ExplorEnz: EC 2.4.*.*

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2.4.1.101

Accepted name:

α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + Man₅GlcNAc₂-[protein] = UDP + Man₅GlcNAc₃-[protein]

For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here

Glossary:

Man₅GlcNAc₂-[protein] = α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]
Man₅GlcNAc₃-[protein]= β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]

Other name(s):

MGAT1 (gene name); N-acetylglucosaminyltransferase I; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; uridine diphosphoacetylglucosamine-α-1,3-mannosylglycoprotein β-1,2-N-acetylglucosaminyltransferase; UDP-N-acetylglucosaminyl:α-1,3-D-mannoside-β-1,2-N-acetylglucosaminyltransferase I; UDP-N-acetylglucosaminyl:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I; α-1,3-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTI; GlcNAc-T I; UDP-N-acetyl-D-glucosamine:3-(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→3)-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 action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act. While the natural substrate (produced by EC 3.2.1.113, mannosyl-oligosaccharide 1,2-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→3)-β-D-Man-R.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102576-81-8

References:

1.	Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity. J. Biol. Chem. 255 (1980) 4885–4893. [PMID: 6445358]
2.	Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa. Biochemistry 20 (1981) 967–976. [PMID: 6452163]
3.	Oppenheimer, C.L. and Hill, R.L. Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase. J. Biol. Chem. 256 (1981) 799–804. [PMID: 6450208]
4.	Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. The nonidentity of porcine N-acetylglucosaminyltransferases I and II. J. Biol. Chem. 256 (1981) 11477–11482. [PMID: 6457827]
5.	Miyagi, T. and Tsuiki, S. Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas. Biochim. Biophys. Acta 661 (1981) 148–157. [DOI] [PMID: 6170335]
6.	Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
7.	Vella, G.J., Paulsen, H. and Schachter, H. Control of glycoprotein synthesis. IX. A terminal Man alphal-3Man β1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: α-D-mannoside (GlcNAc to Man α1-3) β2-N-acetylglucosaminyltransferase I. Can. J. Biochem. Cell Biol. 62 (1984) 409–417. [PMID: 6235906]
8.	Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H. and Rini, J.M. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J. 19 (2000) 5269–5280. [DOI] [PMID: 11032794]

[EC 2.4.1.101 created 1983, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]

2.4.1.102

Accepted name:

β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + O³-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein] = UDP + O³-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]

Glossary:

core 1 = O³-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein]
core 2 = O³-{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 I; β6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-mucin β-(1→6)-acetylglucosaminyltransferase; core 2 acetylglucosaminyltransferase; core 6-β-GlcNAc-transferase A; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase; GCNT1; GCNT3; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R) 6-β-N-acetyl-D-glucosaminyltransferase

Systematic name:

UDP-N-acetyl-α-D-glucosamine:O³-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)

Comments:

The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 1 structure of O-glycans forming core 2.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95978-15-7

References:

1.	Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
2.	Williams, D., Longmore, G., Matta, K.L. and Schachter, H. Mucin synthesis. II. Substrate specificity and product identification studies on canine submaxillary gland UDP-GlcNAc:Gal β1-3GalNAc(GlcNAc→GalNAc) β6-N-acetylglucosaminyltransferase. J. Biol. Chem. 255 (1980) 11253–11261. [PMID: 6449508]
3.	Williams, D. and Schachter, H. Mucin synthesis. I. Detection in canine submaxillary glands of an N-acetylglucosaminyltransferase which acts on mucin substrates. J. Biol. Chem. 255 (1980) 11247–11252. [PMID: 6449507]

[EC 2.4.1.102 created 1983, modified 2018]

2.4.1.103

Accepted name:

alizarin 2-β-glucosyltransferase

Reaction:

UDP-glucose + 1,2-dihydroxy-9,10-anthraquinone = UDP + 1-hydroxy-2-(β-D-glucosyloxy)-9,10-anthraquinone

Glossary:

alizarin = 1,2-dihydroxy-9,10-anthraquinone

Other name(s):

uridine diphosphoglucose-alizarin glucosyltransferase

Systematic name:

UDP-glucose:1,2-dihydroxy-9,10-anthraquinone 2-O-β-D-glucosyltransferase

Comments:

Acts on other hydroxy- and dihydroxy-derivatives of 9,10-anthraquinone.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74506-41-5

References:

1.	Mateju, J., Cudlin, J., Steinerova, N., Blumauerova, M. and Vanek, Z. Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens. Folia Microbiol. 24 (1979) 205–210. [PMID: 38193]

[EC 2.4.1.103 created 1983]

2.4.1.104

Accepted name:

o-dihydroxycoumarin 7-O-glucosyltransferase

Reaction:

UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin

Other name(s):

uridine diphosphoglucose-o-dihydroxycoumarin 7-O-glucosyltransferase; UDP-glucose:o-dihydroxycoumarin glucosyltransferase

Systematic name:

UDP-glucose:7,8-dihydroxycoumarin 7-O-β-D-glucosyltransferase

Comments:

Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74114-37-7

References:

1.	Ibrahim, R.K. and Boulay, B. Purification and some properties of UDP-glucose:o-hydroxycoumarin 7-O-glucosyltransferase from tobacco cell cultures. Plant Sci. Lett. 18 (1980) 177–184.

