In enzymology, an aculeacin-A deacylase (EC 3.5.1.70) is an enzyme that catalyzes the chemical reaction that cleaves the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side chain.
| Aculeacin-A deacylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.70 | ||||||||
| CAS no. | 121479-50-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase.
References
edit- Takeshima H, Inokoshi J, Takada Y, Tanaka H, Omura S (April 1989). "A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization". J. Biochem. 105 (4). Tokyo: 606–10. PMID 2760018.
