fucokinase, its anomeric specificity and mechanism of phosphate group transfer. Biochim. Biophys. Acta 829 (1985) 238–243. [DOI] [PMID: 2986701]
3.  Park, S.H., Pastuszak, I., Drake, R. and Elbein, A.D. Purification to apparent homogeneity and properties of pig kidney L-fucose kinase. J. Biol. Chem. 273 (1998) 5685–5691. [DOI] [PMID: 9488699]
[EC 2.7.1.52 created 1972, modified 2004]
 
 
EC 2.7.1.58     
Accepted name: 2-dehydro-3-deoxygalactonokinase
Reaction: ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
For diagram of the Entner-Doudoroff pathway, click here
Other name(s): 2-keto-3-deoxygalactonokinase; 2-keto-3-deoxygalactonate kinase (phosphorylating); 2-oxo-3-deoxygalactonate kinase
Systematic name: ATP:2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-05-0
References:
1.  Stouthamer, A.H. Glucose and galactose metabolism in Gluconobacter liquefaciens. Biochim. Biophys. Acta 48 (1961) 484–500.
[EC 2.7.1.58 created 1972]
 
 
EC 2.7.1.69      
Transferred entry: protein-Nπ-phosphohistidine—sugar phosphotransferase, now covered by EC 2.7.1.191 protein-Nπ-phosphohistidine—D-mannose phosphotransferase, EC 2.7.1.192 protein-Nπ-phosphohistidine—N-acetylmuramate phosphotransferase, EC 2.7.1.193 protein-Nπ-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase, EC 2.7.1.194 protein-Nπ-phosphohistidine—L-ascorbate phosphotransferase, EC 2.7.1.195 protein-Nπ-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase, EC 2.7.1.196 protein-Nπ-phosphohistidine—N,N′-diacetylchitobiose phosphotransferase, EC 2.7.1.197 protein-Nπ-phosphohistidine—D-mannitol phosphotransferase, EC 2.7.1.198 protein-Nπ-phosphohistidine—D-sorbitol phosphotransferase, EC 2.7.1.199 protein-Nπ-phosphohistidine—D-glucose phosphotransferase, EC 2.7.1.200 protein-Nπ-phosphohistidine—galactitol phosphotransferase, EC 2.7.1.201 protein-Nπ-phosphohistidine—trehalose phosphotransferase, EC 2.7.1.202 protein-Nπ-phosphohistidine—D-fructose phosphotransferase, EC 2.7.1.203 protein-Nπ-phosphohistidine—D-glucosaminate phosphotransferase, EC 2.7.1.204 protein-Nπ-phosphohistidine—D-galactose phosphotransferase, EC 2.7.1.205 protein-Nπ-phosphohistidine—D-cellobiose phosphotransferase, EC 2.7.1.206 protein-Nπ-phosphohistidine—L-sorbose phosphotransferase, EC 2.7.1.207 protein-Nπ-phosphohistidine—lactose phosphotransferase and EC 2.7.1.208 protein-Nπ-phosphohistidine—maltose phosphotransferase.
[EC 2.7.1.69 created 1972, modified 2000, deleted 2016]
 
 
EC 2.7.1.157     
Accepted name: N-acetylgalactosamine kinase
Reaction: ATP + N-acetyl-α-D-galactosamine = ADP + N-acetyl-α-D-galactosamine 1-phosphate
Other name(s): GALK2; GK2; GalNAc kinase; N-acetylgalactosamine (GalNAc)-1-phosphate kinase; ATP:N-acetyl-D-galactosamine 1-phosphotransferase
Systematic name: ATP:N-acetyl-α-D-galactosamine 1-phosphotransferase
Comments: The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose [2]. Requires Mg2+, Mn2+ or Co2+ for activity, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Pastuszak, I., Drake, R. and Elbein, A.D. Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. J. Biol. Chem. 271 (1999) 20776–20782. [DOI] [PMID: 8702831]
2.  Pastuszak, I., O'Donnell, J. and Elbein, A.D. Identification of the GalNAc kinase amino acid sequence. J. Biol. Chem. 271 (1996) 23653–23656. [DOI] [PMID: 8798585]
3.  Thoden, J.B. and Holden, H.M. The molecular architecture of human N-acetylgalactosamine kinase. J. Biol. Chem. 280 (2005) 32784–32791. [DOI] [PMID: 16006554]
[EC 2.7.1.157 created 2005]
 
 
EC 2.7.1.178     
Accepted name: 2-dehydro-3-deoxyglucono/galactono-kinase
Reaction: (1) ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
(2) ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
For diagram of the Entner-Doudoroff pathway, click here
Other name(s): KDG kinase (ambiguous); KDGK (ambiguous); 2-keto-3-deoxy-D-gluconate kinase (ambiguous)
Systematic name: ATP:2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
Comments: The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency. cf. EC 2.7.1.45, 2-dehydro-3-deoxygluconokinase and EC 2.7.1.58, 2-dehydro-3-deoxygalactonokinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lamble, H.J., Theodossis, A., Milburn, C.C., Taylor, G.L., Bull, S.D., Hough, D.W. and Danson, M.J. Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus. FEBS Lett. 579 (2005) 6865–6869. [DOI] [PMID: 16330030]
2.  Potter, J.A., Kerou, M., Lamble, H.J., Bull, S.D., Hough, D.W., Danson, M.J. and Taylor, G.L. The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase. Acta Crystallogr. D Biol. Crystallogr. 64 (2008) 1283–1287. [DOI] [PMID: 19018105]
3.  Kim, S. and Lee, S.B. Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway. Biosci. Biotechnol. Biochem. 70 (2006) 1308–1316. [DOI] [PMID: 16794308]
[EC 2.7.1.178 created 2013]
 
 
EC 2.7.1.196     
Accepted name: protein-Nπ-phosphohistidine—N,N′-diacetylchitobiose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + N,N′-diacetylchitobiose[side 1] = [protein]-L-histidine + N,N′-diacetylchitobiose 6′-phosphate[side 2]
Other name(s): chbABC (gene names); N,N′-diacetylchitobiose PTS permease; chitobiose PTS permease; EIIcel; EIIchb; Enzyme IIcel; Enzyme IIchb
Systematic name: protein-Nπ-phospho-L-histidine:N,N′-diacetylchitobiose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Keyhani, N.O., Wang, L.X., Lee, Y.C. and Roseman, S. The chitin disaccharide, N,N′-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J. Biol. Chem. 275 (2000) 33084–33090. [DOI] [PMID: 10913117]
2.  Reizer, J., Reizer, A. and Saier, M.H., Jr. The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus. Res. Microbiol. 141 (1990) 1061–1067. [DOI] [PMID: 2092358]
3.  Keyhani, N.O., Boudker, O. and Roseman, S. Isolation and characterization of IIAChb, a soluble protein of the enzyme II complex required for the transport/phosphorylation of N, N′-diacetylchitobiose in Escherichia coli. J. Biol. Chem. 275 (2000) 33091–33101. [DOI] [PMID: 10913118]
4.  Keyhani, N.O., Bacia, K. and Roseman, S. The transport/phosphorylation of N,N′-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) AND IIB(Chb). J. Biol. Chem. 275 (2000) 33102–33109. [DOI] [PMID: 10913119]
[EC 2.7.1.196 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.196]
 
 


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