Protein N-acetylglucosaminyltransferase
| protein N-acetylglucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.94 | ||||||||
| CAS no. | 72319-34-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a protein N-acetylglucosaminyltransferase (EC 2.4.1.94) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetyl-D-glucosamine + protein UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and protein, whereas its two products are UDP and 4-N-(N-acetyl-D-glucosaminyl)-protein.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:protein beta-N-acetyl-D-glucosaminyl-transferase. Other names in common use include uridine diphosphoacetylglucosamine-protein, acetylglucosaminyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide, beta-N-acetylglucosaminyltransferase, and O-GlcNAc transferase.
References
[edit]- Khalkhall Z, Marshall RD (1975). "Glycosylation of ribonuclease A catalysed by rabbit liver extracts". Biochem. J. 146 (2): 299–307. PMC 1165306. PMID 1156375.
- Khalkhali Z, Marshall RD (1976). "UDP-N-acetyl-D-glucosamine-asparagine sequon N-acetyl-beta-D-glucosaminyl-transferase-activity in human serum". Carbohydr. Res. 49: 455–73. doi:10.1016/S0008-6215(00)83163-8. PMID 986874.
- Khalkhali Z, Marshall RD, Reuvers F, Habets-Willems C, Boer P (1976). "Glycosylation in vitro of an asparagine sequon catalysed by preparations of yeast cell membranes". Biochem. J. 160 (1): 37–41. PMC 1164198. PMID 795426.
External links
[edit]- N-Acetylglucosaminyltransferases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