[EC 2.4.1.104 created 1983]

2.4.1.105

Accepted name:

vitexin β-glucosyltransferase

Reaction:

UDP-glucose + vitexin = UDP + vitexin 2′′-O-β-D-glucoside

For diagram of the biosynthesis of vitexin and isovitexin derivatives, click here

Other name(s):

uridine diphosphoglucose-vitexin 2′′-glucosyltransferase

Systematic name:

UDP-glucose:vitexin 2′′-O-β-D-glucosyltransferase

Comments:

Vitexin is a flavonoid from Cannabis sativa (hemp) and some populations of Silene alba.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76828-68-7

References:

1.	Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2′′-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935–1937.

[EC 2.4.1.105 created 1983]

2.4.1.106

Accepted name:

isovitexin β-glucosyltransferase

Reaction:

UDP-glucose + isovitexin = UDP + isovitexin 2′′-O-β-D-glucoside

For diagram of the biosynthesis of vitexin and isovitexin derivatives, click here

Other name(s):

uridine diphosphoglucose-isovitexin 2′′-glucosyltransferase

Systematic name:

UDP-glucose:isovitexin 2′′-O-β-D-glucosyltransferase

Comments:

Isovitexin is a flavonoid from petals of Silene alba.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72102-99-9

References:

1.	Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2′′-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935–1937.

[EC 2.4.1.106 created 1983]

2.4.1.107

Deleted entry:

UDP-glucuronate—testosterone glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase

[EC 2.4.1.107 created 1983, deleted 1984]

2.4.1.108

Deleted entry:

UDP-glucuronate—phenol glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase

[EC 2.4.1.108 created 1983, deleted 1984]

2.4.1.109

Accepted name:

dolichyl-phosphate-mannose—protein mannosyltransferase

Reaction:

(1) dolichyl β-D-mannosyl phosphate + L-threonyl-[protein] = dolichyl phosphate + 3-O-(α-D-mannosyl)-L-threonyl-[protein]
(2) dolichyl β-D-mannosyl phosphate + L-seryl-[protein] = dolichyl phosphate + 3-O-(α-D-mannosyl)-L-seryl-[protein]

For diagram of glycoprotein biosynthesis, click here

Other name(s):

dolichol phosphomannose-protein mannosyltransferase; protein O-D-mannosyltransferase; dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase; dolichyl-phosphate-mannose-protein mannosyltransferase; dolichyl-D-mannosyl-phosphate:protein O-D-mannosyltransferase

Systematic name:

dolichyl β-D-mannosyl-phosphate:L-threonyl/L-seryl-[protein] O-D-mannosyltransferase (configuration-inverting)

Comments:

The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain α-dihydropolyprenyl derivatives, larger than C₃₅.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74315-99-4

References:

1.	Babczinski, P., Haselbeck, A. and Tanner, W. Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme. Eur. J. Biochem. 105 (1980) 509–515. [DOI] [PMID: 6989607]
2.	Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives. Eur. J. Biochem. 105 (1980) 517–523. [DOI] [PMID: 6445267]

[EC 2.4.1.109 created 1983, modified 2014]

2.4.1.110

Accepted name:

tRNA-queuosine α-mannosyltransferase

Reaction:

GDP-α-D-mannose + queuosine³⁴ in tRNA^Asp = GDP + O-4′′-α-D-mannosylqueuosine³⁴ in tRNA^Asp

Other name(s):

GDP-mannose:tRNA^Asp-queuosine O-5′′-β-D-mannosyltransferase (incorrect); tRNA-queuosine β-mannosyltransferase (incorrect)

Systematic name:

GDP-α-D-mannose:queuosine³⁴ in tRNA^Asp O-4′′-α-D-mannosyltransferase (configuration-retaining)

Comments:

This enzyme, found in higher vertebrates, modifies tRNA^Asp at the wobble position of the anticodon loop.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-06-5

References:

