The Enzyme Database

Displaying entries 51-100 of 1824.

<< Previous | Next >>    printer_iconPrintable version

EC 2.4.1.174     Relevance: 100%
Accepted name: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of chondroitin biosynthesis (later stages), click here
Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
Other name(s): N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I; UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1→3)-β-D-galactosyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting)
Comments: Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96189-39-8
References:
1.  Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754]
2.  Uyama, T., Kitagawa, H., Tamura, J.-i. and Sugahara, K. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277 (2002) 8841–8846. [DOI] [PMID: 11788602]
[EC 2.4.1.174 created 1989, modified 2002]
 
 
EC 3.2.1.97     Relevance: 99.2%
Accepted name: endo-α-N-acetylgalactosaminidase
Reaction: β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-[glycoprotein]-L-serine/L-threonine + H2O = β-D-galactosyl-(1→3)-N-acetyl-D-galactosamine + [glycoprotein]-L-serine/L-threonine
Other name(s): endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase; endo-α-GalNAc-ase; glycopeptide α-N-acetylgalactosaminidase; D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Systematic name: glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Comments: The enzyme catalyses the liberation of Gal-(1→3)-β-GalNAc α-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1→3)-β-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1→3)-β-(GlcNAc-(1→6)-β)-GalNAc or the core 3 disaccharide GlcNAc-(1→3)-β-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59793-96-3
References:
1.  Ashida, H., Maki, R., Ozawa, H., Tani, Y., Kiyohara, M., Fujita, M., Imamura, A., Ishida, H., Kiso, M. and Yamamoto, K. Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. Glycobiology 18 (2008) 727–734. [DOI] [PMID: 18559962]
2.  Koutsioulis, D., Landry, D. and Guthrie, E.P. Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity. Glycobiology 18 (2008) 799–805. [DOI] [PMID: 18635885]
3.  Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H. and Yamamoto, K. Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biol. Chem. 280 (2005) 37415–37422. [DOI] [PMID: 16141207]
4.  Suzuki, R., Katayama, T., Kitaoka, M., Kumagai, H., Wakagi, T., Shoun, H., Ashida, H., Yamamoto, K. and Fushinobu, S. Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biochem. 146 (2009) 389–398. [DOI] [PMID: 19502354]
5.  Gregg, K.J. and Boraston, A.B. Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 133–135. [DOI] [PMID: 19194003]
6.  Ashida, H., Yamamoto, K., Murata, T., Usui, T. and Kumagai, H. Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity. Arch. Biochem. Biophys. 373 (2000) 394–400. [DOI] [PMID: 10620364]
7.  Goda, H.M., Ushigusa, K., Ito, H., Okino, N., Narimatsu, H. and Ito, M. Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis. Biochem. Biophys. Res. Commun. 375 (2008) 441–446. [DOI] [PMID: 18725192]
[EC 3.2.1.97 created 1978 (EC 3.2.1.110 created 1984, incorporated 2008), modified 2008, modified 2011]
 
 
EC 3.2.1.110      
Deleted entry: mucinaminylserine mucinaminidase. The enzyme is identical to EC 3.2.1.97, glycopeptide α-N-acetylgalactosaminidase
[EC 3.2.1.110 created 1984, deleted 2008]
 
 
EC 2.4.1.82     Relevance: 92.7%
Accepted name: galactinol—sucrose galactosyltransferase
Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + sucrose = myo-inositol + raffinose
For diagram of stachyose biosynthesis, click here
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): 1-α-D-galactosyl-myo-inositol:sucrose 6-α-D-galactosyltransferase; α-D-galactosyl-(1→3)-myo-inositol:sucrose 6-α-D-galactosyltransferase; raffinose synthase; RafS
Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:sucrose 6-α-D-galactosyltransferase
Comments: 4-Nitrophenyl α-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-α-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-45-0
References:
1.  Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [DOI] [PMID: 4774118]
2.  Lehle, L., Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of raffinose. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 1494–1498. [PMID: 5491608]
[EC 2.4.1.82 created 1976, modified 2003]
 
 
EC 2.4.1.73     Relevance: 91.8%
Accepted name: lipopolysaccharide glucosyltransferase II
Reaction: UDP-glucose + lipopolysaccharide = UDP + α-D-glucosyl-lipopolysaccharide
Other name(s): uridine diphosphoglucose-galactosylpolysaccharide glucosyltransferase
Systematic name: UDP-glucose:galactosyl-lipopolysaccharide α-D-glucosyltransferase
Comments: Transfers glucosyl residues to the D-galactosyl-D-glucosyl side-chains in the partially completed core of lipopolysaccharides. cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase), EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51004-27-4
References:
1.  Edstrom, R.D. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. VI. Enzymatic transfer of galactose, glucose, N-acetylglucosamine, and colitose into the polymer. J. Biol. Chem. 242 (1967) 3581–3588. [PMID: 5341482]
[EC 2.4.1.73 created 1972]
 
 
EC 2.4.1.344     Relevance: 89.3%
Accepted name: type 2 galactoside α-(1,2)-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase (ambiguous); α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); H-gene-encoded β-galactoside α(1→2)fucosyltransferase; β-galactoside α(1→2)fucosyltransferase (ambiguous); GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT1 (gene name); FUT2 (gene name)
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)
Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956–2962. [PMID: 804484]
2.  Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351–353.
3.  Ernst, L.K., Rajan, V.P., Larsen, R.D., Ruff, M.M. and Lowe, J.B. Stable expression of blood group H determinants and GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264 (1989) 3436–3447. [PMID: 2464598]
4.  Larsen, R.D., Ernst, L.K., Nair, R.P. and Lowe, J.B. Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc. Natl. Acad. Sci. USA 87 (1990) 6674–6678. [DOI] [PMID: 2118655]
[EC 2.4.1.344 created 2017]
 
