Acetylesterase
| acetylesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.6 | ||||||||
| CAS no. | 9000-82-2 | ||||||||
| 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 biochemistry, an acetylesterase (EC 3.1.1.6) is a class of enzyme which catalyzes the hydrolysis of acetic esters into an alcohol and acetic acid:
![{\displaystyle {\ce {R-OC(O)CH3 + H2O}}\quad {\xrightarrow[{\text{acetylesterase}}]{}}\quad {\ce {R-OH + HO-C(O)CH3}}}](https://wikimedia.riteme.site/api/rest_v1/media/math/render/svg/978e47445ae4058f30de5d39e307bab0723d9209)
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds (esterases). The systematic name of this enzyme class is acetic-ester acetylhydrolase. Other names in common use include C-esterase (in animal tissues), acetic ester hydrolase, chloroesterase, p-nitrophenyl acetate esterase, and citrus acetylesterase.
Structural studies
[edit]As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1BS9, 1G66, and 2AXE.
References
[edit]- Aldridge WN (January 1953). "Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination". The Biochemical Journal. 53 (1): 110–7. doi:10.1042/bj0530110. PMC 1198110. PMID 13032041.
- Bergmann F, Rimon S (November 1960). "Fractionation of C-esterase from the hog's kidney extract" (PDF). The Biochemical Journal. 77 (2): 209–14. doi:10.1042/bj0770209. PMC 1204974. PMID 16748846.
- Jansen EF, Nutting MD, Balls AK (September 1948). "The reversible inhibition of acetylesterase by diisopropyl fluorophosphate and tetraethyl pyrophosphate" (PDF). The Journal of Biological Chemistry. 175 (2): 975–87. doi:10.1016/S0021-9258(18)57217-3. PMID 18880795.