1.	Okada, N. and Nishimura, S. Enzymatic synthesis of Q nucleoside containing mannose in the anticodon of tRNA: isolation of a novel mannosyltransferase from a cell-free extract of rat liver. Nucleic Acids Res. 4 (1977) 2931–2938. [DOI] [PMID: 20603]
2.	Hillmeier, M., Wagner, M., Ensfelder, T., Korytiakova, E., Thumbs, P., Muller, M. and Carell, T. Synthesis and structure elucidation of the human tRNA nucleoside mannosyl-queuosine. Nat. Commun. 12:7123 (2021). [DOI] [PMID: 34880214]

[EC 2.4.1.110 created 1984, modified 2022]

2.4.1.111

Accepted name:

coniferyl-alcohol glucosyltransferase

Reaction:

UDP-glucose + coniferyl alcohol = UDP + coniferin

Other name(s):

uridine diphosphoglucose-coniferyl alcohol glucosyltransferase; UDP-glucose coniferyl alcohol glucosyltransferase

Systematic name:

UDP-glucose:coniferyl-alcohol 4′-β-D-glucosyltransferase

Comments:

Sinapyl alcohol can also act as acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61116-23-2

References:

1.	Ibrahim, R.K. and Grisebach, H. Purification and properties of UDP-glucose: coniferyl alcohol glucosyltransferase from suspension cultures of Paul's scarlet rose. Arch. Biochem. Biophys. 176 (1976) 700–708. [DOI] [PMID: 10853]

[EC 2.4.1.111 created 1984]

2.4.1.112

Deleted entry:

α-1,4-glucan-protein synthase (UDP-forming). The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase

[EC 2.4.1.112 created 1984, deleted 2007]

2.4.1.113

Accepted name:

α-1,4-glucan-protein synthase (ADP-forming)

Reaction:

ADP-glucose + protein = ADP + α-D-glucosyl-protein

Other name(s):

ADP-glucose:protein glucosyltransferase; adenosine diphosphoglucose-protein glucosyltransferase

Systematic name:

ADP-glucose:protein 4-α-D-glucosyltransferase

Comments:

The enzyme builds up α-1,4-glucan chains covalently bound to protein, thus acting as an initiator of glycogen synthesis.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67053-99-0

References:

1.	Barengo, R. and Krisman, C.R. Initiation of glycogen biosynthesis in Escherichia coli. Studies of the properties of the enzymes involved. Biochim. Biophys. Acta 540 (1978) 190–196. [DOI] [PMID: 418819]

[EC 2.4.1.113 created 1984]

2.4.1.114

Accepted name:

2-coumarate O-β-glucosyltransferase

Reaction:

UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-β-D-glucosyl-2-hydroxycinnamate

Other name(s):

uridine diphosphoglucose-o-coumarate glucosyltransferase; UDPG:o-coumaric acid O-glucosyltransferase

Systematic name:

UDP-glucose:trans-2-hydroxycinnamate O-β-D-glucosyltransferase

Comments:

Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73665-97-1

References:

1.	Kleinhofs, A., Haskins, F.A. and Gorz, H.J. trans-o-Hydroxylcinnamic acid glucosylation in cell-free extracts of Melilotus alba. Phytochemistry 6 (1967) 1313–1318.
2.	Poulton, J.E., McRee, B.E. and Conn, E.E. Intracellular localization of two enzymes involved in coumarin biosynthesis in Melilotus alba. Plant Physiol. 65 (1980) 171–175. [PMID: 16661155]

[EC 2.4.1.114 created 1984]

2.4.1.115

Accepted name:

anthocyanidin 3-O-glucosyltransferase

Reaction:

UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-β-D-glucoside

For diagram of anthocyanin biosynthesis, click here

Other name(s):

uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase; UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-glucosyltransferase; UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase; 3-GT

Systematic name:

UDP-D-glucose:anthocyanidin 3-O-β-D-glucosyltransferase

Comments:

The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.20.4, anthocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65607-32-1

References:

1.	Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1045–1058. [PMID: 751640]
2.	Ford, C.M., Boss, P.K. and Høj, P.B. Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273 (1998) 9224–9233. [DOI] [PMID: 9535914]
3.	Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276 (2001) 25797–25803. [DOI] [PMID: 11316805]

[EC 2.4.1.115 created 1984 (EC 2.4.1.233 created 2004, incorporated 2005), modified 2005]

2.4.1.116

Accepted name:

cyanidin 3-O-rutinoside 5-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside

For diagram of anthocyanidin rutoside biosynthesis, click here

Glossary:

cyanidin 3-O-rutinoside = cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase

Comments:

Isolated from the plants Silene dioica (red campion) [1], Iris ensata (Japanese iris) [2] and Iris hollandica (Dutch iris) [3]. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 70248-66-7

References:

1.	Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059–1071. [PMID: 751641]
2.	Yabuya, T., Yamaguchi, M., Imayama, T., Katoh, K. and Ino I. Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata. Plant Sci. 162 (2002) 779–784.
3.	Imayama, T., Yoshihara, Y., Fukuchi-Mizutani, M., Tanaka, Y., Ino, I. and Yabuya, T. Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica. Plant Sci. 167 (2004) 1243–1248.