 
EC 2.4.1.67     Relevance: 89%
Accepted name: galactinol—raffinose galactosyltransferase
Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + raffinose = myo-inositol + stachyose
For diagram of stachyose biosynthesis, click here
Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside
Other name(s): galactinol-raffinose galactosyltransferase; stachyose synthetase; α-D-galactosyl-(1→3)-myo-inositol:raffinose galactosyltransferase
Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:raffinose galactosyltransferase
Comments: This enzyme also catalyses galactosyl transfer from stachyose to raffinose (shown by labelling) [4]. For synthesis of the substrate, see EC 2.4.1.123, inositol 3-α-galactosyltransferase. See also EC 2.4.1.82, galactinol—sucrose galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-70-6
References:
1.  Tanner, W. Die Biosynthese der Stachyose. Ber. Dtsch. Bot. Ges. 80 (1967) 111.
2.  Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of stachyose. Eur. J. Biochem. 4 (1968) 233–239. [DOI] [PMID: 5655499]
3.  Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [DOI] [PMID: 4774118]
4.  Kandler, O. and Hopf, H. Occurrence, metabolism and function of oligosaccharides. In: Preiss, J. (Ed.), The Biochemistry of Plant, vol. 3, Academic Press, New York, 1980, pp. 221–270.
[EC 2.4.1.67 created 1972, modified 2003]
 
 
EC 2.4.99.4      
Transferred entry: β-galactoside α-2,3-sialyltransferase. Now EC 2.4.3.4, β-galactoside α-2,3-sialyltransferase
[EC 2.4.99.4 created 1984, modified 1986, deleted 2022]
 
 
EC 2.4.1.241     Relevance: 88.2%
Accepted name: digalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): DGD1; DGD2; DGDG synthase (ambiguous); UDP-galactose-dependent DGDG synthase; UDP-galactose-dependent digalactosyldiacylglycerol synthase; UDP-galactose:MGDG galactosyltransferase; UDP-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol 6-α-galactosyltransferase
Comments: Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalysed by EC 2.4.1.46, monogalactosyldiacylglyerol synthase. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids [3]. The enzyme has been localized to the outer side of chloroplast envelope membranes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 69913-00-4
References:
1.  Kelly, A.A. and Dörmann, P. DGD2, an Arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J. Biol. Chem. 277 (2002) 1166–1173. [DOI] [PMID: 11696551]
2.  Härtel, H., Dörmann, P. and Benning, C. DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis. Proc. Natl. Acad. Sci. USA 97 (2000) 10649–10654. [DOI] [PMID: 10973486]
3.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC 2.4.1.241 created 2005]
 
 
EC 2.4.3.8     Relevance: 87.9%
Accepted name: α-N-acetylneuraminate α-2,8-sialyltransferase
Reaction: CMP-N-acetylneuraminate + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R = CMP + α-N-acetylneuraminyl-(2→8)-α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R
For diagram of ganglioside biosynthesis (pathway to GD3), click here
Other name(s): cytidine monophosphoacetylneuraminate-ganglioside GM3; α-2,8-sialyltransferase; ganglioside GD3 synthase; ganglioside GD3 synthetase sialyltransferase; CMP-NeuAc:LM1(α2-8) sialyltranferase; GD3 synthase; SAT-2
Systematic name: CMP-N-acetylneuraminate:α-N-acetylneuraminyl-(2→3)-β-D-galactoside α-(2→8)-N-acetylneuraminyltransferase
Comments: Gangliosides act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67339-00-8
References:
1.  Eppler, M.C., Morré, J.D. and Keenan, T.W. Ganglioside biosynthesis in rat liver: alteration of sialyltransferase activities by nucleotides. Biochim. Biophys. Acta 619 (1980) 332–343. [DOI] [PMID: 7407217]
2.  Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172]
3.  McCoy, R.D., Vimr, E.R. and Troy, F.A. CMP-NeuNAc:poly-α-2,8-sialosyl sialyltransferase and the biosynthesis of polysialosyl units in neural cell adhesion molecules. J. Biol. Chem. 260 (1985) 12695–12699. [PMID: 4044605]
4.  Yohe, H.C. and Yu, R.K. In vitro biosynthesis of an isomer of brain trisialoganglioside, GT1a. J. Biol. Chem. 255 (1980) 608–613. [PMID: 6766128]
[EC 2.4.3.8 created 1984 as EC 2.4.99.8, modified 1986, transferred 2022 to EC 2.4.3.8]
 
 
EC 2.4.99.8      
Transferred entry: α-N-acetylneuraminate α-2,8-sialyltransferase. Now EC 2.4.3.8, α-N-acetylneuraminate α-2,8-sialyltransferase
[EC 2.4.99.8 created 1984, modified 1986, deleted 2022]
 
 
EC 2.4.1.46     Relevance: 87.3%
Accepted name: monogalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose:diacylglycerol galactosyltransferase; MGDG synthase; UDP galactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose-diacylglyceride galactosyltransferase; UDP-galactose:1,2-diacylglycerol 3-β-D-galactosyltransferase; 1β-MGDG; 1,2-diacylglycerol 3-β-galactosyltransferase; UDP-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Comments: This enzyme adds only one galactosyl group to the diacylglycerol; EC 2.4.1.241, digalactosyldiacylglycerol synthase, adds a galactosyl group to the product of the above reaction. There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3). MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-55-7
References:
1.  Veerkamp, J.H. Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus after cell-wall inhibition. VI. Biosynthesis of the galactosyldiglycerides. Biochim. Biophys. Acta 348 (1974) 23–34. [DOI] [PMID: 4838219]
2.  Wenger, D.A., Petipas, J.W. and Pieringer, R.A. The metabolism of glyceride glycolipids. II. Biosynthesis of monogalactosyl diglyceride from uridine diphosphate galactose and diglyceride in brain. Biochemistry 7 (1968) 3700–3707. [PMID: 5681471]
3.  Miège, C., Maréchal, E., Shimojima, M., Awai, K., Block, M.A., Ohta, H., Takamiya, K., Douce, R. and Joyard, J. Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG. Eur. J. Biochem. 265 (1999) 990–1001. [DOI] [PMID: 10518794]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC 2.4.1.46 created 1972, modified 2003, modified 2005]
 
