The Enzyme Database

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EC 2.4.1.139     
Accepted name: maltose synthase
Reaction: 2 α-D-glucose 1-phosphate + H2O = maltose + 2 phosphate
Systematic name: α-D-glucose-1-phosphate:α-D-glucose-1-phosphate 4-α-D-glucosyltransferase (dephosphorylating)
Comments: Neither free phosphate nor maltose 1-phosphate is an intermediate in the reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81669-74-1
References:
1.  Schilling, N. Characterization of maltose biosynthesis from α-D-glucose-1-phosphate in Spinacia oleracea L. Planta 154 (1982) 87–93. [PMID: 24275923]
[EC 2.4.1.139 created 1984]
 
 
EC 2.4.1.140     
Accepted name: alternansucrase
Reaction: Transfers alternately an α-D-glucosyl residue from sucrose to the 6-position and the 3-position of the non-reducing terminal residue of an α-D-glucan, thus producing a glucan having alternating α-(1→6)- and α-(1→3)-linkages
Other name(s): sucrose-1,6(3)-α-glucan 6(3)-α-glucosyltransferase; sucrose:1,6-, 1,3-α-D-glucan 3-α- and 6-α-D-glucosyltransferase; sucrose:1,6(1,3)-α-D-glucan 6(3)-α-D-glucosyltransferase
Systematic name: sucrose:(1→6)[(1→3)]-α-D-glucan 6(3)-α-D-glucosyltransferase
Comments: The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. This enzyme forms both α(1→3) and α(1→6) linkages in approximately equal amounts by alternating the linkage type. cf. EC 2.4.1.125, sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 100630-46-4
References:
1.  Cote, G.L. and Robyt, J.F. Isolation and partial characterization of an extracellular glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that synthesizes an alternating (1→6), (1→3)-α-D-glucan. Carbohydr. Res. 101 (1982) 57–74. [DOI] [PMID: 7060056]
2.  Arguello-Morales, M.A., Remaud-Simeon, M., Pizzut, S., Sarcabal, P., Willemot, R. and Monsan, P. Sequence analysis of the gene encoding alternansucrase, a sucrose glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355. FEMS Microbiol. Lett. 182 (2000) 81–85. [PMID: 10612736]
[EC 2.4.1.140 created 1984, modified 2003]
 
 
EC 2.4.1.141     
Accepted name: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + N-acetyl-α-D-glucosaminyl-diphosphodolichol = UDP + N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = N,N′-diacetylchitobiosyl-diphosphodolichol
Other name(s): UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase; uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase; N,N′-diacetylchitobiosylpyrophosphoryldolichol synthase; UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-glucosaminyl-diphosphodolichol 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 75536-54-8
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245]
2.  Turco, S.J. and Heath, E.C. Glucuronosyl-N-acetylglucosaminyl pyrophosphoryldolichol. Formation in SV40-transformed human lung fibroblasts and biosynthesis in rat lung microsomal preparations. J. Biol. Chem. 252 (1977) 2918–2928. [PMID: 192724]
[EC 2.4.1.141 created 1984]
 
 
EC 2.4.1.142     
Accepted name: chitobiosyldiphosphodolichol β-mannosyltransferase
Reaction: GDP-α-D-mannose + N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = GDP + β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = N,N′-diacetylchitobiosyl-diphosphodolichol
Other name(s): guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose:chitobiosyldiphosphodolichol β-D-mannosyltransferase
Systematic name: GDP-α-D-mannose:N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol 4-β-D-mannosyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83380-85-2
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245]
2.  Takahashi, T., Honda, R. and Nishikawa, Y. Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1. Glycobiology 10 (2000) 321–327. [DOI] [PMID: 10704531]
[EC 2.4.1.142 created 1984, modified 2001]
 
