| glucosamine-1-phosphate N-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.157 | ||||||||
| 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 glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + alpha-D-glucosamine 1-phosphate CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Thus, the two substrates of this enzyme are acetyl-CoA and alpha-D-glucosamine 1-phosphate, whereas its two products are CoA and N-acetyl-alpha-D-glucosamine 1-phosphate.
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:alpha-D-glucosamine-1-phosphate N-acetyltransferase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2OI5, 2OI6, and 2OI7.
References
- Mengin-Lecreulx D, van Heijenoort J (1994). "Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis". J. Bacteriol. 176 (18): 5788–95. doi:10.1128/jb.176.18.5788-5795.1994. PMC 196783. PMID 8083170.
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