 
EC 3.2.1.102     Relevance: 87.2%
Accepted name: blood-group-substance endo-1,4-β-galactosidase
Reaction: Endohydrolysis of (1→4)-β-D-galactosidic linkages in blood group A and B substances
Other name(s): endo-β-galactosidase (ambiguous); blood-group-substance 1,4-β-D-galactanohydrolase
Systematic name: blood-group-substance 4-β-D-galactanohydrolase
Comments: Hydrolyses the 1,4-β-D-galactosyl linkages adjacent to a 1,3-α-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-α-D-fucosyl residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52720-51-1
References:
1.  Fukuda, M.N. and Matsumara, G. Endo-β-galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratan sulfates, oligosaccharides, and blood group active glycoprotein. J. Biol. Chem. 251 (1976) 6218–6225. [PMID: 135762]
2.  Nakazawa, K. and Suzuki, S. Purification of keratan sulfate-endogalactosidase and its action on keratan sulfates of different origin. J. Biol. Chem. 250 (1975) 912–917. [PMID: 234443]
3.  Takasaki, S. and Kobata, A. Purification and characterization of an endo-β-galactosidase produced by Diplococcus pneumoniae. J. Biol. Chem. 251 (1976) 3603–3609. [PMID: 6459]
[EC 3.2.1.102 created 1984]
 
 
EC 3.2.1.45     Relevance: 85.1%
Accepted name: glucosylceramidase
Reaction: a D-glucosyl-N-acylsphingosine + H2O = D-glucose + a ceramide
For diagram of glycolipid biosynthesis, click here
Glossary: a ceramide = an N-acylsphingosine
Other name(s): psychosine hydrolase; glucosphingosine glucosylhydrolase; GlcCer-β-glucosidase; β-D-glucocerebrosidase; glucosylcerebrosidase; β-glucosylceramidase; ceramide glucosidase; glucocerebrosidase; glucosylsphingosine β-glucosidase; glucosylsphingosine β-D-glucosidase
Systematic name: D-glucosyl-N-acylsphingosine glucohydrolase
Comments: Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37228-64-1
References:
1.  Brady, R.O., Kanfer, J.N. and Shapiro, D. The metabolism of glucocerebrosides. I. Preparation and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J. Biol. Chem. 240 (1966) 39–43. [PMID: 14253443]
2.  Vaccaro, A.M., Muscillo, M. and Suzuki, K. Characterization of human glucosylsphingosine glucosyl hydrolase and comparison with glucosylceramidase. Eur. J. Biochem. 146 (1985) 315–321. [DOI] [PMID: 3967661]
[EC 3.2.1.45 created 1972]
 
 
EC 2.4.1.38     Relevance: 84.5%
Accepted name: β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminylglycopeptide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminylglycopeptide
Other name(s): UDP-galactose—glycoprotein galactosyltransferase; glycoprotein 4-β-galactosyl-transferase; β-N-acetyl-β1-4-galactosyltransferase; thyroid glycoprotein β-galactosyltransferase; glycoprotein β-galactosyltransferase; thyroid galactosyltransferase; uridine diphosphogalactose-glycoprotein galactosyltransferase; β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase; GalT; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide β-1,4-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase
Comments: Terminal N-acetyl-β-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by β-1,6-links to galactose residues; lower activity towards residues linked to galactose by β-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-43-7
References:
1.  Beyer, T.A., Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Glucosyltransferases and their uses in assessing oligosaccharide structure and structure-function relationship. Adv. Enzymol. 52 (1981) 23–175. [PMID: 6784450]
2.  Blanken, W.M., Hooghwinkel, G.J.M. and van den Eijnden, D.H. Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum β-N-acetyl-D-glucosaminide β1→4 galactosyltransferase. Eur. J. Biochem. 127 (1982) 547–552. [DOI] [PMID: 6816588]
3.  Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335]
4.  Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid galactosyltransferase. J. Biol. Chem. 243 (1968) 6529–6537. [PMID: 5726898]
[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986]
 
 
EC 2.4.1.80     Relevance: 83.4%
Accepted name: ceramide glucosyltransferase
Reaction: UDP-α-D-glucose + an N-acylsphingosine = UDP + a β-D-glucosyl-N-acylsphingosine
For diagram of glycolipid biosynthesis, click here
Other name(s): UDP-glucose:ceramide glucosyltransferase; ceramide:UDP-Glc glucosyltransferase; uridine diphosphoglucose-ceramide glucosyltransferase; ceramide:UDP-glucose glucosyltransferase; glucosylceramide synthase; UDP-glucose:N-acylsphingosine D-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acylsphingosine β-D-glucosyltransferase (configuration-inverting)
Comments: Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37237-44-8
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388–1394. [PMID: 4631392]
[EC 2.4.1.80 created 1976]
 