 
EC 2.4.1.143     
Accepted name: α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): MGAT2 (gene name); N-acetylglucosaminyltransferase II; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mannoside α1→6-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-1,6-mannosylglycoprotein β-1-2-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-D-mannoside β1-2-acetylglucosaminyltransferase; UDP-GlcNAc:mannoside α1-6 acetylglucosaminyltransferase; α-1,6-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTII; GlcNAc-T II; UDP-N-acetyl-D-glucosamine:6-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its activity initiates the synthesis of the second antenna of di-antennary complex N-glycans. While the natural substrate (produced by EC 3.2.1.114, mannosyl-oligosaccharide 1,3-1,6-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→6)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→3)]-β-D-Man-R.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105913-04-0
References:
1.  Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity. J. Biol. Chem. 255 (1980) 4885–4893. [PMID: 6445358]
2.  Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa. Biochemistry 20 (1981) 967–976. [PMID: 6452163]
3.  Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. The nonidentity of porcine N-acetylglucosaminyltransferases I and II. J. Biol. Chem. 256 (1981) 11477–11482. [PMID: 6457827]
4.  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]
5.  Bendiak, B. and Schachter, H. Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:α-D-mannoside β-1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem. 262 (1987) 5784–5790. [PMID: 2952645]
6.  Bendiak, B. and Schacter, H. Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:α-D-mannoside β1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem. 262 (1987) 5775–5783. [PMID: 2952644]
7.  Tan, J., D'Agostaro, A.F., Bendiak, B., Reck, F., Sarkar, M., Squire, J.A., Leong, P. and Schachter, H. The human UDP-N-acetylglucosamine: α-6-D-mannoside-β-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein. Eur. J. Biochem. 231 (1995) 317–328. [DOI] [PMID: 7635144]
[EC 2.4.1.143 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.4.1.144     
Accepted name: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-[β-D-GlcNAc-(1→4)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): N-acetylglucosaminyltransferase III; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase III; β-1,4-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIII; GlcNAc-T III; MGAT3 (gene name); UDP-N-acetyl-D-glucosamine:β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. The residue added by the enzyme at position 4 of the β-linked mannose of the trimannosyl core of N-glycans is known as a bisecting GlcNAc. Unlike GlcNAc residues added to other positions, it is not extended or modified. In addition, its presence prevents the action of other branching enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145) and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-T III leads to a decrease in highly branched N-glycan structures.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83744-93-8
References:
1.  Narasimhan, S. Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide β4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β1-4 linkage to the β-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J. Biol. Chem. 257 (1982) 10235–10242. [PMID: 6213618]
2.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
3.  Brockhausen, I., Carver, J.P. and Schachter, H. Control of glycoprotein synthesis. The use of oligosaccharide substrates and HPLC to study the sequential pathway for N-acetylglucosaminyltransferases I, II, III, IV, V, and VI in the biosynthesis of highly branched N-glycans by hen oviduct membranes. Biochem. Cell Biol. 66 (1988) 1134–1151. [PMID: 2975180]
4.  Nishikawa, A., Ihara, Y., Hatakeyama, M., Kangawa, K. and Taniguchi, N. Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: β-D-mannoside β-1,4N-acetylglucosaminyltransferase III from rat kidney. J. Biol. Chem. 267 (1992) 18199–18204. [PMID: 1325461]
5.  Ihara, Y., Nishikawa, A., Tohma, T., Soejima, H., Niikawa, N. and Taniguchi, N. cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J. Biochem. 113 (1993) 692–698. [PMID: 8370666]
[EC 2.4.1.144 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.4.1.145     
Accepted name: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): N-acetylglucosaminyltransferase IV; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; β-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase IV; α-1,3-mannosylglycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIV; UDP-N-acetyl-D-glucosamine:3-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86498-16-0
References:
1.  Gleeson, P.A. and Schachter, H. Control of glycoprotein synthesis. J. Biol. Chem. 258 (1983) 6162–6173. [PMID: 6222042]
2.  Oguri, S., Minowa, M.T., Ihara, Y., Taniguchi, N., Ikenaga, H. and Takeuchi, M. Purification and characterization of UDP-N-acetylglucosamine: α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase-IV) from bovine small intestine. J. Biol. Chem. 272 (1997) 22721–22727. [DOI] [PMID: 9278430]
3.  Minowa, M.T., Oguri, S., Yoshida, A., Hara, T., Iwamatsu, A., Ikenaga, H. and Takeuchi, M. cDNA cloning and expression of bovine UDP-N-acetylglucosamine: α1, 3-D-mannoside β1,4-N-acetylglucosaminyltransferase IV. J. Biol. Chem. 273 (1998) 11556–11562. [DOI] [PMID: 9565571]
4.  Yoshida, A., Minowa, M.T., Takamatsu, S., Hara, T., Oguri, S., Ikenaga, H. and Takeuchi, M. Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine: α1,3-d-mannoside β1, 4-N-acetylglucosaminyltransferase. Glycobiology 9 (1999) 303–310. [DOI] [PMID: 10024668]
5.  Yoshida, A., Minowa, M.T., Takamatsu, S., Hara, T., Ikenaga, H. and Takeuchi, M. A novel second isoenzyme of the human UDP-N-acetylglucosamine:α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment. Glycoconj. J. 15 (1998) 1115–1123. [PMID: 10372966]
6.  Takamatsu, S., Antonopoulos, A., Ohtsubo, K., Ditto, D., Chiba, Y., Le, D.T., Morris, H.R., Haslam, S.M., Dell, A., Marth, J.D. and Taniguchi, N. Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice. Glycobiology 20 (2010) 485–497. [DOI] [PMID: 20015870]
[EC 2.4.1.145 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
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 2.4.1.147     
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + O3-[N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] = UDP + O3-[N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein]
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase; mucin core 3 β3-GlcNAc-transferase; Core 3β-GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase (incorrect)
Systematic name: UDP-N-acetyl-α-D-glucosamine:O3-[N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] 3-β-N-acetyl-D-glucosaminyltransferase
Comments: The product of the enzyme is known as core 3, one of the eight core structures of mucin-type O-glycans. O-Linked glycans are polysaccharides or oligosaccharides that are linked to a protein via the oxygen atom in the side chain of an L-serine or L-threonine residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87927-96-6
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
2.  Brockhausen, I., Matta, K.L., Orr, J. and Schachter, H. Mucin synthesis. UDP-GlcNAc:GalNAc-R β 3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc β 1-3GalNAc-R (GlcNAc to GalNAc) β 6-N-acetylglucosaminyltransferase from pig and rat colon mucosa. Biochemistry 24 (1985) 1866–1874. [PMID: 3160388]
3.  Vavasseur, F., Yang, J.M., Dole, K., Paulsen, H. and Brockhausen, I. Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-R β 3-N-acetyl-glucosaminyltransferase activity from colonic mucosal tissues and lack of the activity in human cancer cell lines. Glycobiology 5 (1995) 351–357. [DOI] [PMID: 7655172]
[EC 2.4.1.147 created 1984, modified 2015]
 
 
EC 2.4.1.148     
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→3)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-mucin β(1→6)-acetylglucosaminyltransferase B; core 4 β6-GalNAc-transferase; core 6β-GalNAc-transferase B; UDP-N-acetyl-D-glucosamine:O-oligosaccharide-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of N-acetyl-β-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R 6-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
[EC 2.4.1.148 created 1984]
 
