Enzyme Nomenclature

EC 2.4.1 (continued)


Continued from:
EC to EC
EC to EC
EC to EC
See separate file for EC to EC, EC to EC and EC to EC


EC included with EC
EC 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase
EC UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase
EC now EC
EC α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase
EC indolylacetyl-myo-inositol galactosyltransferase
EC transferred now EC and EC
EC 13-hydroxydocosanoate 13-β-glucosyltransferase
EC flavonol-3-O-glucoside L-rhamnosyltransferase
EC pyridoxine 5'-O-β-D-glucosyltransferase
EC oligosaccharide 4-α-D-glucosyltransferase
EC aldose β-D-fructosyltransferase
EC now included with EC
EC transferred now EC
EC N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase
EC raffinose—raffinose α-galactosyltransferase
EC sucrose 6F-α-galactosyltransferase
EC xyloglucan 4-glucosyltransferase
EC now EC
EC isoflavone 7-O-glucosyltransferase
EC methyl-ONN-azoxymethanol β-D-glucosyltransferase
EC salicyl-alcohol β-D-glucosyltransferase
EC sterol 3β-glucosyltransferase
EC glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase
EC glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase
EC gibberellin β-D-glucosyltransferase
EC cinnamate β-D-glucosyltransferase
EC hydroxymandelonitrile glucosyltransferase
EC lactosylceramide β-1,3-galactosyltransferase
EC lipopolysaccharide N-acetylmannosaminouronosyltransferase
EC hydroxyanthraquinone glucosyltransferase
EC lipid-A-disaccharide synthase
EC α-1,3-glucan synthase
EC galactolipid galactosyltransferase
EC flavanone 7-O-β-glucosyltransferase
EC glycogenin glucosyltransferase
EC N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-β-D-mannosaminyltransferase
EC N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase
EC luteolin 7-O-glucuronosyltransferase
EC luteolin-7-O-glucuronide 2"-O-glucuronosyltransferase
EC luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase
EC nuatigenin 3β-glucosyltransferase
EC sarsapogenin 3β-glucosyltransferase
EC 4-hydroxybenzoate 4-O-β-D-glucosyltransferase
EC N-hydroxythioamide S-β-glucosyltransferase
EC nicotinate glucosyltransferase
EC high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase
EC phosphatidylinositol N-acetylglucosaminyltransferase
EC β-mannosylphosphodecaprenol—mannooligosaccharide 6-mannosyltransferase
EC now EC

See the following file for:

EC to EC
EC to EC
EC to EC


[EC Transferred entry: now included with EC, N-acetyllactosaminide 3-α-galactosyltransferase (EC created 1984, deleted 2002)]


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 reaction, click here

Other name(s): Lewis-negative α-3-fucosyltransferase; plasma α-3-fucosyltransferase; guanosine diphosphofucose-glucoside α1→3-fucosyltransferase; galactoside 3-fucosyltransferase; GDP-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase; 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

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, 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


1. Johnson, P.H., Yates, A.D. and Watkins, W.M. Human salivary fucosyltransferase: evidence for two distinct α-3-L-fucosyltransferase activities one of which is associated with the Lewis blood Le gene. Biochem. Biophys. Res. Commun. 100 (1981) 1611-1618. [PMID: 7295318]

2. Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98-134. [PMID: 6366476]

3. Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893-21900. [PMID: 12676935]

[EC created 1984, modified 2002, modified 2019]


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, UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-73-5


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. [PMID: 23624439]

[EC created 1984, modified 2015]

[EC Deleted entry: globotriosylceramide β-1,6-N-acetylgalactosaminyl-transferase. The enzyme is identical to EC, 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 created 1986, deleted 2006)]


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 reaction 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


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. [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 created 1986, modified 2001, modified 2018]


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


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 created 1986]

[EC Transferred entry: 1,2-diacylglycerol 3-glucosyltransferase. Now classified as EC, monoglucosyldiacylglycerol synthase, and EC, 1,2-diacylglycerol 3-α-glucosyltransferase (EC created 1986, deleted 2015)]


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


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 created 1986]


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 reaction 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


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. [PMID: 12900416]

[EC created 1986, modified 2015]


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


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 created 1986]


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, 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


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. [PMID: 23132856]

[EC created 1989, modified 2013]


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


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 created 1989, modified 1999]

[EC Transferred entry: β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase, now included in EC, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase (EC created 1989, deleted 2016)]

[EC Transferred entry: galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,6-N-acetylglucosaminyltransferase, now included with EC, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase (EC created 1989, deleted 2016)]


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 reaction 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-acetylgalactosaminyltransferasee

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


1. Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a -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. [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 created 1989]


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


1. Hopf, H., Gruber, G., Zinn, A. and Kandler, O. Physiology and biosynthesis of lychnose in Cerastium arvense. Planta 162 (1984) 283-288.