 
EC 2.4.1.330     Relevance: 80.2%
Accepted name: β-D-glucosyl crocetin β-1,6-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + β-D-gentiobiosyl crocetin
(2) UDP-α-D-glucose + bis(β-D-glucosyl) crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl β-D-glucosyl crocetin = UDP + crocin
For diagram of crocin biosynthesis, click here
Glossary: crocin = bis(β-D-gentiobiosyl) crocetin
crocetin = (2E,4E,6E,8E,10E,12E,14E)-2,6,11,15-tetramethylhexadeca-2,4,6,8,10,12,14-heptaenedioate
Other name(s): UGT94E5; UDP-glucose:crocetin glucosyl ester glucosyltransferasee
Systematic name: UDP-α-D-glucose:β-D-glucosyl crocetin β-1,6-glucosyltransferase
Comments: The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271, crocetin glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett. 586 (2012) 1055–1061. [DOI] [PMID: 22569263]
[EC 2.4.1.330 created 2014]
 
 
EC 2.4.1.386     Relevance: 79.8%
Accepted name: GlcNAc-β-1,3-Gal β-1,6-N-acetylglucosaminyltransferase (distally acting)
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Other name(s): UDP-GlcNAc:GlcNAcβ1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase; dIGnT; C2GnT2 (misleading)
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Involved in the production of milk oligosaccharides in the lacto-N-triose (LNT) series. Cf. EC 2.4.1.150 (N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase; cIGnT) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  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]
2.  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 2.4.1.386 created 2021]
 
 
EC 2.4.1.377     Relevance: 79.5%
Accepted name: dTDP-Rha:α-D-Gal-diphosphoundecaprenol α-1,3-rhamnosyltransferase
Reaction: dTDP-β-L-rhamnose + α-D-galactosyl-diphospho-ditrans,octacis-undecaprenol = dTDP + α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaN (gene name); rfbN (gene name)
Systematic name: dTDP-β-L-rhamnose:α-D-galactosyl-diphospho-ditrans,octacis-undecaprenol 3-α-rhamnosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from several Salmonella strains, participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B, D and E groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408–3413. [DOI] [PMID: 7684736]
[EC 2.4.1.377 created 2021]
 
 
EC 2.4.1.28     Relevance: 79.4%
Accepted name: glucosyl-DNA β-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-α-D-glucose to a glucosylhydroxymethylcytosine residue in DNA
Other name(s): T6-glucosyl-HMC-β-glucosyl transferase; T6-β-glucosyl transferase; uridine diphosphoglucose-glucosyldeoxyribonucleate β-glucosyltransferase
Systematic name: UDP-α-D-glucose:D-glucosyl-DNA β-D-glucosyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-15-3
References:
1.  Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193]
[EC 2.4.1.28 created 1965]
 
 
EC 2.4.1.267     Relevance: 78.7%
Accepted name: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG6; Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493–498. [DOI] [PMID: 8877369]
2.  Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412–417. [PMID: 6423630]
3.  Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420–421. [DOI] [PMID: 14517965]
[EC 2.4.1.267 created 2011, modified 2012]
 
 
EC 3.2.1.215     Relevance: 78%
Accepted name: arabinogalactan exo α-(1,3)-α-D-galactosyl-(1→3)-L-arabinofuranosidase (non-reducing end)
Reaction: Hydrolysis of α-D-Galp-(1→3)-L-Araf disaccharides from non-reducing terminals in branches of type II arabinogalactan attached to proteins.
Glossary: Araf = arabinofuranose
Arap = arabinopyranose
Galp = galactopyranose
Other name(s): 3-O-α-D-galactosyl-α-L-arabinofuranosidase
Systematic name: type II arabinogalactan exo α-(1,3)-[α-D-galactosyl-(1→3)-L-arabinofuranose] hydrolase (non-reducing end)
Comments: The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses α-D-Galp-(1→3)-L-Araf disaccharides from the non-reducing terminal of arabinogalactan using an exo mode of action. It is particularly active with gum arabic arabinogalactan, a type II arabinogalactan produced by acacia trees. The enzyme can also hydrolyse β-L-Arap-(1→3)-L-Araf disaccharides, but this activity is significantly lower.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sasaki, Y., Horigome, A., Odamaki, T., Xiao, J.Z., Ishiwata, A., Ito, Y., Kitahara, K. and Fujita, K. Characterization of a novel 3-O-α-D-galactosyl-α-L-arabinofuranosidase for the assimilation of gum arabic AGP in Bifidobacterium longum subsp. longum. Appl. Environ. Microbiol. (2021) . [DOI] [PMID: 33674431]
[EC 3.2.1.215 created 2021]
 
 
EC 2.4.1.265     Relevance: 76.7%
Accepted name: dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG8; Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977–5981. [DOI] [PMID: 8016100]
2.  Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582–15590. [PMID: 3536907]
3.  Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962–9971. [DOI] [PMID: 12480927]
[EC 2.4.1.265 created 2011, modified 2012]
 
 
EC 2.4.1.23     Relevance: 76.7%
Accepted name: sphingosine β-galactosyltransferase
Reaction: UDP-α-D-galactose + sphingosine = UDP + psychosine
Other name(s): psychosine—UDP galactosyltransferase; galactosyl-sphingosine transferase; psychosine-uridine diphosphate galactosyltransferase; UDP-galactose:sphingosine O-galactosyl transferase; uridine diphosphogalactose-sphingosine β-galactosyltransferase; UDP-galactose:sphingosine 1-β-galactotransferase; UDP-galactose:sphingosine 1-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:sphingosine 1-β-galactosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-90-0
References:
1.  Cleland, W.W. and Kennedy, E.P. The enzymatic synthesis of psychosine. J. Biol. Chem. 235 (1960) 45–51. [PMID: 13810623]
[EC 2.4.1.23 created 1965]
 
