N-acyl-D-glutamate deacylase

From Wikipedia, the free encyclopedia

In enzymology, a N-acyl-D-glutamate deacylase (EC 3.5.1.82) is an enzyme that catalyzes the chemical reaction

N-acyl-D-glutamate + H₂O a carboxylate + D-glutamate

Thus, the two substrates of this enzyme are N-acyl-D-glutamate and H₂O, whereas its two products are carboxylate and D-glutamate.

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-acyl-D-glutamate amidohydrolase. It employs one cofactor, zinc.

[edit] References

• IUBMB entry for 3.5.1.82
• BRENDA references for 3.5.1.82 (Recommended.)
• PubMed references for 3.5.1.82
• PubMed Central references for 3.5.1.82
• Google Scholar references for 3.5.1.82
• Moriguchi M (Tokyo). "Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". J. Biochem.: 204–9. PMID 8537313. 
• Wakayama M, Miura Y, Oshima K, Sakai K, Moriguchi M (1995). "Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1". Biosci. Biotechnol. Biochem. 59: 1489–92. PMID 7549100. 
• Wakayama M, Tsutsumi T, Yada H, Sakai K, Moriguchi M (1996). "Chemical modification of histidine residue of N-acyl-D-Glutamate amidohydrolase from Pseudomonas sp. 5f-1". Biosci. Biotechnol. Biochem. 60: 650–3. PMID 8829533. 

[edit] External links

• IUBMB entry for 3.5.1.82

• KEGG entry for 3.5.1.82

• BRENDA entry for 3.5.1.82

• NiceZyme view of 3.5.1.82

• EC2PDB: PDB structures for 3.5.1.82

• PRIAM entry for 3.5.1.82

• PUMA2 entry for 3.5.1.82

• IntEnz: Integrated Enzyme entry for 3.5.1.82

• MetaCyc entry for 3.5.1.82

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0047421: N-acyl-D-glutamate deacylase

• AMIGO entry for GO code 0047421: N-acyl-D-glutamate deacylase