From Wikipedia, the free encyclopedia
galactosyldiacylglycerol alpha-2,3-sialyltransferase
Identifiers
EC no. 2.4.99.5
CAS no. 80237-98-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a galactosyldiacylglycerol alpha-2,3-sialyltransferase ( EC 2.4.99.5) is an enzyme that catalyzes the chemical reaction

CMP-N-acetylneuraminate + 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol CMP + 1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]-sn- glycerol

Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol, whereas its 3 products are CMP, [[1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]-sn-]], and glycerol.

This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:1,2-diacyl-3-beta-D-galactosyl-sn-glycerol N-acetylneuraminyltransferase. This enzyme participates in glycerolipid metabolism.

References

  • Pieringer J, Keech S, Pieringer RA (1981). "Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse brain microsomes". J. Biol. Chem. 256 (23): 12306–9. PMID  7298658.
  • Weinstein J, de Souza-e-Silva U, Paulson JC (1982). "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". J. Biol. Chem. 257 (22): 13835–44. PMID  7142179.
  • Weinstein J, de Souza-e-Silva U, Paulson JC (1982). "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". J. Biol. Chem. 257 (22): 13845–53. PMID  7142180.


From Wikipedia, the free encyclopedia
galactosyldiacylglycerol alpha-2,3-sialyltransferase
Identifiers
EC no. 2.4.99.5
CAS no. 80237-98-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a galactosyldiacylglycerol alpha-2,3-sialyltransferase ( EC 2.4.99.5) is an enzyme that catalyzes the chemical reaction

CMP-N-acetylneuraminate + 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol CMP + 1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]-sn- glycerol

Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol, whereas its 3 products are CMP, [[1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]-sn-]], and glycerol.

This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:1,2-diacyl-3-beta-D-galactosyl-sn-glycerol N-acetylneuraminyltransferase. This enzyme participates in glycerolipid metabolism.

References

  • Pieringer J, Keech S, Pieringer RA (1981). "Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse brain microsomes". J. Biol. Chem. 256 (23): 12306–9. PMID  7298658.
  • Weinstein J, de Souza-e-Silva U, Paulson JC (1982). "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". J. Biol. Chem. 257 (22): 13835–44. PMID  7142179.
  • Weinstein J, de Souza-e-Silva U, Paulson JC (1982). "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". J. Biol. Chem. 257 (22): 13845–53. PMID  7142180.



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