N-acyl-D-amino-acid deacylase
| N-acyl-D-amino-acid deacylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.81 | ||||||||
| CAS no. | 65979-42-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a N-acyl-D-amino-acid deacylase (EC 3.5.1.81) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-amino acid + H2O an acid + D-amino acid
Thus, the two substrates of this enzyme are N-acyl-D-amino acid and H2O, whereas its two products are acid and D-amino acid.
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-amino acid amidohydrolase. It employs one cofactor, zinc.
Structural studies
[edit]As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1M7J, 1RJP, 1RJQ, 1RJR, 1RK5, 1RK6, 1V4Y, and 1V51.
References
[edit]- Wakayama M, Katsuno Y, Hayashi S, Miyamoto Y, Sakai K, Moriguchi M (1995). "Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli". Biosci. Biotechnol. Biochem. 59 (11): 2115–9. doi:10.1271/bbb.59.2115. PMID 8541651.
- Wakayama M, Hayashi S, Yatsuda Y, Katsuno Y, Sakai K, Moriguchi M (1996). "Overproduction of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 in Escherichia coli and its purification". Protein Expr. Purif. 7 (4): 395–9. doi:10.1006/prep.1996.0059. PMID 8776758.