[EC 2.4.1.116 created 1984 (EC 2.4.1.235 created 2004, incorporated 2006), modified 2006, modified 2013]

2.4.1.117

Accepted name:

dolichyl-phosphate β-glucosyltransferase

Reaction:

UDP-α-D-glucose + dolichyl phosphate = UDP + dolichyl β-D-glucosyl phosphate

Other name(s):

polyprenyl phosphate:UDP-D-glucose glucosyltransferase; UDP-glucose dolichyl-phosphate glucosyltransferase; uridine diphosphoglucose-dolichol glucosyltransferase; UDP-glucose:dolichol phosphate glucosyltransferase; UDP-glucose:dolicholphosphoryl glucosyltransferase; UDP-glucose:dolichyl monophosphate glucosyltransferase; UDP-glucose:dolichyl phosphate glucosyltransferase; UDP-glucose:dolichyl-phosphate β-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:dolichyl-phosphate β-D-glucosyltransferase (configuration-inverting)

Comments:

Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 71061-42-2

References:

1.	Behrens, N.H. and Leloir, L.F. Dolichol monophosphate glucose: an intermediate in glucose transfer in liver. Proc. Natl. Acad. Sci. USA 66 (1970) 153–159. [DOI] [PMID: 5273893]
2.	Herscovics, A., Bugge, B. and Jeanloz, R.W. Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. J. Biol. Chem. 252 (1977) 2271–2277. [PMID: 849929]
3.	Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase. J. Biol. Chem. 254 (1979) 4814–4819. [PMID: 438216]

[EC 2.4.1.117 created 1984]

2.4.1.118

Accepted name:

cytokinin 7-β-glucosyltransferase

Reaction:

UDP-glucose + an N⁶-alkylaminopurine = UDP + an N⁶-alkylaminopurine-7-β-D-glucoside

Glossary:

zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N⁶-(4-hydroxy-3-methylbut-2-enyl)adenine

Other name(s):

uridine diphosphoglucose-zeatin 7-glucosyltransferase; cytokinin 7-glucosyltransferase; UDP-glucose:zeatin 7-glucosyltransferase

Systematic name:

UDP-glucose:N⁶-alkylaminopurine 7-glucosyltransferase

Comments:

Acts on a range of N⁶-substituted adenines, including zeatin and N⁶-benzylaminopurine, but not N⁶-benzyladenine. With some acceptors, 9-β-D-glucosides are also formed.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72103-03-8

References:

1.	Entsch, B. and Letham, D.S. Enzymic glucosylation of the cytokinin, 6-benzylaminopurine. Plant Sci. Lett. 14 (1979) 205–212.
2.	Entsch, B., Parker, C.W., Letham, D.S. and Summons, R.E. Preparation and characterization, using high-performance liquid chromatography, of an enzyme forming glucosides of cytokinins. Biochim. Biophys. Acta 570 (1979) 124–139. [DOI] [PMID: 486500]

[EC 2.4.1.118 created 1984]

2.4.1.119

Transferred entry:

dolichyl-diphosphooligosaccharideprotein glycotransferase. As the enzyme transfers more than one hexosyl group, it has been transferred to EC 2.4.99.18, dolichyl-diphosphooligosaccharideprotein glycotransferase

[EC 2.4.1.119 created 1984, deleted 2012]

2.4.1.120

Accepted name:

sinapate 1-glucosyltransferase

Reaction:

UDP-α-D-glucose + sinapate = UDP + 1-O-sinapoyl-β-D-glucose

Glossary:

sinapate = (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate

Other name(s):

uridine diphosphoglucose-sinapate glucosyltransferase; UDP-glucose:sinapic acid glucosyltransferase; uridine 5′-diphosphoglucose-hydroxycinnamic acid acylglucosyltransferase; UDP-glucose:sinapate D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:sinapate D-glucosyltransferase

Comments:

Some other hydroxycinnamates, including 4-coumarate, ferulate and caffeate, can act as acceptors, but more slowly. Only glucose esters, not glucosides, are formed (cf. EC 2.4.1.126 hydroxycinnamate 4-β-glucosyltransferase).

