In enzymology, an acyl-lysine deacylase (EC 3.5.1.17) is an enzyme that catalyzes the chemical reaction
| acyl-lysine deacylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.17 | ||||||||
| CAS no. | 9025-11-0 | ||||||||
| 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 | ||||||||
| |||||||||
- N6-acyl-L-lysine + H2O a carboxylate + L-lysine
Thus, the two substrates of this enzyme are N6-acyl-L-lysine and H2O, whereas its two products are carboxylate and L-lysine.
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 N6-acyl-L-lysine amidohydrolase. Other names in common use include epsilon-lysine acylase, and 6-N-acyl-L-lysine amidohydrolase. This enzyme participates in lysine degradation.
References
edit- PAIK WK, BLOCH-FRANKENTHAL L, BIRNBAUM SM, WINITZ M, GREENSTEIN JP (1957). "epsilon-lysine acylase". Arch. Biochem. Biophys. 69: 56–66. doi:10.1016/0003-9861(57)90472-1. PMID 13445179.
