N-acetylglucosamine-6-phosphate deacetylase
| N-acetylglucosamine-6-phosphate deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.25 | ||||||||
| CAS number | 9027-50-3 | ||||||||
| 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 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) is an enzyme that catalyzes the chemical reaction
- N-acetyl-D-glucosamine 6-phosphate + H2O D-glucosamine 6-phosphate + acetate
Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine 6-phosphate and H2O, whereas its two products are D-glucosamine 6-phosphate and acetate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetyl-D-glucosamine-6-phosphate amidohydrolase. Other names in common use include acetylglucosamine phosphate deacetylase, acetylaminodeoxyglucosephosphate acetylhydrolase, and 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1O12, 1UN7, 1YMY, 1YRR, 2P50, and 2P53.
References
- White RJ, Pasternak CA (1967). "The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli". Biochem. J. 105 (1): 121&ndash, 5. PMC 1198282. PMID 4861885.
- Yamano N, Matsushita Y, Kamada Y, Fujishima S, Arita M (1996). "Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1". Biosci. Biotechnol. Biochem. 60 (8): 1320&ndash, 3. doi:10.1271/bbb.60.1320. PMID 8987551.