 
EC 2.4.1.149     
Accepted name: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-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, PDB, 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 2.4.1.150     
Accepted name: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Glossary: β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = type 2 precursor disaccharide
Other name(s): GCNT2 (gene name); GCNT3 (gene name); IGnT; I-branching β1,6-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: The enzyme acts on poly-N-acetyllactosamine [glycan chains of β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine units connected by β(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by β(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
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.  Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658]
4.  Bierhuizen, M.F., Maemura, K., Kudo, S. and Fukuda, M. Genomic organization of core 2 and I branching β-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the β-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology 5 (1995) 417–425. [DOI] [PMID: 7579796]
5.  Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O., Clausen, H., Fukuda, M.N. and Fukuda, M. Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274 (1999) 9296–9304. [DOI] [PMID: 10092606]
6.  Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862]
[EC 2.4.1.150 created 1984 (EC 2.4.1.164 created 1989, incorporated 2016), modified 2017]
 
 
EC 2.4.1.151      
Transferred entry: N-acetyllactosaminide α-1,3-galactosyltransferase. Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase
[EC 2.4.1.151 created 1984, deleted 2002]
 
 
EC 2.4.1.152     
Accepted name: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = GDP + β-D-galactosyl-(1→4)-[α-L-fucosyl-(1→3)]-N-acetyl-D-glucosaminyl-R
For diagram of fucosylneolactotetraosylceramide biosynthesis, click here
Other name(s): Lewis-negative α-3-fucosyltransferase; plasma α-3-fucosyltransferase; guanosine diphosphofucose-glucoside α1→3-fucosyltransferase; galactoside 3-fucosyltransferase; GDP-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase; GDP-β-L-fucose:(1→4)-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase (configuration-inverting)
Comments: Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39279-34-0
References:
1.  Johnson, P.H., Yates, A.D. and Watkins, W.M. Human salivary fucosyltransferase: evidence for two distinct α-3-L-fucosyltransferase activities one of which is associated with the Lewis blood Le gene. Biochem. Biophys. Res. Commun. 100 (1981) 1611–1618. [DOI] [PMID: 7295318]
2.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
3.  Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893–21900. [DOI] [PMID: 12676935]
[EC 2.4.1.152 created 1984, modified 2002, modified 2019]
 
 
EC 2.4.1.153     
Accepted name: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UDP + dolichyl N-acetyl-α-D-glucosaminyl phosphate
Other name(s): aglK (gene name); dolichyl-phosphate α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Comments: The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism. The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15, UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-73-5
References:
1.  Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367–373. [DOI] [PMID: 23624439]
[EC 2.4.1.153 created 1984, modified 2015]
 
 
EC 2.4.1.154      
Deleted entry: globotriosylceramide β-1,6-N-acetylgalactosaminyl-transferase. The enzyme is identical to EC 2.4.1.79, globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase. The reference cited referred to a 1→3 linkage and not to a 1→6 linkage, as indicated in the enzyme entry
[EC 2.4.1.154 created 1986, deleted 2006]
 
 
EC 2.4.1.155     
Accepted name: α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Other name(s): MGAT5 (gene name); N-acetylglucosaminyltransferase V; α-mannoside β-1,6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-mannoside β1→6-acetylglucosaminyltransferase; UDP-N-acetylglucosamine:α-mannoside-β1,6 N-acetylglucosaminyltransferase; α-1,3(6)-mannosylglycoprotein β-1,6-N-acetylglucosaminyltransferase; GnTV; GlcNAc-T V; UDP-N-acetyl-D-glucosamine:6-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires Mg2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. It catalyses the addition of N-acetylglucosamine in β 1-6 linkage to the α-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83588-90-3
References:
1.  Cummings, R.D., Trowbridge, I.S. and Kornfeld, S. A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: α-D-mannoside β1,6 N-acetylglucosaminyltransferase. J. Biol. Chem. 257 (1982) 13421–13427. [PMID: 6216250]
2.  Hindsgaul, O., Tahir, S.H., Srivastava, O.P. and Pierce, M. The trisaccharide β-D-GlcpNAc-(1→2)-α-D-Manp-(1→6)-β-D-Manp, as its 8-methoxycarbonyloctyl glycoside, is an acceptor selective for N-acetylglucosaminyltransferase V. Carbohydr. Res. 173 (1988) 263–272. [DOI] [PMID: 2834054]
3.  Shoreibah, M.G., Hindsgaul, O. and Pierce, M. Purification and characterization of rat kidney UDP-N-acetylglucosamine: α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 2920–2927. [PMID: 1531335]
4.  Gu, J., Nishikawa, A., Tsuruoka, N., Ohno, M., Yamaguchi, N., Kangawa, K. and Taniguchi, N. Purification and characterization of UDP-N-acetylglucosamine: α-6-D-mannoside β 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. J. Biochem. 113 (1993) 614–619. [PMID: 8393437]
5.  Park, C., Jin, U.H., Lee, Y.C., Cho, T.J. and Kim, C.H. Characterization of UDP-N-acetylglucosamine:α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B. Arch. Biochem. Biophys. 367 (1999) 281–288. [PMID: 10395745]
6.  Saito, T., Miyoshi, E., Sasai, K., Nakano, N., Eguchi, H., Honke, K. and Taniguchi, N. A secreted type of β 1,6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity. J. Biol. Chem. 277 (2002) 17002–17008. [PMID: 11872751]
[EC 2.4.1.155 created 1986, modified 2001, modified 2018]
 
 
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 2.4.1.157      
Transferred entry: 1,2-diacylglycerol 3-glucosyltransferase. Now classified as EC 2.4.1.336, monoglucosyldiacylglycerol synthase, and EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase
[EC 2.4.1.157 created 1986, deleted 2015]
 