[EC created 1989]


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


1. Hopf, H., Spanfelner, M. and Kandler, O. Planteose synthesis in seeds of Sesamum indicum L. Z. Pflanzenphysiol. 114 (1984) 485-492.

[EC created 1989]


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

Systematic name: UDP-glucose:xyloglucan 1,4-β-D-glucosyltransferase

Comments: In association with EC (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 cellulose synthase (UDP-forming).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80237-91-8


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 created 1989]

[EC Transferred entry: now EC, xyloglucan 6-xylosyltransferase (EC created 1989, deleted 2003)]


Accepted name: isoflavone 7-O-glucosyltransferase

Reaction: UDP-glucose + an isoflavone = UDP + an isoflavone 7-O-β-D-glucoside

See diagram for reaction on biochanin A or formononetin.

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


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. [PMID: 6458246]

[EC created 1989]


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


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 created 1989]


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


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 created 1989]


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 (nuatigenin 3β-glucosyltransferase) or EC (sarsapogenin 3β-glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 123940-38-5 and 9075-00-7


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. [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 created 1989]


Accepted name: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-D-galactosamine + β-D-glucuronyl-(1→3)-D-galactosyl-proteoglycan = UDP + N-acetyl-D-galactosaminyl-(1→4)-β-D-glucuronyl-(1→3)-β-D-galactosylproteoglycan

For diagram click here.

Other name(s): N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I

Systematic name: UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase

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


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. [PMID: 3922754]

2. Uyama, T., Kitagawa, H., Tamura, Ji J. 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. [PMID: 11788602]

[EC created 1989, modified 2002]


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 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, 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


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. [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. [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. [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. [PMID: 11943778]

[EC created 1989, modified 2002]


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 and 94489-97-1


1. Sembdner, G., Knoefel, H.D., Schwarzkopf, E. and Liebisch, H.W. In vitro glucosylation of gibberellins. Biol. Plant. 27 (1985) 231-236.

[EC created 1989]


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


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: 6092175]

[EC created 1989]


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


1. Hösel, W. and Schiel, O. Biosynthesis of cyanogenic glucosides: in vitro analysis of the glucosylation step. Arch. Biochem. Biophys. 229 (1984) 177-186. [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 created 1989]


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 reaction click here.

Other name(s): uridine diphosphogalactose-lactosylceramide β1→3-galactosyltransferase; UDP-galactose:D-galactosyl-1,4-β-D-glucosyl-R β-1,3-galactosyltransferase

Systematic name: UDP-α-D-galactose:β-D-galactosyl-1,4-β-D-glucosyl-R β-1,3-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


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. [PMID: 3129295]

[EC created 1989]


Accepted name: lipopolysaccharide N-acetylmannosaminouronosyltransferase

Reaction: UDP-N-acetyl-α-D-mannosaminouronate + N-acetyl-β-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

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


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. [PMID: 3275612]

[EC created 1990, modified 2011]


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-dihydroxyanthraquinone and 1,8-dihydroxyanthraquinone.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112198-78-4


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 created 1990]


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 lreaction click here

Glossary: a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
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 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC (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


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. [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. [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 (2018) 377. [PMID: 29371662]

[EC created 1990, modified 2021]


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

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


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 (in Japanese).

[EC created 1990]


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 reaction 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, monogalactosyldiacylglycerol synthase, and EC, digalactosyldiacylglycerol synthase. Note that the β,β-digalactosyldiacylglycerol formed by this enzyme is different from the more common α,β-digalactosyldiacylglycerol formed by EC 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


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.