 
EC 2.3.1.141     Relevance: 76.4%
Accepted name: galactosylacylglycerol O-acyltransferase
Reaction: an acyl-[acyl-carrier protein] + a 2-acyl-3-O-(β-D-galactosyl)-sn-glycerol = an [acyl-carrier protein] + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol
Other name(s): acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase; acyl-ACP:lyso-MGDG acyltransferase; acyl-[acyl-carrier-protein]:D-galactosylacylglycerol O-acyltransferase
Systematic name: acyl-[acyl-carrier protein]:2-acyl-3-O-(β-D-galactosyl)-sn-glycerol O-acyltransferase
Comments: Transfers long-chain acyl groups to the sn-1 position of the glycerol residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119129-68-9
References:
1.  Chen, H.-H., Wickrema, A. and Jaworski, J.G. Acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase from the cyanobacterium Anabaena variabilis. Biochim. Biophys. Acta 963 (1988) 493–500. [DOI] [PMID: 3143419]
[EC 2.3.1.141 created 1992]
 
 
EC 2.4.1.256     Relevance: 74.5%
Accepted name: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = dolichyl phosphate + α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-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): ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase (configuration-retaining)
Comments: This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455–462. [DOI] [PMID: 9597543]
[EC 2.4.1.256 created 2011, modified 2012]
 
 
EC 2.4.1.388     Relevance: 73.1%
Accepted name: glucosylgalactose phosphorylase
Reaction: β-D-glucosyl-(1→4)-D-galactose + phosphate = α-D-glucopyranose 1-phosphate + D-galactopyranose
Other name(s): 4-O-β-D-glucosyl-D-galactose phosphorylase
Systematic name: β-D-glucosyl-(1→4)-D-galactose:phosphate α-D-glucosyltransferase (configuration-inverting)
Comments: The enzyme from the bacterium Paenibacillus polymyxa belongs to glycoside hydrolase family 94. It has a much lower activity with 4-O-β-D-glucosyl-L-arabinose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  De Doncker, M., De Graeve, C., Franceus, J., Beerens, K., Kren, V., Pelantova, H., Vercauteren, R. and Desmet, T. Exploration of GH94 sequence space for enzyme discovery reveals a novel glucosylgalactose phosphorylase specificity. ChemBioChem (2021) . [DOI] [PMID: 34541742]
[EC 2.4.1.388 created 2022]
 
 
EC 2.4.1.391     Relevance: 73%
Accepted name: β-1,2-glucosyltransferase
Reaction: [(1→2)-β-D-glucosyl]n + a D-glucoside = [(1→2)-β-D-glucosyl]n-1 + a β-D-glucosyl-(1→2)-D-glucoside
Systematic name: 1,2-β-D-glucan:D-glucoside 2-β-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme, characterized from the bacterium Ignavibacterium album, transfers a glucosyl residue from the non-reducing end of a 1,2-β-D-glucan to a glucose residue of an acceptor molecule, forming a β(1,2) linkage. The donor molecule can be as small as sophorose (which contains two glucosyl residues). The enzyme has a very broad specificity for the acceptor, and can act on various aryl- and alkyl-glucosides. In addition, the accepting glucose unit can be in either α or β configuration.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kobayashi, K., Shimizu, H., Tanaka, N., Kuramochi, K., Nakai, H., Nakajima, M. and Taguchi, H. Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages. J. Biol. Chem. 298:101606 (2022). [DOI] [PMID: 35065074]
[EC 2.4.1.391 created 2022]
 
 
EC 2.4.1.27     Relevance: 72.6%
Accepted name: DNA β-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-α-D-glucose to an hydroxymethylcytosine residue in DNA
Other name(s): T4-HMC-β-glucosyl transferase; T4-β-glucosyl transferase; T4 phage β-glucosyltransferase; UDP glucose-DNA β-glucosyltransferase; uridine diphosphoglucose-deoxyribonucleate β-glucosyltransferase; UDP-glucose:DNA β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:DNA β-D-glucosyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-14-2
References:
1.  Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193]
[EC 2.4.1.27 created 1965]
 
 
EC 2.3.1.173     Relevance: 72.3%
Accepted name: flavonol-3-O-triglucoside O-coumaroyltransferase
Reaction: 4-coumaroyl-CoA + a flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] = CoA + a flavonol 3-O-[6-(4-coumaroyl)-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside]
For diagram of kaempferol-glycoside biosynthesis, click here
Other name(s): 4-coumaroyl-CoA:flavonol-3-O-[β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase (incorrect)
Systematic name: 4-coumaroyl-CoA:flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase
Comments: Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit, almost certainly at C-6.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64972-79-8
References:
1.  Saylor, M.H. and Mansell, R.L. Hydroxycinnamoyl:coenzyme A transferase involved in the biosynthesis of kaempferol-3-(p-coumaroyl triglucoside) in Pisum sativum. Z. Naturforsch. 32 (1977) 765–768. [PMID: 145116]
[EC 2.3.1.173 created 2004]
 
 
EC 3.2.1.123     Relevance: 72.2%
Accepted name: endoglycosylceramidase
Reaction: oligoglycosylglucosyl-(1↔1)-ceramide + H2O = ceramide + oligoglycosylglucose
Other name(s): endoglycoceramidase; EGCase; glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase; oligoglycosylglucosylceramide glycohydrolase; oligoglycosylglucosyl(1↔1)ceramide glycohydrolase
Systematic name: oligoglycosylglucosyl-(1↔1)-ceramide glycohydrolase
Comments: An enzyme from Rhodococcus sp. that degrades various acidic and neutral glycosphingolipids to oligosaccharides and ceramides, by cleaving a glucosyl bond. Does not act on monoglycosylceramides. cf. EC 3.2.1.62 glycosylceramidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105503-61-5
References:
1.  Ito, M. and Yamagata, T. A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids. J. Biol. Chem. 261 (1986) 14278–14282. [PMID: 3771534]
[EC 3.2.1.123 created 1989]
 