 
EC 2.4.1.158     
Accepted name: 13-hydroxydocosanoate 13-β-glucosyltransferase
Reaction: UDP-glucose + 13-hydroxydocosanoate = UDP + 13-β-D-glucosyloxydocosanoate
Other name(s): 13-glucosyloxydocosanoate 2′-β-glucosyltransferase; UDP-glucose:13-hydroxydocosanoic acid glucosyltransferase; uridine diphosphoglucose-hydroxydocosanoate glucosyltransferase; UDP-glucose-13-hydroxydocosanoate glucosyltransferase
Systematic name: UDP-glucose:13-hydroxydocosanoate 13-β-D-glucosyltransferase
Comments: 13-β-D-Glucosyloxydocosanoate can also act as acceptor, leading to the formation by Candida bogoriensis of the extracellular glycolipid, hydroxydocosanoate sophoroside diacetate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 70457-13-5
References:
1.  Breithaupt, T.B. and Light, R.J. Affinity chromatography and further characterization of the glucosyltransferases involved in hydroxydocosanoic acid sophoroside production in Candida bogoriensis. J. Biol. Chem. 257 (1982) 9622–9628. [PMID: 6213610]
[EC 2.4.1.158 created 1986]
 
 
EC 2.4.1.159     
Accepted name: flavonol-3-O-glucoside L-rhamnosyltransferase
Reaction: UDP-β-L-rhamnose + a flavonol 3-O-β-D-glucoside = UDP + a flavonol 3-O-[α-L-rhamnosyl-(1→6)-β-D-glucoside]
For diagram of quercetin 3-O-Glycoside derivatives biosynthesis, click here
Glossary: UDP-β-L-rhamnose = UDP-6-deoxy-β-L-mannose
Other name(s): uridine diphosphorhamnose-flavonol 3-O-glucoside rhamnosyltransferase; UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase; UDP-L-rhamnose:flavonol-3-O-D-glucoside 6′′-O-L-rhamnosyltransferase
Systematic name: UDP-β-L-rhamnose:flavonol-3-O-β-D-glucoside 6′′-O-L-rhamnosyltransferase (configuration-inverting)
Comments: A configuration-inverting rhamnosyltransferase that converts flavonol 3-O-glucosides to 3-O-rutinosides. Also acts, more slowly, on rutin, quercetin 3-O-galactoside and flavonol 3-O-rhamnosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83380-89-6
References:
1.  Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587–599.
2.  Jones, P., Messner, B., Nakajima, J., Schaffner, A.R. and Saito, K. UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in Arabidopsis thaliana. J. Biol. Chem. 278 (2003) 43910–43918. [DOI] [PMID: 12900416]
[EC 2.4.1.159 created 1986, modified 2015]
 
 
EC 2.4.1.160     
Accepted name: pyridoxine 5′-O-β-D-glucosyltransferase
Reaction: UDP-glucose + pyridoxine = UDP + 5′-O-β-D-glucosylpyridoxine
Other name(s): UDP-glucose:pyridoxine 5′-O-β-glucosyltransferase; uridine diphosphoglucose-pyridoxine 5′-β-glucosyltransferase; UDP-glucose-pyridoxine glucosyltransferase
Systematic name: UDP-glucose:pyridoxine 5′-O-β-D-glucosyltransferase
Comments: 4′-Deoxypyridoxine and pyridoxamine can also act as acceptors, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83744-97-2
References:
1.  Tadera, K., Fumio, Y. and Kobayashi, A. Specificity of a particulate glucosyltransferase in seedlings of Pisum sativum L. which catalyzes the formation of 5′-O-(β-D-glucopyranosyl)pyridoxine. J. Nutr. Sci. Vitaminol. 28 (1982) 359–366. [PMID: 6217302]
[EC 2.4.1.160 created 1986]
 
 
EC 2.4.1.161     
Accepted name: oligosaccharide 4-α-D-glucosyltransferase
Reaction: Transfers the non-reducing terminal α-D-glucose residue from a (1→4)-α-D-glucan to the 4-position of a free glucose or of a glucosyl residue at the non-reducing terminus of a (1→4)-α-D-glucan, thus bringing about the rearrangement of oligosaccharides
Other name(s): amylase III; 1,4-α-glucan:1,4-α-glucan 4-α-glucosyltransferase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glucosyltransferase; α-1,4-transglucosylase
Systematic name: (1→4)-α-D-glucan:(1→4)-α-D-glucan 4-α-D-glucosyltransferase
Comments: The enzyme acts on amylose, amylopectin, glycogen and maltooligosaccharides. No detectable free glucose is formed, indicating the enzyme does not act as a hydrolase. The enzyme from the bacterium Cellvibrio japonicus has the highest activity with maltotriose as a donor, and also accepts maltose [3], while the enzyme from amoeba does not accept maltose [1,2]. Oligosaccharides with 1→6 linkages cannot function as donors, but can act as acceptors [3]. Unlike EC 2.4.1.25, 4-α-glucanotransferase, this enzyme can transfer only a single glucosyl residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9000-92-4
References:
1.  Nebinger, P. Separation and characterization of four different amylases of Entamoeba histolytica. I. Purification and properties. Biol. Chem. Hoppe-Seyler 367 (1986) 161–167. [PMID: 2423097]
2.  Nebinger, P. Separation and characterization of four different amylases of Entamoeba histolytica. II. Characterization of amylases. Biol. Chem. Hoppe-Seyler 367 (1986) 169–176. [PMID: 2423098]
3.  Larsbrink, J., Izumi, A., Hemsworth, G.R., Davies, G.J. and Brumer, H. Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31. J. Biol. Chem. 287 (2012) 43288–43299. [DOI] [PMID: 23132856]
[EC 2.4.1.161 created 1989, modified 2013]
 
