In enzymology, a N-acetylglucosamine deacetylase (EC 3.5.1.33) is an enzyme that catalyzes the chemical reaction
| N-acetylglucosamine deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.33 | ||||||||
| CAS no. | 9012-32-2 | ||||||||
| 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 | ||||||||
| |||||||||
- N-acetyl-D-glucosamine + H2O D-glucosamine + acetate
Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and H2O, whereas its two products are D-glucosamine 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 amidohydrolase. Other names in common use include acetylaminodeoxyglucose acetylhydrolase, and N-acetyl-D-glucosaminyl N-deacetylase. This enzyme participates in aminosugars metabolism.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2C1G and 2C1I.
References
edit- Roseman S (May 1957). "Glucosamine metabolism. I. N-acetylglucosamine deacetylase". The Journal of Biological Chemistry. 226 (1): 115–24. PMID 13428742.