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 74082-53-4

References:

1.	Strack, D. Enzymatic synthesis of 1-sinapoylglucose from free sinapic acid and UDP-glucose by a cell free system from Raphanus sativus seedlings. Z. Naturforsch. C: Biosci. 35 (1980) 204–208.

[EC 2.4.1.120 created 1984]

2.4.1.121

Accepted name:

indole-3-acetate β-glucosyltransferase

Reaction:

UDP-glucose + (indol-3-yl)acetate = UDP + 1-O-(indol-3-yl)acetyl-β-D-glucose

Other name(s):

uridine diphosphoglucose-indoleacetate glucosyltransferase; UDPG-indol-3-ylacetyl glucosyl transferase; UDP-glucose:indol-3-ylacetate glucosyltransferase; indol-3-ylacetylglucose synthase; UDP-glucose:indol-3-ylacetate glucosyl-transferase; IAGlu synthase; IAA-glucose synthase; UDP-glucose:indole-3-acetate β-D-glucosyltransferase

Systematic name:

UDP-glucose:(indol-3-yl)acetate β-D-glucosyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74082-56-7

References:

1.	Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of 1-O-indol-3-ylacetyl-β-D-glucose and indol-3-ylacetyl-myo-inositol. Biochem. J. 207 (1982) 273–281. [PMID: 6218801]

[EC 2.4.1.121 created 1984]

2.4.1.122

Accepted name:

N-acetylgalactosaminide β-1,3-galactosyltransferase

Reaction:

UDP-α-D-galactose + N-acetyl-α-D-galactosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R

Other name(s):

glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase; uridine diphosphogalactose-mucin β-(1→3)-galactosyltransferase; UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase; UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase; wbnJ (gene name); wbiP (gene name); C1GALT1 (gene name); UDP-α-D-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:N-acetyl-α-D-galactosaminyl-R β-1,3-galactosyltransferase (configuration-inverting)

Comments:

The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-61-7

References:

1.	Hesford, F.J., Berger, E.G. and van den Eijnden, D.H. Identification of the product formed by human erythrocyte galactosyltransferase. Biochim. Biophys. Acta 659 (1981) 302–311. [DOI] [PMID: 6789880]
2.	Mendicino, J., Sivakami, S., Davila, M. and Chandrasekaran, E.V. Purification and properties of UDP-gal:N-acetylgalactosaminide mucin:β1,3-galactosyltransferase from swine trachea mucosa. J. Biol. Chem. 257 (1982) 3987–3994. [PMID: 6801057]
3.	Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
4.	Ju, T., Brewer, K., D'Souza, A., Cummings, R.D. and Canfield, W.M. Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277 (2002) 178–186. [DOI] [PMID: 11677243]
5.	Yi, W., Perali, R.S., Eguchi, H., Motari, E., Woodward, R. and Wang, P.G. Characterization of a bacterial β-1,3-galactosyltransferase with application in the synthesis of tumor-associated T-antigen mimics. Biochemistry 47 (2008) 1241–1248. [DOI] [PMID: 18179256]
6.	Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]

[EC 2.4.1.122 created 1984 (EC 2.4.1.307 created 2013, incorporated 2016), modified 2016]

2.4.1.123

Accepted name:

inositol 3-α-galactosyltransferase

Reaction:

UDP-α-D-galactose + myo-inositol = UDP + O-α-D-galactosyl-(1→3)-1D-myo-inositol

For diagram of stachyose biosynthesis, click here

Glossary:

O-α-D-galactosyl-(1→3)-1D-myo-inositol = galactinol

Other name(s):

UDP-D-galactose:inositol galactosyltransferase; UDP-galactose:myo-inositol 1-α-D-galactosyltransferase; UDPgalactose:myo-inositol 1-α-D-galactosyltransferase; galactinol synthase; inositol 1-α-galactosyltransferase; uridine diphosphogalactose-inositol galactosyltransferase; GolS; UDP-galactose:myo-inositol 3-α-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:myo-inositol 3-α-D-galactosyltransferase

Comments:

An enzyme from plants involved in the formation of raffinose and stachyose [cf. EC 2.4.1.67 (galactinol—raffinose galactosyltransferase) and EC 2.4.1.82 (galactinol—sucrose galactosyltransferase)].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79955-89-8

References:

1.	Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C. Partial characterization of the galactinol forming enzyme from leaves of Cucumis sativus L. Plant Sci. Lett. 23 (1981) 25–33.