 
EC 2.4.1.162     
Accepted name: aldose β-D-fructosyltransferase
Reaction: α-D-aldosyl1 β-D-fructoside + D-aldose2 = D-aldose1 + α-D-aldosyl2 β-D-fructoside
Systematic name: α-D-aldosyl-β-D-fructoside:aldose 1-β-D-fructosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-67-8
References:
1.  Cheetham, P.S.J., Hacking, A.J., Vlitos, M. Synthesis of novel disaccharides by a newly isolated fructosyl transferase from Bacillus subtilis. Enzyme Microb. Technol. 11 (1989) 212–219.
[EC 2.4.1.162 created 1989, modified 1999]
 
 
EC 2.4.1.163      
Transferred entry: β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase, now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
[EC 2.4.1.163 created 1989, deleted 2016]
 
 
EC 2.4.1.164      
Transferred entry: galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,6-N-acetylglucosaminyltransferase, now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
[EC 2.4.1.164 created 1989, deleted 2016]
 
 
EC 2.4.1.165     
Accepted name: N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Other name(s): uridine diphosphoacetylgalactosamine-acetylneuraminyl(α2→3)galactosyl(β1→4)glucosyl β1→4-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-2,3-α-D-galactosyl-1,4-β-D-glucosylceramide β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2→3)-α-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2→3)-α-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-N-acetylgalactosaminyltransferase
Comments: Requires Mn2+. Only substances containing sialic acid residues can act as acceptors; bovine fetuin is the best acceptor tested.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109136-50-7
References:
1.  Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917]
2.  Piller, F., Blanchard, D., Huet, M. and Cartron, J.-P. Identification of a α-NeuAc-(2-3)-β-D-galactopyranosyl N-acetyl-β-D-galactosaminyltransferase in human kidney. Carbohydr. Res. 149 (1986) 171–184. [DOI] [PMID: 2425965]
3.  Takeya, A., Hosomi, O. and Kogure, T. Identification and characterization of UDP-GalNAc: NeuAc α2-3Gal β1-4Glc(NAc) β1-4(GalNAc to Gal)N-acetylgalactosaminyltransferase in human blood plasma. J. Biochem. (Tokyo) 101 (1987) 251–259. [PMID: 3106337]
[EC 2.4.1.165 created 1989]
 
 
EC 2.4.1.166     
Accepted name: raffinose—raffinose α-galactosyltransferase
Reaction: 2 raffinose = 1F-α-D-galactosylraffinose + sucrose
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): raffinose (raffinose donor) galactosyltransferase; raffinose:raffinose α-galactosyltransferase; raffinose—raffinose α-galactotransferase
Systematic name: raffinose:raffinose α-D-galactosyltransferase
Comments: The 3F position of raffinose can also act as galactosyl acceptor; the enzyme is involved in the accumulation of the tetrasaccharides lychnose and isolychnose in the leaves of Cerastium arvense and other plants of the family Caryophyllaceae during late autumn.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93389-38-9
References:
1.  Hopf, H., Gruber, G., Zinn, A. and Kandler, O. Physiology and biosynthesis of lychnose in Cerastium arvense. Planta 162 (1984) 283–288. [PMID: 24253101]
[EC 2.4.1.166 created 1989]
 
 
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 2.4.1.168     
Accepted name: xyloglucan 4-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a β-(1→4)-D-glucosyl-D-glucose linkage
Other name(s): uridine diphosphoglucose-xyloglucan 4β-glucosyltransferase; xyloglucan 4β-D-glucosyltransferase; xyloglucan glucosyltransferase; UDP-glucose:xyloglucan 1,4-β-D-glucosyltransferase
Systematic name: UDP-glucose:xyloglucan 4-β-D-glucosyltransferase
Comments: In association with EC 2.4.2.39 (xyloglucan 6-xylosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are essential for this synthesis. Not identical with EC 2.4.1.12 cellulose synthase (UDP-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80237-91-8
References:
1.  Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-β-D-glucosyltransferase and 6-α-D-xylosyltransferase. J. Biol. Chem. 256 (1981) 11117–11122. [PMID: 6457048]
2.  Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells - synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant Cell Physiol. 22 (1981) 517–523.
[EC 2.4.1.168 created 1989]
 
 
EC 2.4.1.169      
Transferred entry: xyloglucan 6-xylosyltransferase. Now EC 2.4.2.39, xyloglucan 6-xylosyltransferase
[EC 2.4.1.169 created 1989, deleted 2003]
 
 
EC 2.4.1.170     
Accepted name: isoflavone 7-O-glucosyltransferase
Reaction: UDP-glucose + an isoflavone = UDP + an isoflavone 7-O-β-D-glucoside
For diagram of the biosynthesis of biochanin A, click here and for diagram of the biosynthesis of formononetin and derivatives, click here
Other name(s): uridine diphosphoglucose-isoflavone 7-O-glucosyltransferase; UDPglucose-favonoid 7-O-glucosyltransferase; UDPglucose:isoflavone 7-O-glucosyltransferase
Systematic name: UDP-glucose:isoflavone 7-O-β-D-glucosyltransferase
Comments: The 4′-methoxy isoflavones biochanin A and formononetin and, more slowly, the 4′-hydroxyisoflavones genistein and daidzein, can act as acceptors. The enzyme does not act on isoflavanones, flavones, flavanones, flavanols or coumarins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97089-62-8
References:
1.  Köster, J. and Barz, W. UDP-glucose:isoflavone 7-O-glucosyltransferase from roots of chick pea (Cicer arietinum L.). Arch. Biochem. Biophys. 212 (1981) 98–104. [DOI] [PMID: 6458246]
[EC 2.4.1.170 created 1989]
 
