Acetylesterase

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:

${\displaystyle {\ce {R-OC(O)CH3 + H2O}}\quad {\xrightarrow[{\text{acetylesterase}}]{}}\quad {\ce {R-OH + HO-C(O)CH3}}}$

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

• 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. PMID 18880795.

This page was last edited on 28 October 2023, at 05:14