[EC 2.4.1.123 created 1984, modified 2003]

2.4.1.124

Transferred entry:

N-acetyllactosamine 3-α-galactosyltransferase. Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase

[EC 2.4.1.124 created 1984, deleted 2002]

2.4.1.125

Accepted name:

sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase

Reaction:

(1) sucrose + [(1→6)-α-D-glucosyl]_n = D-fructose + [(1→6)-α-D-glucosyl]_n+1
(2) sucrose + [(1→6)-α-D-glucosyl]_n = D-fructose + (1→3)-α-D-glucosyl-[(1→6)-α-D-glucosyl]_n

Other name(s):

water-soluble-glucan synthase (misleading); GTF-I; GTF-S; GTF-SI; sucrose-1,6-α-glucan 3(6)-α-glucosyltransferase; sucrose:1,6-α-D-glucan 3-α- and 6-α-glucosyltransferase; sucrose:1,6-, 1,3-α-D-glucan 3-α- and 6-α-D-glucosyltransferase; sucrose:1,6-α-D-glucan 3(6)-α-D-glucosyltransferase; gtfB (gene name); gtfC (gene name); gtfD (gene name)

Systematic name:

sucrose:(1→6)-α-D-glucan 3(6)-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 extends (1→6)-α-D-glucans by both α(1→3) and α(1→6) linkages, with one of the linkage types being dominant. cf. EC 2.4.1.140, alternansucrase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81725-87-3

References:

1.	Mukasa, H., Shimamura, A. and Tsumori, H. Purification and characterization of basic glucosyltransferase from Streptococcus mutans serotype c. Biochim. Biophys. Acta 719 (1982) 81–89. [DOI] [PMID: 6216919]
2.	Shimamura, A., Tsumori, H. and Mukasa, H. Purification and properties of Streptococcus mutans extracellular glucosyltransferase. Biochim. Biophys. Acta 702 (1982) 72–80. [DOI] [PMID: 6461359]
3.	Tsumori, H., Shimamura, A. and Mukasa, H. Purification and properties of extracellular glucosyltransferase synthesizing 1,6-, 1,3-α-D-glucan from Streptococcus mutans serotype a. J. Gen. Microbiol. 131 (1985) 3347–3353. [DOI] [PMID: 2937877]
4.	Fujiwara, T., Tamesada, M., Bian, Z., Kawabata, S., Kimura, S. and Hamada, S. Deletion and reintroduction of glucosyltransferase genes of Streptococcus mutans and role of their gene products in sucrose dependent cellular adherence. Microb Pathog 20 (1996) 225–233. [DOI] [PMID: 8737492]
5.	Monchois, V., Willemot, R.M. and Monsan, P. Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol. Rev. 23 (1999) 131–151. [DOI] [PMID: 10234842]
6.	Ito, K., Ito, S., Shimamura, T., Weyand, S., Kawarasaki, Y., Misaka, T., Abe, K., Kobayashi, T., Cameron, A.D. and Iwata, S. Crystal structure of glucansucrase from the dental caries pathogen Streptococcus mutans. J. Mol. Biol. 408 (2011) 177–186. [DOI] [PMID: 21354427]

[EC 2.4.1.125 created 1984]

2.4.1.126

Accepted name:

hydroxycinnamate 4-β-glucosyltransferase

Reaction:

UDP-glucose + trans-4-hydroxycinnamate = UDP + 4-O-β-D-glucosyl-4-hydroxycinnamate

Other name(s):

uridine diphosphoglucose-hydroxycinnamate glucosyltransferase; UDP-glucose-hydroxycinnamate glucosyltransferase; hydroxycinnamoyl glucosyltransferase

Systematic name:

UDP-glucose:trans-4-hydroxycinnamate 4-O-β-D-glucosyltransferase

Comments:

Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120 sinapate 1-glucosyltransferase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77848-85-2

References:

1.	Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K. Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from tomato fruits. Z. Naturforsch. C: Biosci. 35 (1980) 967–972.

[EC 2.4.1.126 created 1984]

2.4.1.127

Accepted name:

monoterpenol β-glucosyltransferase

Reaction:

UDP-glucose + (-)-menthol = UDP + (-)-menthyl O-β-D-glucoside

For diagram of menthol biosynthesis, click here

Other name(s):

uridine diphosphoglucose-monoterpenol glucosyltransferase; UDPglucose:monoterpenol glucosyltransferase

Systematic name:

UDP-glucose:(-)-menthol O-β-D-glucosyltransferase

Comments:

(+)-Neomenthol can also act as acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78990-64-4

References:

1.	Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K. Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from tomato fruits. Z. Naturforsch. C: Biosci. 35 (1980) 967–972.