 
EC 2.4.1.171     
Accepted name: methyl-ONN-azoxymethanol β-D-glucosyltransferase
Reaction: UDP-glucose + methyl-ONN-azoxymethanol = UDP + cycasin
Glossary: methyl-ONN-azoxymethanol = CH3-N(O)=N-CH2OH
Other name(s): cycasin synthase; uridine diphosphoglucose-methylazoxymethanol glucosyltransferase; UDP-glucose-methylazoxymethanol glucosyltransferase
Systematic name: UDP-glucose:methyl-ONN-azoxymethanol β-D-glucosyltransferase
Comments: Brings about the biosynthesis of the toxic substance cycasin in the leaves of Japanese cycad, Cycas revoluta.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99283-65-5
References:
1.  Tadera, K., Yagi, F., Arima, M. and Kobayashi, A. Formation of cycasin from methylazoxymethanol by UDP-glucosyltransferase from leaves of Japanese cycad. Agric. Biol. Chem. 49 (1985) 2827–2828.
[EC 2.4.1.171 created 1989]
 
 
EC 2.4.1.172     
Accepted name: salicyl-alcohol β-D-glucosyltransferase
Reaction: UDP-glucose + salicyl alcohol = UDP + salicin
Other name(s): uridine diphosphoglucose-salicyl alcohol 2-glucosyltransferase; UDPglucose:salicyl alcohol phenyl-glucosyltransferase
Systematic name: UDP-glucose:salicyl-alcohol β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89400-32-8
References:
1.  Mizukami, H., Terao, T. and Ohashi, H. Partial-purification and characterization of UDP-glucose-salicyl alcohol glucosyltransferase from Gardeni jasminoides cell-cultures. Planta Med. 1985 (1985) 104–107.
[EC 2.4.1.172 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, PDB, 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 2.4.1.174     
Accepted name: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of chondroitin biosynthesis (later stages), click here
Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
Other name(s): N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I; UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1→3)-β-D-galactosyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting)
Comments: Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96189-39-8
References:
1.  Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754]
2.  Uyama, T., Kitagawa, H., Tamura, J.-i. and Sugahara, K. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277 (2002) 8841–8846. [DOI] [PMID: 11788602]
[EC 2.4.1.174 created 1989, modified 2002]
 
 
EC 2.4.1.175     
Accepted name: glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase
Reaction: (1) UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
(2) UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n+1-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of chondroitin biosynthesis (later stages), click here
Other name(s): N-acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-β-D-galactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; chondroitin synthase; glucuronyl-N-acetylgalactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:β-D-glucuronosyl-(1→3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-α-D-galactosamine:β-D-glucuronosyl-(1→3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of chondroitin sulfate. The human form of this enzyme is a bifunctional glycosyltransferase, which also has the 3-β-glucuronosyltransferase (EC 2.4.1.226, N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase) activity required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 96189-40-1
References:
1.  Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754]
2.  Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [DOI] [PMID: 11514575]
3.  DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [DOI] [PMID: 10818104]
4.  Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [DOI] [PMID: 11943778]
[EC 2.4.1.175 created 1989, modified 2002]
 
 
EC 2.4.1.176     
Accepted name: gibberellin β-D-glucosyltransferase
Reaction: UDP-glucose + gibberellin = UDP + gibberellin 2-O-β-D-glucoside
Other name(s): uridine diphosphoglucose-gibberellate 7-glucosyltransferase; uridine diphosphoglucose-gibberellate 3-O-glucosyltransferase
Systematic name: UDP-glucose:gibberellin 2-O-β-D-glucosyltransferase
Comments: Acts on the plant hormone gibberellin GA3 and related compounds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99775-14-1, 94489-97-1
References:
1.  Sembdner, G., Knoefel, H.D., Schwarzkopf, E. and Liebisch, H.W. In vitro glucosylation of gibberellins. Biol. Plant. 27 (1985) 231–236.
[EC 2.4.1.176 created 1989]
 
 
EC 2.4.1.177     
Accepted name: cinnamate β-D-glucosyltransferase
Reaction: UDP-glucose + trans-cinnamate = UDP + trans-cinnamoyl β-D-glucoside
Other name(s): uridine diphosphoglucose-cinnamate glucosyltransferase; UDPG:t-cinnamate glucosyltransferase
Systematic name: UDP-glucose:trans-cinnamate β-D-glucosyltransferase
Comments: 4-Coumarate, 2-coumarate, benzoate, feruloate and caffeate can also act as acceptors, but more slowly. Involved in the biosynthesis of chlorogenic acid in the root of the sweet potato, Ipomoea batatas.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83744-95-0
References:
1.  Shimizu, T. and Kojima, M. Partial purification and characterization of UDPG:t-cinnamate glucosyltransferase in the root of sweet potato, Ipomoea batatas Lam. J. Biochem. (Tokyo) 95 (1984) 205–213. [PMID: 6231280]
[EC 2.4.1.177 created 1989]
 
