N-acyl-D-aspartate deacylase
| N-acyl-D-aspartate deacylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.83 | ||||||||
| CAS number | 9031-86-1 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a N-acyl-D-aspartate deacylase (EC 3.5.1.83) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-aspartate + H2O a carboxylate + D-aspartate
Thus, the two substrates of this enzyme are N-acyl-D-aspartate and H2O, whereas its two products are carboxylate and D-aspartate.
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-aspartate amidohydrolase. It employs one cofactor, zinc.
References
- Moriguchi M, Sakai K, Katsuno Y, Maki T, Wakayama M (1993). "Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". Biosci. Biotechnol. Biochem. 57 (7): 1145–8. PMID 7763985. doi:10.1271/bbb.57.1145.
- Sakai K, Moriguchi M (1995). "Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". J. Ferment. Bioeng. 80 (4): 311–317. doi:10.1016/0922-338X(95)94197-Y.
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