[EC 2.4.1.127 created 1984]

2.4.1.128

Accepted name:

scopoletin glucosyltransferase

Reaction:

UDP-glucose + scopoletin = UDP + scopolin

Other name(s):

uridine diphosphoglucose-scopoletin glucosyltransferase; UDP-glucose:scopoletin glucosyltransferase; SGTase

Systematic name:

UDP-glucose:scopoletin O-β-D-glucosyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81210-69-7

References:

1.	Hino, F., Okazaki, M. and Miura, Y. Effect of 2,4-dichlorophenoxyacetic acid on glucosylation of scopoletin to scopolin in tobacco tissue-culture. Plant Physiol. 69 (1982) 810–813. [PMID: 16662301]

[EC 2.4.1.128 created 1984]

2.4.1.129

Transferred entry:

peptidoglycan glycosyltransferase. Now EC 2.4.99.28, peptidoglycan glycosyltransferase

[EC 2.4.1.129 created 1984, modified 2002, deleted 2023]

2.4.1.130

Transferred entry:

dolichyl-phosphate-mannose—glycolipid α-mannosyltransferase. Now covered by EC 2.4.1.258 (Dol-P-Man:Man₅GlcNAc₂-PP-Dol α-1,3-mannosyltransferase), EC 2.4.1.259 (Dol-P-Man:Man₆GlcNAc₂-PP-Dol α-1,2-mannosyltransferase), EC 2.4.1.260 (Dol-P-Man:Man₇GlcNAc₂-PP-Dol α-1,6-mannosyltransferase) and EC 2.4.1.261 (Dol-P-Man:Man₈GlcNAc₂-PP-Dol α-1,2-mannosyltransferase).

[EC 2.4.1.130 created 1984, deleted 2011]

2.4.1.131

Accepted name:

GDP-Man:Man₃GlcNAc₂-PP-dolichol α-1,2-mannosyltransferase

Reaction:

2 GDP-α-D-mannose + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = 2 GDP + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Other name(s):

ALG11; ALG11 mannosyltransferase; LEW3 (gene name); At2G40190 (gene name); gmd3 (gene name); galactomannan deficiency protein 3; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase; glycolipid 2-α-mannosyltransferase; GDP-mannose:glycolipid 2-α-D-mannosyltransferase; GDP-Man:Man₃GlcNAc₂-PP-Dol α-1,2-mannosyltransferase; GDP-α-D-mannose:D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase

Systematic name:

GDP-α-D-mannose:α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-retaining)

Comments:

The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in α(1→2) linkages to the nascent oligosaccharide.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74506-43-7

References:

1.	O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
2.	Absmanner, B., Schmeiser, V., Kampf, M. and Lehle, L. Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an α1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. Biochem. J. 426 (2010) 205–217. [DOI] [PMID: 19929855]
3.	Schutzbach, J.S., Springfield, J.D. and Jensen, J.W. The biosynthesis of oligosaccharide-lipids. Formation of an α-1,2-mannosyl-mannose linkage. J. Biol. Chem. 255 (1980) 4170–4175. [PMID: 6154707]

[EC 2.4.1.131 created 1984, modified 2011, modified 2012]

2.4.1.132

Accepted name:

GDP-Man:Man₁GlcNAc₂-PP-dolichol α-1,3-mannosyltransferase

Reaction:

GDP-α-D-mannose + β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Glossary:

β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = β-D-mannosyl-(1→4)-N,N′-diacetylchitobiosyldiphosphodolichol

Other name(s):

Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man₁GlcNAc₂-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase

Systematic name:

GDP-α-D-mannose:β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-mannosyltransferase (configuration-retaining)

Comments:

The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81181-76-2

References:

1.	Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900–11912. [DOI] [PMID: 19282279]
2.	O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]

[EC 2.4.1.132 created 1984, modified 2011, modified 2012]

2.4.1.133

Accepted name:

xylosylprotein 4-β-galactosyltransferase

Reaction:

UDP-α-D-galactose + [protein]-3-O-(β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine

For diagram of heparan and chondroitin biosynthesis (early stages), click here

Other name(s):

UDP-D-galactose:D-xylose galactosyltransferase; UDP-D-galactose:xylose galactosyltransferase; galactosyltransferase I; uridine diphosphogalactose-xylose galactosyltransferase; UDP-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase; UDP-α-D-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase; UDP-α-D-galactose:O-β-D-xylosyl-[protein] 4-β-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:[protein]-3-O-(β-D-xylosyl)-L-serine 4-β-D-galactosyltransferase (configuration-inverting)

Comments:

Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn²⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52227-72-2

References:

1.	Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200–5207. [PMID: 1150655]
2.	Okajima, T., Yoshida, K., Kondo, T. and Furukawa, K. Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 274 (1999) 22915–22918. [DOI] [PMID: 10438455]

[EC 2.4.1.133 created 1984, modified 2002]