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. [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. [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. [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. [PMID: 20798281]

[EC created 1990, modified 2005, modified 2015]


Accepted name: flavanone 7-O-β-glucosyltransferase

Reaction: UDP-glucose + a flavanone = UDP + a flavanone 7-O-β-D-glucoside

For diagram 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


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. [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 created 1992]


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, 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


1. Krisman, C.R. and Barengo, R. A precursor of glycogen biosynthesis: α-1,4-glucan-protein. Eur. J. Biochem. 52 (1975) 117-123. [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. [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. [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. (Eds), 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. [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. [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. [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) 463-177. [PMID: 12051921]

[EC created 1992 (EC created 1984, incorporated 2007)]


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-glucosaminyl-diphospho-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


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. [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. [PMID: 16953575]

[EC created 1992, modified 2016]


Accepted name: N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase

Reaction: UDP-glucose + N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol = UDP + β-D-glucosyl-(1→4)-N-acetyl-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol

Other name(s): UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase; uridine diphosphoglucose-acetylglucosaminylpyrophosphorylundecaprenol glucosyltransferase; UDP-glucose:N-acetyl-D-glucosaminyl-diphosphoundecaprenol 4-β-D-glucosyltransferase

Systematic name: UDP-&alpha-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


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 created 1992]


Accepted name: luteolin 7-O-glucuronosyltransferase

Reaction: UDP-glucuronate + luteolin = UDP + luteolin 7-O-β-D-glucuronide

For diagram click here.

Other name(s): uridine diphosphoglucuronate-luteolin 7-O-glucuronosyltransferase; LGT

Systematic name: UDP-glucuronate:luteolin 7-O-glucuronosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115490-49-8


1. Schulz, M. and Weissenböck, G. 3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale cereale. Phytochemistry 27 (1988) 1261-1267.

[EC created 1992]


Accepted name: luteolin-7-O-glucuronide 2"-O-glucuronosyltransferase

Reaction: UDP-glucuronate + luteolin 7-O-β-D-glucuronide = UDP + luteolin 7-O-[β-D-glucuronosyl-(1→2)-β-D-glucuronide]

For diagram click here.

Other name(s): uridine diphosphoglucuronate-luteolin 7-O-glucuronide glucuronosyltransferase; LMT; UDP-glucuronate:luteolin 7-O-glucuronide-glucuronosyltransferase

Systematic name: UDP-glucuronate:luteolin-7-O-β-D-glucuronide 2"-O-glucuronosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115490-51-2


1. Schulz, M. and Weissenböck, G. 3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale cereale. Phytochemistry 27 (1988) 1261-1267.

2. Anhalt, S. and Weissenböck, G. Subcellular localization of luteolin glucuronides and related enzymes in rye mesophyll. Planta 187 (1992) 83-88.

[EC created 1992]


Accepted name: luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase

Reaction: UDP-glucuronate + luteolin 7-O-[β-D-glucuronosyl-(1→2)-β-D-glucuronide] = UDP + luteolin 7-O-[β-D-glucuronosyl-(1→2)-β-D-glucuronide]-4'-O-β-D-glucuronide

For diagram of reaction click here

Other name(s): uridine diphosphoglucuronate-luteolin 7-O-diglucuronide glucuronosyltransferase; UDP-glucuronate:luteolin 7-O-diglucuronide-glucuronosyltransferase; UDPglucuronate:luteolin 7-O-diglucuronide-4'-O-glucuronosyl-transferase; LDT

Systematic name: UDP-glucuronate:luteolin-7-O-β-D-diglucuronide 4'-O-glucuronosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115490-50-1


1. Schulz, M. and Weissenböck, G. 3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale cereale. Phytochemistry 27 (1988) 1261-1267.

[EC created 1992, modified 2011]


Accepted name: nuatigenin 3β-glucosyltransferase

Reaction: UDP-glucose + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3β,26-diol = UDP + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3β,26-diol 3-O-β-D-glucoside

Other name(s): uridine diphosphoglucose-nuatigenin glucosyltransferase

Systematic name: UDP-glucose:(20S,22S,25S)-22,25-epoxyfurost-5-ene-3β,26-diol 3-O-β-D-glucosyltransferase

Comments: Some other sapogenins can act as glucosyl acceptors. Involved in the biosynthesis of plant saponins. Not identical with EC (sterol 3β-glucosyltransferase) or EC (sarsapogenin 3β-glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 108891-57-2


1. Kalinowska, M. and Wojciechowski, Z.A. Enzymatic-synthesis of nuatigenin 3-β-D-glucoside in oat (Avena sativa) leaves. Phytochemistry 25 (1986) 2525-2529.

