EC |
2.4.3.1 |
Accepted name: |
β-galactoside α-(2,6)-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + β-D-galactosyl-R = CMP + N-acetyl-α-neuraminyl-(2→6)-β-D-galactosyl-R |
Other name(s): |
ST6Gal-I; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; lactosylceramide α-2,6-N-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine α-(2→6)-N-acetylneuraminyltransferase; β-galactoside α-2,6-sialyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:β-D-galactoside α-(2→6)-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9075-81-4 |
References: |
1. |
Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520–6528. [PMID: 5726897] |
2. |
Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759–766. [PMID: 4313609] |
3. |
Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751–5762. [PMID: 4723915] |
4. |
Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356–2362. [PMID: 849932] |
5. |
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] |
6. |
Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559–565. [PMID: 2460092] |
|
[EC 2.4.3.1 created 1972 as EC 2.4.99.1, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2016), modified 2017, transferred 2021 to EC 2.4.3.1] |
|
|
|
|
EC |
2.4.3.2 |
Accepted name: |
β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R = CMP + an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R |
|
For diagram of ganglioside biosynthesis, click here |
Glossary: |
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GD1a |
Other name(s): |
CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase (ambiguous); monosialoganglioside sialyltransferase; CMP-N-acetylneuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide N-acetyl-β-neuraminyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R α-(2→3)-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme recognizes the sequence β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 60202-12-2 |
References: |
1. |
Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198] |
2. |
Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [DOI] [PMID: 4351506] |
|
[EC 2.4.3.2 created 1976 as EC 2.4.99.2, modified 1986, modified 2017, transferred 2022 to EC 2.4.3.2] |
|
|
|
|
EC |
2.4.3.3 |
Accepted name: |
α-N-acetylgalactosaminide α-2,6-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + glycano-(1→3)-(N-acetyl-α-D-galactosaminyl)-glycoprotein = CMP + glycano-[(2→6)-α-N-acetylneuraminyl]-(N-acetyl-D-galactosaminyl)-glycoprotein |
Systematic name: |
CMP-N-acetylneuraminate:glycano-1,3-(N-acetyl-α-D-galactosaminyl)-glycoprotein α-2,6-N-acetylneuraminyltransferase |
Comments: |
N-acetyl-α-D-galactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 71124-50-0 |
References: |
1. |
Sadler, J.E., Rearick, J.I. and Hill, R.L. Purification to homogeneity and enzymatic characterization of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 5934–5941. [PMID: 447688] |
|
[EC 2.4.3.3 created 1984 as EC 2.4.99.3, modified 1986, transferred 2022 to EC 2.4.3.3] |
|
|
|
|
EC |
2.4.3.4 |
Accepted name: |
β-galactoside α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R |
Other name(s): |
CMP-N-acetylneuraminate:β-D-galactoside α-2,3-N-acetylneuraminyl-transferase |
Systematic name: |
CMP-N-acetylneuraminate:β-D-galactoside α-(2→3)-N-acetylneuraminyl-transferase |
Comments: |
The acceptor is Galβ1,3GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid. Lactose can also act as acceptor. May be identical with EC 2.4.3.2 β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 71124-51-1 |
References: |
1. |
Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198] |
2. |
Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Purification to homogeneity of a β-galactoside α2→3 sialyltransferase and partial purification of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 4434–4442. [PMID: 438196] |
|
[EC 2.4.3.4 created 1984 as EC 2.4.99.4, modified 1986, transferred 2022 to EC 2.4.3.4] |
|
|
|
|
EC |
2.4.3.5 |
Accepted name: |
galactosyldiacylglycerol α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + 1,2-diacyl-3-β-D-galactosyl-sn-glycerol = CMP + 1,2-diacyl-3-[3-(N-acetyl-α-D-neuraminyl)-β-D-galactosyl]-sn-glycerol |
Systematic name: |
CMP-N-acetyl-β-neuraminate:1,2-diacyl-3-β-D-galactosyl-sn-glycerol N-acetylneuraminyltransferase |
Comments: |
The β-D-galactosyl residue of the oligosaccharide of glycoproteins may also act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80237-98-5 |
References: |
1. |
Pieringer, J., Keech, S. and Pieringer, R.A. Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse brain microsomes. J. Biol. Chem. 256 (1981) 12306–12309. [PMID: 7298658] |
2. |
Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. Purification of a Gal β1→4GlcNAc α2→6 sialyltransferase and a Gal β1→3(4)GlcNAc α2→3 sialyltransferase to homogeneity from rat liver. J. Biol. Chem. 257 (1982) 13835–13844. [PMID: 7142179] |
3. |
Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal β1→3(4)GlcNAc α2→3 sialyltransferase and a Gal β1→4GlcNAc α2→6 sialyltransferase from rat liver. J. Biol. Chem. 257 (1982) 13845–13853. [PMID: 7142180] |
|
[EC 2.4.3.5 created 1984 as EC 2.4.99.5, modified 1986, transferred 2022 to EC 2.4.3.5] |
|
|
|
|
EC |
2.4.3.6 |
Accepted name: |
N-acetyllactosaminide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R |
Other name(s): |