 
EC 2.4.2.42     Relevance: 71.6%
Accepted name: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase
Reaction: UDP-α-D-xylose + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine
Other name(s): β-glucoside α-1,3-xylosyltransferase; UDP-α-D-xylose:β-D-glucoside 3-α-D-xylosyltransferase; GXYLT1 (gene name); GXYLT2 (gene name)
Systematic name: UDP-α-D-xylose:[protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine 3-α-D-xylosyltransferase (configuration-retaining)
Comments: The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains [2,3]. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143–146. [DOI] [PMID: 9128735]
2.  Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593–600. [DOI] [PMID: 17317689]
3.  Sethi, M.K., Buettner, F.F., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Identification of glycosyltransferase 8 family members as xylosyltransferases acting on O-glucosylated notch epidermal growth factor repeats. J. Biol. Chem. 285 (2010) 1582–1586. [PMID: 19940119]
[EC 2.4.2.42 created 2010, modified 2020]
 
 
EC 2.4.1.271     Relevance: 70.3%
Accepted name: crocetin glucosyltransferase
Reaction: (1) UDP-α-D-glucose + crocetin = UDP + β-D-glucosyl crocetin
(2) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + bis(β-D-glucosyl) crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
For diagram of crocin biosynthesis, click here
Other name(s): crocetin GTase; UGTCs2; UGT75L6; UDP-glucose:crocetin glucosyltransferase; UDP-glucose:crocetin 8-O-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:crocetin 8-O-D-glucosyltransferase
Comments: In the plants Crocus sativus and Gardenia jasminoides this enzyme esterifies a free carboxyl group of crocetin and some crocetin glycosyl esters. The enzyme from Gardenia can also form glucosyl esters with 4-coumarate, caffeate and ferulate [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Côté, F., Cormier, F., Dufresne, C. and Willemot, C. Properties of a glucosyltransferase involved in crocin synthesis. Plant Sci. 153 (2000) 55–63.
2.  Moraga, A.R., Nohales, P.F., Perez, J.A. and Gomez-Gomez, L. Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta 219 (2004) 955–966. [DOI] [PMID: 15605174]
3.  Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett. 586 (2012) 1055–1061. [DOI] [PMID: 22569263]
[EC 2.4.1.271 created 2011]
 
 
EC 2.4.2.62     Relevance: 70%
Accepted name: xylosyl α-1,3-xylosyltransferase
Reaction: UDP-α-D-xylose + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine
Other name(s): XXYLT1 (gene name)
Systematic name: UDP-α-D-xylose:[EGF-like domain protein]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine 3-α-D-xylosyltransferase (configuration-retaining)
Comments: The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S. and Hase, S. Detection of UDP-D-xylose: α-D-xyloside α 1-→3xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. 120 (1996) 1002–1006. [PMID: 8982869]
2.  Sethi, M.K., Buettner, F.F., Ashikov, A., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch. J. Biol. Chem. 287 (2012) 2739–2748. [PMID: 22117070]
3.  Yu, H., Takeuchi, M., LeBarron, J., Kantharia, J., London, E., Bakker, H., Haltiwanger, R.S., Li, H. and Takeuchi, H. Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. Nat. Chem. Biol. 11 (2015) 847–854. [PMID: 26414444]
[EC 2.4.2.62 created 2020]
 
 
EC 2.4.1.133     Relevance: 69.4%
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]
 
 
EC 3.2.1.164     Relevance: 68.7%
Accepted name: galactan endo-1,6-β-galactosidase
Reaction: Endohydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield galactose and (1→6)-β-galactobiose as the final products
Other name(s): endo-1,6-β-galactanase
Systematic name: endo-β-(1→6)-galactanase
Comments: The enzyme specifically hydrolyses 1,6-β-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals [2]. 1,3-β-D- and 1,4-β-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse α-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots [2,3]. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brillouet, J.-M., Williams, P. and Moutounet, M. Purification and some properties of a novel endo-β-(1→6)-D-galactanase from Aspergillus niger. Agric. Biol. Chem. 55 (1991) 1565–1571.
2.  Okemoto, K., Uekita, T., Tsumuraya, Y., Hashimoto, Y. and Kasama, T. Purification and characterization of an endo-β-(1→6)-galactanase from Trichoderma viride. Carbohydr. Res. 338 (2003) 219–230. [DOI] [PMID: 12543554]
3.  Kotake, T., Kaneko, S., Kubomoto, A., Haque, M.A., Kobayashi, H. and Tsumuraya, Y. Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-β-(1→6)-galactanase gene. Biochem. J. 377 (2004) 749–755. [DOI] [PMID: 14565843]
[EC 3.2.1.164 created 2007]
 
 
EC 2.4.1.122     Relevance: 68.4%
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]
 
 
EC 2.4.1.148     Relevance: 68.4%
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→3)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-mucin β(1→6)-acetylglucosaminyltransferase B; core 4 β6-GalNAc-transferase; core 6β-GalNAc-transferase B; UDP-N-acetyl-D-glucosamine:O-oligosaccharide-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of N-acetyl-β-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R 6-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
[EC 2.4.1.148 created 1984]
 
