The enzyme cephalosporin-C deacetylase (EC 3.1.1.41) catalyzes the reaction
| cephalosporin-C deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.41 | ||||||||
| CAS no. | 52227-71-1 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
- cephalosporin C + H2O deacetylcephalosporin C + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is cephalosporin-C acetylhydrolase. Other names in common use include cephalosporin C acetyl-hydrolase, cephalosporin C acetylase, cephalosporin acetylesterase, cephalosporin C acetylesterase, cephalosporin C acetyl-esterase, and cephalosporin C deacetylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies
editAs of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1L7A, 1ODS, 1ODT, and 1VLQ.
References
edit- Fujisawa Y, Shirafugi H, Kida M, Nara K, Yoneda M, Kanzaki T (1973). "New findings on cephalosporin C biosynthesis". Nat. New Biol. 246 (153): 154–5. doi:10.1038/newbio246154a0. PMID 4519146.