 
EC 2.4.1.178     
Accepted name: hydroxymandelonitrile glucosyltransferase
Reaction: UDP-glucose + 4-hydroxymandelonitrile = UDP + taxiphyllin
Other name(s): cyanohydrin glucosyltransferase; uridine diphosphoglucose-cyanohydrin glucosyltransferase
Systematic name: UDP-glucose:4-hydroxymandelonitrile glucosyltransferase
Comments: 3,4-Dihydroxymandelonitrile can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89287-39-8
References:
1.  Hösel, W. and Schiel, O. Biosynthesis of cyanogenic glucosides: in vitro analysis of the glucosylation step. Arch. Biochem. Biophys. 229 (1984) 177–186. [DOI] [PMID: 6230992]
2.  Poulton, J.E. and Shin, S.-I. Prunasin biosynthesis by cell-free-extracts from black cherry (Prunus serotina Ehrh) fruits and leaves. Z. Naturforsch. C: Biosci. 38 (1983) 369–374.
[EC 2.4.1.178 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 2.4.1.180     
Accepted name: lipopolysaccharide N-acetylmannosaminouronosyltransferase
Reaction: UDP-N-acetyl-α-D-mannosaminouronate + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate
Other name(s): ManNAcA transferase; uridine diphosphoacetylmannosaminuronate-acetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminuronosyltransferase; UDP-N-acetyl-β-D-mannosaminouronate:lipid I N-acetyl-β-D-mannosaminouronosyltransferase (incorrect)
Systematic name: UDP-N-acetyl-α-D-mannosaminouronate:lipid I N-acetyl-α-D-mannosaminouronosyltransferase
Comments: Involved in the biosynthesis of common antigen in Enterobacteriaceae.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-30-1
References:
1.  Barr, K., Ward, S., Meier-Dieter, U., Mayer, H. and Rick, P.D. Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis. J. Bacteriol. 170 (1988) 228–233. [DOI] [PMID: 3275612]
[EC 2.4.1.180 created 1990, modified 2011]
 
 
EC 2.4.1.181     
Accepted name: hydroxyanthraquinone glucosyltransferase
Reaction: UDP-glucose + an hydroxyanthraquinone = UDP + a glucosyloxyanthraquinone
Other name(s): uridine diphosphoglucose-anthraquinone glucosyltransferase; anthraquinone-specific glucosyltransferase
Systematic name: UDP-glucose:hydroxyanthraquinone O-glucosyltransferase
Comments: A range of anthraquinones and some flavones can act as acceptors; best substrates are emodin, anthrapurpurin, quinizarin, 2,6-dihydroanthraquinone and 1,8-dihydroxyanthraquinone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112198-78-4
References:
1.  Khouri, H.E. and Ibrahim, R.K. Purification and some properties of five anthraquinone-specific glucosyltransferases from Cinchona succiruba cell suspension culture. Phytochemistry 26 (1987) 2531–2535.
[EC 2.4.1.181 created 1990]
 
 
EC 2.4.1.182     
Accepted name: lipid-A-disaccharide synthase
Reaction: a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + a lipid X = UDP + a lipid A disaccharide
For diagram of lipid IVA biosynthesis, click here
Glossary: a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine
a lipid A disaccharide = a 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
Other name(s): lpxB (gene name); UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis-(3-hydroxytetradecanoyl)-β-D-glucosaminyl-1-phosphate 2,3-bis(3-hydroxytetradecanoyl)-glucosaminyltransferase (incorrect)
Systematic name: UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine:2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosaminyltransferase
Comments: Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide 4′-kinase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-81-0
References:
1.  Ray, B.L., Painter, G. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A disaccharides from monosaccharide precursors in extracts of Escherichia coli. J. Biol. Chem. 259 (1984) 4852–4859. [PMID: 6370995]
2.  Crowell, D.N., Reznikoff, W.S. and Raetz, C.R.H. Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase. J. Bacteriol. 169 (1987) 5727–5734. [DOI] [PMID: 2824445]
3.  Metzger, L.E., 4th and Raetz, C.R. Purification and characterization of the lipid A disaccharide synthase (LpxB) from Escherichia coli, a peripheral membrane protein. Biochemistry 48 (2009) 11559–11571. [DOI] [PMID: 19883124]
4.  Bohl, T.E., Shi, K., Lee, J.K. and Aihara, H. Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat. Commun. 9:377 (2018). [DOI] [PMID: 29371662]
[EC 2.4.1.182 created 1990, modified 2021]
 
 
EC 2.4.1.183     
Accepted name: α-1,3-glucan synthase
Reaction: UDP-glucose + [α-D-glucosyl-(1→3)]n = UDP + [α-D-glucosyl-(1→3)]n+1
Other name(s): uridine diphosphoglucose-1,3-α-glucan glucosyltransferase; 1,3-α-D-glucan synthase; UDP-glucose:α-D-(1-3)-glucan 3-α-D-glucosyltransferase
Systematic name: UDP-glucose:α-D-(1→3)-glucan 3-α-D-glucosyltransferase
Comments: A glucan primer is needed to begin the reaction, which brings about elongation of the glucan chains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-38-9
References:
1.  Andoh, M., Yamashita, Y., Shigeoka, T., Hanada, N. and Takehara, T. [Extension of the length of glucan chain by 1,3-α-D-glucansynthase from Streptococcus mutans serotype.] Koku Eisei Gakkai Zasshi 37 (1987) 516–517.
[EC 2.4.1.183 created 1990]
 
 
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 2.4.1.185     
Accepted name: flavanone 7-O-β-glucosyltransferase
Reaction: UDP-glucose + a flavanone = UDP + a flavanone 7-O-β-D-glucoside
For diagram of the biosynthesis of naringenin derivatives, click here
Other name(s): uridine diphosphoglucose-flavanone 7-O-glucosyltransferase; naringenin 7-O-glucosyltransferase; hesperetin 7-O-glucosyl-transferase
Systematic name: UDP-glucose:flavanone 7-O-β-D-glucosyltransferase
Comments: Naringenin and hesperetin can act as acceptors. No action on flavones or flavonols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-73-0
References:
1.  McIntosh, C.A., Latchinian, L. and Mansell, R.L. Flavanone-specific 7-O-glucosyltransferase activity in Citrus paradisi seedlings: purification and characterization. Arch. Biochem. Biophys. 282 (1990) 50–57. [DOI] [PMID: 2171434]
2.  McIntosh, C.A. and Mansell, R.L. Biosynthesis of naringin in Citrus paradisi - UDP-glucosyl-transferase activity in grapefruit seedlings. Phytochemistry 29 (1990) 1533–1538.
[EC 2.4.1.185 created 1992]
 