 
EC 2.4.1.392     Relevance: 68.3%
Accepted name: 3-O-β-D-glucopyranosyl-β-D-glucuronide phosphorylase
Reaction: a 3-O-β-D-glucosyl-β-D-glucuronoside + phosphate = a β-D-glucuronoside + α-D-glucopyranose 1-phosphate
Other name(s): PBOR_13355 (locus name)
Systematic name: 3-O-β-D-glucopyranosyl-β-D-glucuronide:phosphate α-D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Paenibacillus borealis, catalyses a reversible reaction, transferring a glucosyl residue attached by a β(1,3) linkage to a D-glucuronate residue (either free or as a part of a β-D-glucuronide) to a free phosphate, generating α-D-glucopyranose 1-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Isono, N., Mizutani, E., Hayashida, H., Katsuzaki, H. and Saburi, W. Functional characterization of a novel GH94 glycoside phosphorylase, 3-O-β-D-glucopyranosyl β-D-glucuronide phosphorylase, and implication of the metabolic pathway of acidic carbohydrates in Paenibacillus borealis. Biochem. Biophys. Res. Commun. 625 (2022) 60–65. [DOI] [PMID: 35947916]
[EC 2.4.1.392 created 2022]
 
 
EC 2.4.1.341     Relevance: 67.9%
Accepted name: α-1,2-colitosyltransferase
Reaction: GDP-β-L-colitose + β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = GDP + α-L-colitosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-D-glucosamine
Glossary: β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = lacto-N-biose
Other name(s): wbgN (gene name)
Systematic name: GDP-β-L-colitose:β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine L-colitosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the bacterium Escherichia coli O55:H7, participates in the biosynthesis of an O-antigen. The reaction involves anomeric inversion, and does not require any metal ions. The enzyme is highly specific towards the acceptor, exclusively recognizing lacto-N-biose, but can accept GDP-L-fucose as the donor with almost the same activity as with GDP-β-L-colitose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wu, Z., Zhao, G., Li, T., Qu, J., Guan, W., Wang, J., Ma, C., Li, X., Zhao, W., Wang, P.G. and Li, L. Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. Glycobiology (2015) . [DOI] [PMID: 26703456]
[EC 2.4.1.341 created 2016]
 
 
EC 2.4.1.97     Relevance: 67.2%
Accepted name: 1,3-β-D-glucan phosphorylase
Reaction: [(1→3)-β-D-glucosyl]n + phosphate = [(1→3)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Other name(s): laminarin phosphoryltransferase; 1,3-β-D-glucan:orthophosphate glucosyltransferase; 1,3-β-D-glucan:phosphate α-D-glucosyltransferase
Systematic name: (1→3)-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: Acts on a range of β-1,3-oligoglucans, and on glucans of laminarin type. Different from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.31 (laminaribiose phosphorylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37340-31-1
References:
1.  Albrecht, G.J. and Kauss, H. Purification, crystallization and properties of a β-(1→3)-glucan phosphorylase from Ochromonas malhamensis. Phytochemistry 10 (1971) 1293–1298.
[EC 2.4.1.97 created 1978]
 
 
EC 2.3.1.213     Relevance: 67.2%
Accepted name: cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase
Reaction: 1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside]
For diagram of cyanidin galactoside biosynthesis, click here
Glossary: 1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase
Systematic name: 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582–585. [PMID: 24186789]
[EC 2.3.1.213 created 2013]
 
 
EC 2.4.1.333     Relevance: 67.2%
Accepted name: 1,2-β-oligoglucan phosphorylase
Reaction: [(1→2)-β-D-glucosyl]n + phosphate = [(1→2)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Systematic name: 1,2-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1→2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nakajima, M., Toyoizumi, H., Abe, K., Nakai, H., Taguchi, H. and Kitaoka, M. 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One 9:e92353 (2014). [DOI] [PMID: 24647662]
[EC 2.4.1.333 created 2014]
 
 
EC 2.4.1.375     Relevance: 66.8%
Accepted name: rhamnogalacturonan I galactosyltransferase
Reaction: Transfer of a β-galactosyl residue in a β-(1→4) linkage from UDP-α-D-galactose to rhamnosyl residues within the rhamnogalacturonan I backbone.
Glossary: rhamnogalacturonan I backbone = [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl]n
Systematic name: UDP-α-D-galactose:[rhamnogalacturonan I]-α-L-rhamnosyl β-1,4-galactosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the plant Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan I, one of the components of pectin in plant cell wall. It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 9.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Matsumoto, N., Takenaka, Y., Wachananawat, B., Kajiura, H., Imai, T. and Ishimizu, T. Rhamnogalacturonan I galactosyltransferase: Detection of enzyme activity and its hyperactivation. Plant Physiol. Biochem. 142 (2019) 173–178. [DOI] [PMID: 31299599]
[EC 2.4.1.375 created 2020]
 
 
EC 2.4.1.49     Relevance: 66.5%
Accepted name: cellodextrin phosphorylase
Reaction: [(1→4)-β-D-glucosyl]n + phosphate = [(1→4)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Other name(s): β-1,4-oligoglucan:orthophosphate glucosyltransferase; 1,4-β-D-oligo-D-glucan:phosphate α-D-glucosyltransferase
Systematic name: (1→4)-β-D-glucan:phosphate α-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-58-0
References:
1.  Sheth, K. and Alexander, J.K. Purification and properties of β-1,4-oligoglucan:orthophosphate glucosyltransferase from Clostridium thermocellum. J. Biol. Chem. 244 (1969) 457–464. [PMID: 5773308]
[EC 2.4.1.49 created 1972]
 
