Acetylesterase
Appearance
acetylesterase | |||||||||
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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 | ||||||||
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In enzymology, an acetylesterase (EC 3.1.1.6) is an enzyme that catalyzes the chemical reaction
- an acetic ester + H2O an alcohol + acetate
Thus, the two substrates of this enzyme are acetic ester and H2O, whereas its two products are alcohol and acetate.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. 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 (1953). "Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination". Biochem. J. 53 (1): 110–7. PMC 1198110. PMID 13032041.
- Bergmann F; Rimon S (1960). "Fractionation of C-esterase from the hog's kidney extract" (PDF). Biochem. J. 77 (2): 209–214. PMC 1204974. PMID 16748846.
- Jansen EF; Nutting M-DF; Balls AK (1948). "The reversible inhibition of acetylesterase by diisopropyl fluorophosphate and tetraethyl pyrophosphate" (PDF). J. Biol. Chem. 175 (2): 975–987. PMID 18880795.