cytidine monophosphoacetylneuraminate-β-galactosyl(1→4)acetylglucosaminide α2→3-sialyltransferase; α2→3 sialyltransferase (ambiguous); SiaT (ambiguous); CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein α-2,3-N-acetylneuraminyltransferase; neolactotetraosylceramide α-2,3-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-glycoprotein α-(2→3)-N-acetylneuraminyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R (2→3)-N-acetyl-α-neuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme recognizes the sequence β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl (known as type 2 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids. The enzyme from chicken brain was shown to act on neolactotetraosylceramide, producing ganglioside LM1 [2]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 77537-85-0 |
References: |
1. |
Van den Eijnden, D.H. and Schiphorst, W.E.C.M. Detection of β-galactosyl(1→4)N-acetylglucosaminide α(2→3)-sialyltransferase activity in fetal calf liver and other tissues. J. Biol. Chem. 256 (1981) 3159–3162. [PMID: 7204397] |
2. |
Basu, M., Basu, S., Stoffyn, A. and Stoffyn, P. Biosynthesis in vitro of sialyl(α2-3)neolactotetraosylceramide by a sialyltransferase from embryonic chicken brain. J. Biol. Chem. 257 (1982) 12765–12769. [PMID: 7130178] |
|
[EC 2.4.3.6 created 1984 as EC 2.4.99.6, modified 1986 (EC 2.4.99.10 created 1986, incorporated 2017), transferred 2022 to EC 2.4.3.6] |
|
|
|
|
EC |
2.4.3.7 |
Accepted name: |
α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-D-galactosaminyl-R |
|
For diagram of reaction, click here |
Other name(s): |
sialyltransferase; cytidine monophosphoacetylneuraminate-(α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetylgalactosaminide-α-2,6-sialyltransferase; α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetyl-galactosaminide α-2,6-sialyltransferase; SIAT7; ST6GALNAC; (α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetyl-galactosaminide 6-α-sialyltransferase; CMP-N-acetylneuraminate:(α-N-acetylneuraminyl-2,3-β-D-galactosyl-1,3)-N-acetyl-D-galactosaminide α-2,6-N-acetylneuraminyl-transferase |
Systematic name: |
CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)- N-acetyl-D-galactosaminide galactosamine-6-α-N-acetylneuraminyltransferase |
Comments: |
Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetylgalactosamine only when present in the structure of α-N-acetylneuraminyl-(2→3)-β-galactosyl-(1→3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.3.3 α-N-acetylgalactosaminide α-2,6-sialyltransferase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 129924-24-9 |
References: |
1. |
Bergh, M.L.E., Hooghwinkel, G.J.M. and Van den Eijnden, D.H. Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an α-N-acetylgalactosaminide α2→6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. J. Biol. Chem. 258 (1983) 7430–7436. [PMID: 6190802] |
|
[EC 2.4.3.7 created 1984 as EC 2.4.99.7, modified 1986, modified 2004, transferred 2022 to EC 2.4.3.7] |
|
|
|
|
EC |
2.4.3.8 |
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, Gene, KEGG, MetaCyc, PDB, 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 |
2.4.3.9 |
Accepted name: |
lactosylceramide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
|
For diagram of ganglioside biosynthesis (pathway to GM2), click here |
Glossary: |
lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
Other name(s): |
cytidine monophosphoacetylneuraminate-lactosylceramide α2,3- sialyltransferase; CMP-acetylneuraminate-lactosylceramide-sialyltransferase; CMP-acetylneuraminic acid:lactosylceramide sialyltransferase; CMP-sialic acid:lactosylceramide-sialyltransferase; cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase; ganglioside GM3 synthetase; GM3 synthase; GM3 synthetase; SAT 1; CMP-N-acetylneuraminate:lactosylceramide α-2,3-N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide α-(2→3)-N-acetylneuraminyltransferase |
Systematic name: |
CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-(2→3)-N-acetylneuraminyltransferase |
Comments: |
Lactose cannot act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 125752-90-1 |
References: |
1. |
Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388–1394. [PMID: 4631392] |
2. |
Fishman, P.H., Bradley, R.M. and Henneberry, R.C. Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase. Arch. Biochem. Biophys. 172 (1976) 618–626. [DOI] [PMID: 4022] |
3. |
Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172] |
|
[EC 2.4.3.9 created 1984 as EC 2.4.99.9, modified 1986, transferred 2022 to EC 2.4.3.9] |
|
|
|
|
EC |
2.4.3.10 |
Accepted name: |
N-acetylglucosaminide α-(2,6)-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-β-D-glucosaminyl-R |
Other name(s): |
α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylglucosaminide 6-α-sialyltransferase; N-acetylglucosaminide (α 2→6)-sialyltransferase; ST6GlcNAc |
Systematic name: |
CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminide N-acetyl-β-D-glucosamine-6-α-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetyl-β-D-glucosamine. The enzyme from rat liver also acts on β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl residues, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Paulson, J.C., Weinstein, J. and de Souza-e-Silva, U. Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (α 2→6)-sialyltransferase in Golgi apparatus from rat liver. Eur. J. Biochem. 140 (1984) 523–530. [PMID: 6547092] |
|
[EC 2.4.3.10 created 2020 as EC 2.4.99.22, transferred 2022 to EC 2.4.3.10] |
|
|
|
|