 
EC 3.2.1.130     Relevance: 66.5%
Accepted name: glycoprotein endo-α-1,2-mannosidase
Reaction: GlcMan9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + α-D-glucosyl-(1→3)-α-D-mannopyranose
Glossary: GlcMan9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-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]
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) = {α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-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): glucosylmannosidase; endo-α-D-mannosidase; endo-α-mannosidase; endomannosidase; glucosyl mannosidase; MANEA (gene name); glycoprotein glucosylmannohydrolase
Systematic name: glycoprotein glucosylmannohydrolase (configuration-retaining)
Comments: The enzyme catalyses the hydrolysis of the terminal α-D-glucosyl-(1→3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus. The name for the isomer is based on a nomenclature proposed by Prien et al [7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 108022-16-8
References:
1.  Lubas, W.A. and Spiro, R.G. Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem. 262 (1987) 3775–3781. [PMID: 3818665]
2.  Tulsiani, D.R.P., Coleman, V.P. and Touster, O. Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and endomannosidase (glucosyl mannosidase). Arch. Biochem. Biophys. 277 (1990) 114–121. [DOI] [PMID: 2407194]
3.  Hiraizumi, S., Spohr, U. and Spiro, R.G. Ligand affinity chromatographic purification of rat liver Golgi endomannosidase. J. Biol. Chem. 269 (1994) 4697–4700. [PMID: 8106437]
4.  Spiro, M.J., Bhoyroo, V.D. and Spiro, R.G. Molecular cloning and expression of rat liver endo-α-mannosidase, an N-linked oligosaccharide processing enzyme. J. Biol. Chem. 272 (1997) 29356–29363. [DOI] [PMID: 9361017]
5.  Hamilton, S.R., Li, H., Wischnewski, H., Prasad, A., Kerley-Hamilton, J.S., Mitchell, T., Walling, A.J., Davidson, R.C., Wildt, S. and Gerngross, T.U. Intact α-1,2-endomannosidase is a typical type II membrane protein. Glycobiology 15 (2005) 615–624. [DOI] [PMID: 15677381]
6.  Hardt, B., Volker, C., Mundt, S., Salska-Navarro, M., Hauptmann, M. and Bause, E. Human endo-α1,2-mannosidase is a Golgi-resident type II membrane protein. Biochimie 87 (2005) 169–179. [DOI] [PMID: 15760709]
7.  Prien, J.M., Ashline, D.J., Lapadula, A.J., Zhang, H. and Reinhold, V.N. The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS. J. Am. Soc. Mass Spectrom. 20 (2009) 539–556. [DOI] [PMID: 19181540]
[EC 3.2.1.130 created 1990, modified 2017]
 
 
EC 2.5.1.98     Relevance: 66%
Accepted name: Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase
Reaction: phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→3)-4,6-CH3(COO-)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n + phosphate
Other name(s): PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Systematic name: phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase
Comments: The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae—Pisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731–742. [DOI] [PMID: 20233262]
[EC 2.5.1.98 created 2012, modified 2018]
 
 
EC 2.4.1.240     Relevance: 65.5%
Accepted name: flavonol-3-O-glycoside glucosyltransferase
Reaction: UDP-glucose + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside
For diagram of kaempferol-glycoside biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-triglucoside, click here
Systematic name: UDP-glucose:flavonol-3-O-β-D-glucosyl-(1→2)-β-D-glucoside 2′′′-O-β-D-glucosyltransferase
Comments: One of three specific glucosyltransferases in pea (Pisum sativum) thatsuccessively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 flavonol 3-O-glucosyltransferase, and EC 2.4.1.239 flavonol-3-O-glucoside glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434–443. [DOI] [PMID: 6462109]
[EC 2.4.1.240 created 2004]
 
 
EC 2.4.1.31     Relevance: 65.1%
Accepted name: laminaribiose phosphorylase
Reaction: 3-β-D-glucosyl-D-glucose + phosphate = D-glucose + α-D-glucose 1-phosphate
Systematic name: 3-β-D-glucosyl-D-glucose:phosphate α-D-glucosyltransferase
Comments: Also acts on 1,3-β-D-oligoglucans. Differs in specificity from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-29-7
References:
1.  Goldemberg, S.H., Maréchal, L.R. and De Souza, B.C. β-1,3-Oligoglucan: orthophosphate glucosyltransferase from Euglena gracilis. J. Biol. Chem. 241 (1966) 45–50. [PMID: 5901055]
2.  Manners, D.J. and Taylor, D.C. Studies on carbohydrate metabolizing enzymes. XVI. Specificity of laminaribiose phosphorylase from Astasia ocellata. Arch. Biochem. Biophys. 121 (1967) 443–451. [DOI] [PMID: 6057111]
[EC 2.4.1.31 created 1972]
 
 
EC 2.4.1.30     Relevance: 64.7%
Accepted name: 1,3-β-oligoglucan phosphorylase
Reaction: [(1→3)-β-D-glucosyl]n + phosphate = [(1→3)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate
Other name(s): β-1,3-oligoglucan:orthophosphate glucosyltransferase II; β-1,3-oligoglucan phosphorylase; 1,3-β-D-oligoglucan:phosphate α-D-glucosyltransferase
Systematic name: (1→3)-β-D-glucan:phosphate α-D-glucosyltransferase
Comments: Does not act on laminarin. Differs in specificity from EC 2.4.1.31 (laminaribiose phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-28-6
References:
1.  Maréchal, L.R. β-1,3-Oligoglucan:orthophosphate glucosyltransferases from Euglena gracilis. I. Isolation and some properties of a β-1,3-oligoglucan phosphorylase. Biochim. Biophys. Acta 146 (1967) 417–430. [DOI] [PMID: 6066291]
2.  Maréchal, L.R. β-1,3-Oligoglucan: orthophosphate glucosyltransferases from Euglena gracilis. II. Comparative studies between laminaribiose- and β-1,3-oligoglucan phosphorylase. Biochim. Biophys. Acta 146 (1967) 431–442. [DOI] [PMID: 6066292]
[EC 2.4.1.30 created 1972]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald