Globoside alpha-N-acetylgalactosaminyltransferase
In enzymology, a globoside alpha-N-acetylgalactosaminyltransferase (EC 2.4.1.88) is an enzyme that catalyzes the chemical reaction
| globoside alpha-N-acetylgalactosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.88 | ||||||||
| CAS no. | 52037-97-5 | ||||||||
| 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 | ||||||||
| |||||||||
- UDP-N-acetyl-D-galactosamine + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D- glucosylceramide UDP + N-acetyl-D-galactosaminyl-N-acetyl-D-galactosaminyl-1,3-D- galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
The 3 substrates of this enzyme are UDP-N-acetyl-D-galactosamine, N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-, and glucosylceramide, whereas its 3 products are UDP, N-acetyl-D-galactosaminyl-N-acetyl-D-galactosaminyl-1,3-D-, and galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galacto syl-1,4-D-galactosyl-1,4-D-glucosylceramide alpha-N-acetyl-D-galactosaminyltransferase. Other names in common use include uridine diphosphoacetylgalactosamine-globoside, alpha-acetylgalactosaminyltransferase, Forssman synthase, and globoside acetylgalactosaminyltransferase. This enzyme participates in glycosphingolipid biosynthesis - globoseries and glycan structures - biosynthesis 2.
References
edit- Kijimoto S, Ishibashi T, Makita A (1974). "Biosynthesis of Forssman hapten from globoside by alpha-N-acetylgalactosaminyltransferase of guinea pig tissues". Biochem. Biophys. Res. Commun. 56 (1): 177–84. doi:10.1016/S0006-291X(74)80331-1. PMID 4823436.