2. Kalinowska, M. and Wojciechowski, Z.A. Subcellular-localization of UDPG-nuatigenin glucosyltransferase in oat leaves. Phytochemistry 26 (1987) 353-357.

[EC created 1992]


Accepted name: sarsapogenin 3β-glucosyltransferase

Reaction: UDP-glucose + (25S)-5β-spirostan-3β-ol = UDP + (25S)-5β-spirostan-3β-ol 3-O-β-D-glucoside

Other name(s): uridine diphosphoglucose-sarsapogenin glucosyltransferase

Systematic name: UDP-glucose:(25S)-5β-spirostan-3β-ol 3-O-β-D-glucosyltransferase

Comments: Specific to 5β-spirostanols. Involved in the biosynthesis of plant saponins. Not identical with EC (sterol 3β-glucosyltransferase) or EC (nuatigenin 3β-glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117698-14-3


1. Paczkowski, C. and Wojciechowski, Z.A. The occurrence of UDPG-dependent glucosyltransferase specific for sarsasapogenin in Asparagus officinalis. Phytochemistry 27 (1988) 2743-2747.

[EC created 1992]


Accepted name: 4-hydroxybenzoate 4-O-β-D-glucosyltransferase

Reaction: UDP-glucose + 4-hydroxybenzoate = UDP + 4-(β-D-glucosyloxy)benzoate

Other name(s): uridine diphosphoglucose-4-hydroxybenzoate glucosyltransferase; UDP-glucose:4-(β-D-glucopyranosyloxy)benzoic acid glucosyltransferase; HBA glucosyltransferase; p-hydroxybenzoate glucosyltransferase; PHB glucosyltransferase; PHB-O-glucosyltransferase

Systematic name: UDP-glucose:4-hydroxybenzoate 4-O-β-D-glucosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 120860-68-6


1. Katsumata, T., Shige, H. and Ejiri, S.-I. Biochemical-studies on pollen. 34. UDP glucose-4-(β-D-glucopyranosyloxy) benzoic-acid glucosyltransferase from the pollen of Pinus densiflora. Phytochemistry 28 (1989) 359-362.

[EC created 1992]


Accepted name: N-hydroxythioamide S-β-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + (Z)-2-phenyl-1-thioacetohydroximate = UDP + desulfoglucotropeolin
(2) UDP-α-D-glucose + an (E)-ω-(methylsulfanyl)alkyl-thiohydroximate = UDP + an aliphatic desulfoglucosinolate
(3) UDP-α-D-glucose + (E)-2-(1H-indol-3-yl)-1-thioacetohydroximate = UDP + desulfoglucobrassicin

For diagram of reaction, click here

Glossary: an aliphatic desulfoglucosinolate = an ω-(methylsulfanyl)alkylhydroximate S-glucoside

Other name(s): UGT74B1 (gene name); desulfoglucosinolate-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-thiohydroximate glucosyltransferase; thiohydroximate β-D-glucosyltransferase; UDPG:thiohydroximate glucosyltransferase; thiohydroximate S-glucosyltransferase; thiohydroximate glucosyltransferase; UDP-glucose:thiohydroximate S-β-D-glucosyltransferase; UDP-glucose:N-hydroxy-2-phenylethanethioamide S-β-D-glucosyltransferase

Systematic name: UDP-α-D-glucose:N-hydroxy-2-phenylethanethioamide S-β-D-glucosyltransferase

Comments: The enzyme specifically glucosylates the thiohydroximate functional group. It is involved in the biosynthesis of glucosinolates in cruciferous plants, and acts on aliphatic, aromatic, and indolic substrates.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-14-8


1. Jain, J.C., Reed, D.W., Groot Wassink, J.W.D. and Underhill, E.W. A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species. Anal. Biochem. 178 (1989) 137-140. [PMID: 2524977]

2. Reed, D.W., Davin, L., Jain, J.C., Deluca, V., Nelson, L. and Underhill, E.W. Purification and properties of UDP-glucose:thiohydroximate glucosyltransferase from Brassica napus L. seedlings. Arch. Biochem. Biophys. 305 (1993) 526-532. [PMID: 8373190]

