KEGG   ENZYME: 2.4.3.5
Entry
EC 2.4.3.5                  Enzyme                                 
Name
galactosyldiacylglycerol alpha-2,3-sialyltransferase
Class
Transferases;
Glycosyltransferases;
Sialyltransferases
Sysname
CMP-N-acetyl-beta-neuraminate:1,2-diacyl-3-beta-D-galactosyl-sn-glycerol N-acetylneuraminyltransferase
Reaction(IUBMB)
CMP-N-acetyl-beta-neuraminate + 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol = CMP + 1,2-diacyl-3-[3-(N-acetyl-alpha-D-neuraminyl)-beta-D-galactosyl]-sn-glycerol [RN:R03468]
Reaction(KEGG)
R03468
Substrate
CMP-N-acetyl-beta-neuraminate [CPD:C00128];
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol [CPD:C03692]
Product
CMP [CPD:C00055];
1,2-diacyl-3-[3-(N-acetyl-alpha-D-neuraminyl)-beta-D-galactosyl]-sn-glycerol
Comment
The beta-D-galactosyl residue of the oligosaccharide of glycoproteins may also act as acceptor.
History
EC 2.4.3.5 created 1984 as EC 2.4.99.5, modified 1986, transferred 2022 to EC 2.4.3.5
Pathway
ec00561  Glycerolipid metabolism
Reference
1  [PMID:7298658]
  Authors
Pieringer J, Keech S, Pieringer RA.
  Title
Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse brain microsomes.
  Journal
J Biol Chem 256:12306-9 (1981)
Reference
2  [PMID:7142179]
  Authors
Weinstein J, de Souza-e-Silva U, Paulson JC.
  Title
Purification of a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase and a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase to homogeneity from rat liver.
  Journal
J Biol Chem 257:13835-44 (1982)
Reference
3  [PMID:7142180]
  Authors
Weinstein J, de Souza-e-Silva U, Paulson JC.
  Title
Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver.
  Journal
J Biol Chem 257:13845-53 (1982)
Other DBs
ExplorEnz - The Enzyme Database: 2.4.3.5
IUBMB Enzyme Nomenclature: 2.4.3.5
ExPASy - ENZYME nomenclature database: 2.4.3.5
BRENDA, the Enzyme Database: 2.4.3.5
CAS: 80237-98-5

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