 
EC 2.4.1.186     
Accepted name: glycogenin glucosyltransferase
Reaction: UDP-α-D-glucose + glycogenin = UDP + α-D-glucosylglycogenin
Other name(s): glycogenin; priming glucosyltransferase; UDP-glucose:glycogenin glucosyltransferase
Systematic name: UDP-α-D-glucose:glycogenin α-D-glucosyltransferase
Comments: The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme’s Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains [7]. It continues to glucosylate an existing glucosyl group until a length of about 5–13 residues has been formed. Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11, glycogen (starch) synthase. The enzyme is not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117590-73-5
References:
1.  Krisman, C.R. and Barengo, R. A precursor of glycogen biosynthesis: α-1,4-glucan-protein. Eur. J. Biochem. 52 (1975) 117–123. [DOI] [PMID: 809265]
2.  Pitcher, J., Smythe, C., Campbell, D.G. and Cohen, P. Identification of the 38-kDa subunit of rabbit skeletal muscle glycogen synthase as glycogenin. Eur. J. Biochem. 169 (1987) 497–502. [DOI] [PMID: 3121316]
3.  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. [DOI] [PMID: 2970965]
4.  Kennedy, L.D., Kirkman, B.R., Lomako, J., Rodriguez, I.R. and Whelan, W.J. The biogenesis of rabbit-muscle glycogen. In: Berman, M.C. and Opie, L.A. (Ed.), Membranes and Muscle, ICSU Press/IRL Press, Oxford, 1985, pp. 65–84.
5.  Rodriguez, I.R. and Whelan, W.J. A novel glycosyl-amino acid linkage: rabbit-muscle glycogen is covalently linked to a protein via tyrosine. Biochem. Biophys. Res. Commun. 132 (1985) 829–836. [DOI] [PMID: 4062948]
6.  Lomako, J., Lomako, W.M. and Whelan, W.J. A self-glucosylating protein is the primer for rabbit muscle glycogen biosynthesis. FASEB J. 2 (1988) 3097–3103. [PMID: 2973423]
7.  Alonso, M.D., Lomako, J., Lomako, W.M. and Whelan, W.J. Catalytic activities of glycogenin additional to autocatalytic self-glucosylation. J. Biol. Chem. 270 (1995) 15315–15319. [DOI] [PMID: 7797519]
8.  Alonso, M.D., Lomako, J., Lomako, W.M. and Whelan, W.J. A new look at the biogenesis of glycogen. FASEB J. 9 (1995) 1126–1137. [PMID: 7672505]
9.  Mu, J. and Roach, P.J. Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism. J. Biol. Chem. 273 (1998) 34850–34856. [DOI] [PMID: 9857012]
10.  Gibbons, B.J., Roach, P.J. and Hurley, T.D. Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin. J. Mol. Biol. 319 (2002) 463. [DOI] [PMID: 12051921]
[EC 2.4.1.186 created 1992 (EC 2.4.1.112 created 1984, incorporated 2007)]
 
 
EC 2.4.1.187     
Accepted name: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-β-D-mannosaminyltransferase
Reaction: UDP-N-acetyl-α-D-mannosamine + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): uridine diphosphoacetyl-mannosamineacetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminyltransferase; N-acetylmannosaminyltransferase; UDP-N-acetylmannosamine:N-acetylglucosaminyl diphosphorylundecaprenol N-acetylmannosaminyltransferase; UDP-N-acetyl-D-mannosamine:N-acetyl-β-D-glucosaminyldiphosphoundecaprenol β-1,4-N-acetylmannosaminyltransferase; UDP-N-acetyl-D-mannosamine:N-acetyl-β-D-glucosaminyldiphosphoundecaprenol 4-β-N-acetylmannosaminyltransferase; tagA (gene name); tarA (gene name); UDP-N-acetyl-α-D-mannosamine:N-acetyl-β-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-β-N-acetylmannosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-mannosamine:N-acetyl-α-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol 4-β-N-acetylmannosaminyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 118731-82-1
References:
1.  Murazumi, N., Kumita, K., Araki, Y. and Ito, E. Partial purification and properties of UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase from Bacillus subtilis. J. Biochem. (Tokyo) 104 (1988) 980–984. [PMID: 2977387]
2.  Ginsberg, C., Zhang, Y.H., Yuan, Y. and Walker, S. In vitro reconstitution of two essential steps in wall teichoic acid biosynthesis. ACS Chem. Biol. 1 (2006) 25–28. [DOI] [PMID: 17163636]
3.  Zhang, Y.H., Ginsberg, C., Yuan, Y. and Walker, S. Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis TagA. Biochemistry 45 (2006) 10895–10904. [DOI] [PMID: 16953575]
[EC 2.4.1.187 created 1992, modified 2016]
 
 
EC 2.4.1.188     
Accepted name: N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase
Reaction: UDP-α-D-glucose + N-acetyl-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-glucosyl-(1→4)-N-acetyl-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase; uridine diphosphoglucose-acetylglucosaminylpyrophosphorylundecaprenol glucosyltransferase; UDP-glucose:N-acetyl-D-glucosaminyldiphosphoundecaprenol 4-β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acetyl-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118731-83-2
References:
1.  Kumita, K., Murazumi, N., Arasaki, Y. and Ito, E. Solubilization and properties of UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase from Bacillus coagulans AHU 1366 membranes. J. Biochem. (Tokyo) 104 (1988) 985–988. [PMID: 2977388]
[EC 2.4.1.188 created 1992]
 
 


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