2.4.1.134

Accepted name:

galactosylxylosylprotein 3-β-galactosyltransferase

Reaction:

UDP-α-D-galactose + [protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine

For diagram of heparan and chondroitin biosynthesis (early stages), click here

Other name(s):

galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase; UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase; UDP-α-D-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:[protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine (configuration-inverting)

Comments:

Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn²⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56626-21-2, 56626-19-8

References:

1.	Robinson, J.A. and Robinson, H.C. Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II. Biochem. J. 227 (1985) 805–814. [PMID: 3924029]
2.	Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200–5207. [PMID: 1150655]
3.	Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6). J. Biol. Chem. 276 (2001) 48189–48195. [DOI] [PMID: 11551958]

[EC 2.4.1.134 created 1984, modified 2002]

2.4.1.135

Accepted name:

galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase

Reaction:

UDP-α-D-glucuronate + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine

For diagram of heparan and chondroitin biosynthesis (early 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):

glucuronosyltransferase I; uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-protein D-glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein D-glucuronosyltransferase

Systematic name:

UDP-α-D-glucuronate:[protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine D-glucuronosyltransferase (configuration-inverting)

Comments:

Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn²⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 227184-75-0

References:

1.	Helting, J. and Roden, L. Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region. J. Biol. Chem. 244 (1969) 2799–2805. [PMID: 5770003]
2.	Helting, T. Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma. J. Biol. Chem. 247 (1972) 4327–4332. [PMID: 4260846]
3.	Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, S., Kawasaki, T. and Sugahara, K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273 (1998) 6615–6618. [DOI] [PMID: 9506957]

[EC 2.4.1.135 created 1984, modified 2002, modified 2016]

2.4.1.136

Accepted name:

gallate 1-β-glucosyltransferase

Reaction:

UDP-glucose + gallate = UDP + 1-galloyl-β-D-glucose

Other name(s):

UDP-glucose—vanillate 1-glucosyltransferase; UDPglucose:vanillate 1-O-glucosyltransferase; UDPglucose:gallate glucosyltransferase

Systematic name:

UDP-glucose:gallate β-D-glucosyltransferase

Comments:

A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. Vanillin is the best acceptor investigated.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89700-30-1

References:

1.	Gross, G.G. Synthesis of β-glucogallin from UDP-glucose and gallic acid by an enzyme preparation from oak leaves. FEBS Lett. 148 (1982) 67–70.
2.	Gross, G.G. Partial-purification and properties of UDP-glucose-vanillate 1-O-glucosyl transferase from oak leaves. Phytochemistry 22 (1983) 2179–2182.

[EC 2.4.1.136 created 1984]

2.4.1.137

Accepted name:

sn-glycerol-3-phosphate 2-α-galactosyltransferase

Reaction:

UDP-α-D-galactose + sn-glycerol 3-phosphate = UDP + 2-(α-D-galactosyl)-sn-glycerol 3-phosphate

Other name(s):

floridoside-phosphate synthase; UDP-galactose:sn-glycerol-3-phosphate-2-D-galactosyl transferase; FPS; UDP-galactose,sn-3-glycerol phosphate:1→2′ galactosyltransferase; floridoside phosphate synthetase; floridoside phosphate synthase; UDP-galactose:sn-glycerol-3-phosphate 2-α-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:sn-glycerol-3-phosphate 2-α-D-galactosyltransferase

Comments:

The product is hydrolysed by a phosphatase to floridoside (cf. EC 2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80747-34-8

References:

1.	Gray, N.C.C. and Strickland, K.P. The purification and characterization of a phospholipase A₂ activity from the 106,000 x g pellet (microsomal fraction) of bovine brain acting on phosphatidylinositol. Can. J. Biochem. 60 (1982) 108–117. [PMID: 7083039]

[EC 2.4.1.137 created 1984]

2.4.1.138

Accepted name:

mannotetraose 2-α-N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-D-Man = UDP + α-D-Man-(1→3)-[α-D-GlcNAc-(1→2)]-α-D-Man-(1→2)-α-D-Man-(1→2)-D-Man

Other name(s):

α-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine mannoside α1→2-αcetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:mannotetraose α-N-acetyl-D-glucosaminyltransferase

Systematic name:

UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-D-mannose α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81032-47-5

References:

1.	Douglas, R.H. and Ballou, C.E. Purification of an α-N-acetylglucosaminyltransferase from the yeast Kluyveromyces lactis and a study of mutants defective in this enzyme activity. Biochemistry 21 (1982) 1561–1570. [PMID: 6211189]

[EC 2.4.1.138 created 1984]

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]

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]

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]

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]

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]

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]

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]

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]

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]

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:

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]

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]

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]