Polysialic-acid O-acetyltransferase
Appearance
polysialic-acid O-acetyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.136 | ||||||||
CAS no. | 116412-21-6 | ||||||||
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 | ||||||||
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In enzymology, a polysialic-acid O-acetyltransferase (EC 2.3.1.136) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + an alpha-2,8-linked polymer of sialic acid CoA + polysialic acid acetylated on O-7 or O-9
Thus, the two substrates of this enzyme are acetyl-CoA and alpha-2,8-linked polymer of sialic acid, whereas its 3 products are CoA, polysialic acid acetylated on O-7, and polysialic acid acetylated on O-9.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:polysialic-acid O-acetyltransferase. Other names in common use include lecithin:retinol acyltransferase, lecithin-retinol acyltransferase, retinyl ester synthase, LRAT, and lecithin retinol acyl transferase.
References
[edit]- Higa HH, Varki A (1988). "Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1-positive Escherichia coli. The enzyme responsible for the O-acetyl plus phenotype and for O-acetyl form variation". J. Biol. Chem. 263 (18): 8872–8. PMID 2897964.