3. Marillia, E.F., MacPherson, J.M., Tsang, E.W., Van Audenhove, K., Keller, W.A. and GrootWassink, J.W. Molecular cloning of a Brassica napus thiohydroximate S-glucosyltransferase gene and its expression in Escherichia coli. Physiol. Plant 113 (2001) 176-184. [PMID: 12060294]

4. Fahey, J.W., Zalcmann, A.T. and Talalay, P. The chemical diversity and distribution of glucosinolates and isothiocyanates among plants. Phytochemistry 56 (2001) 5-51. [PMID: 11198818]

5. Grubb, C.D., Zipp, B.J., Ludwig-Muller, J., Masuno, M.N., Molinski, T.F. and Abel, S. Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate biosynthesis and auxin homeostasis. Plant J. 40 (2004) 893-908. [PMID: 15584955]

[EC created 1992, modified 2006, modified 2018]


Accepted name: nicotinate glucosyltransferase

Reaction: UDP-glucose + nicotinate = UDP + N-glucosylnicotinate

Other name(s): uridine diphosphoglucose-nicotinate N-glucosyltransferase; UDP-glucose:nicotinic acid-N-glucosyltransferase

Systematic name: UDP-glucose:nicotinate N-glucosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 120858-56-2


1. Upmeier, B., Thomzik, J.E. and Barz, W. Enzymatic studies on the reversible synthesis of nicotinic acid-N-glucoside in heterotrophic parsley cell suspension cultures. Z. Naturforsch. C: Biosci. 43 (1988) 835-842.

[EC created 1992]


Accepted name: high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase

Reaction: Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked α-(1→6) to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum

Other name(s): uridine diphosphoacetylglucosamine-oligosaccharide acetylglucosaminyltransferase; acetylglucosamine-oligosaccharide acetylglucosaminyltransferase; UDP-GlcNAc:oligosaccharide β-N-acetylglucosaminyltransferase

Systematic name: UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase

Comments: The activity of the intersecting mannose residue as acceptor is dependent on two other mannose residues attached by α-1,3 and α-1,6 links.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 123425-54-7


1. Sharkey, D.J. and Kornfeld, R. Identification of an N-acetylglucosaminyltransferase in Dictyostelium discoideum that transfers an "intersecting" N-acetylglucosamine residue to high mannose oligosaccharides. J. Biol. Chem. 264 (1989) 10411-10419. [PMID: 2525124]

[EC created 1992]


Accepted name: phosphatidylinositol N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

For diagram click here.

Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns

Other name(s): UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase; uridine diphosphoacetylglucosamine α1,6-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-α-D-glucosaminyl)transferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-α-D-glucosaminyl)transferase (configuration-retaining)

Comments: Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 144388-35-2


1. Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168-11173. [PMID: 2525555]

2. Watanabe, R., Inoue, N., Westfall, B., Taron, C.H., Orlean, P., Takeda, J. and Kinoshita, T. The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 17 (1998) 877-885. [PMID: 9463366]

3. Watanabe, R., Murakami, Y., Marmor, M.D., Inoue, N., Maeda, Y., Hino, J., Kangawa, K., Julius, M. and Kinoshita, T. Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 19 (2000) 4402-4411. [PMID: 10944123]

[EC created 1992, modified 2002]


Accepted name: β-mannosylphosphodecaprenol—mannooligosaccharide 6-mannosyltransferase

Reaction: β-D-mannosylphosphodecaprenol + (1→6)-α-D-mannosyloligosaccharide = decaprenol phosphate + (1→6)-α-D-mannosyl-(1→6)-α-D-mannosyl-oligosaccharide

Other name(s): mannosylphospholipid-methylmannoside α-1,6-mannosyltransferase

Systematic name: β-D-mannosylphosphodecaprenol:1,6-α-D-mannosyloligosaccharide 1,6-α-D-mannosyltransferase

Comments: Involved in the formation of mannooligosaccharides in the membrane of Mycobacterium smegmatis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125008-27-7


1. Yokoyama, K. and Ballou, C.E. Synthesis of α1→6-mannooligosaccharides in Mycobacterium smegmatis. Function of β-mannosylphosphoryldecaprenol as the mannosyl donor. J. Biol. Chem. 264 (1989) 21621-21628. [PMID: 2480954]

[EC created 1992]

[EC Transferred entry: now EC, inulin fructotransferase (DFA-I-forming). The enzyme was wrongly classified as a transferase rather than a lyase. (EC created 1992, deleted 2004)]

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