Biology:Acetylesterase
From HandWiki
Short description: Class of enzymes which split acetic esters into alcohols and acetates
| acetylesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.1.6 | ||||||||
| CAS number | 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 | ||||||||
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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:
- [math]\displaystyle{ \ce{R-OC(O)CH3 + H2O} \quad \xrightarrow[\text{acetylesterase}]{} \quad \ce{R-OH + HO-C(O)CH3} }[/math]
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
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1BS9, 1G66, and 2AXE.
References
- "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. January 1953. doi:10.1042/bj0530110. PMID 13032041.
- "Fractionation of C-esterase from the hog's kidney extract". The Biochemical Journal 77 (2): 209–14. November 1960. doi:10.1042/bj0770209. PMID 16748846. PMC 1204974. http://www.biochemj.org/bj/077/0209/0770209.pdf.
- "The reversible inhibition of acetylesterase by diisopropyl fluorophosphate and tetraethyl pyrophosphate". The Journal of Biological Chemistry 175 (2): 975–87. September 1948. PMID 18880795. http://www.jbc.org/content/175/2/975.full.pdf.
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