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:
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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1BS9, 1G66, and 2AXE.
An acetate is a salt formed by the combination of acetic acid with a base. "Acetate" also describes the conjugate base or ion typically found in aqueous solution and written with the chemical formula C
2H
3O−
2. The neutral molecules formed by the combination of the acetate ion and a positive ion are also commonly called "acetates". The simplest of these is hydrogen acetate with corresponding salts, esters, and the polyatomic anion CH
3CO−
2, or CH
3COO−
.
In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond:
In biochemistry, an esterase is a class of enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis.
In enzymology, a microsomal epoxide hydrolase (mEH) is an enzyme that catalyzes the hydrolysis reaction between an epoxide and water to form a diol.
The enzyme acetylsalicylate deacetylase (EC 3.1.1.55) catalyzes the reaction
The enzyme α-amino-acid esterase (EC 3.1.1.43) catalyzes the reaction
Aryldialkylphosphatase is a metalloenzyme that hydrolyzes the triester linkage found in organophosphate insecticides:
The enzyme arylesterase (EC 3.1.1.2) catalyzes the reaction
The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:
The enzyme cephalosporin-C deacetylase (EC 3.1.1.41) catalyzes the reaction
The enzyme feruloyl esterase (EC 3.1.1.73) catalyzes the reaction
The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
The enzyme sialate O-acetylesterase (EC 3.1.1.53) catalyzes the reaction
The enzyme sterol esterase (EC 3.1.1.13) catalyzes the reaction
Liver carboxylesterase 1 also known as carboxylesterase 1 is an enzyme that in humans is encoded by the CES1 gene. The protein is also historically known as serine esterase 1 (SES1), monocyte esterase and cholesterol ester hydrolase (CEH). Three transcript variants encoding three different isoforms have been found for this gene. The various protein products from isoform a, b and c range in size from 568, 567 and 566 amino acids long, respectively.
Chromosome 11 open reading frame 54 (C11orf54) is a protein that in humans is encoded by the C11orf54 gene. The "Homo sapiens" gene, C11orf54 is also known as PTD012 and PTOD12. C11orf54 exhibits hydrolase activity on p-nitrophenyl acetate and acts on ester bonds, though the overall function is still not fully understood by the scientific community. The protein is highly conserved with the most distant homolog found is in bacteria.
CAZy is a database of Carbohydrate-Active enZYmes (CAZymes). The database contains a classification and associated information about enzymes involved in the synthesis, metabolism, and recognition of complex carbohydrates, i.e. disaccharides, oligosaccharides, polysaccharides, and glycoconjugates. Included in the database are families of glycoside hydrolases, glycosyltransferases, polysaccharide lyases, carbohydrate esterases, and non-catalytic carbohydrate-binding modules. The CAZy database also includes a classification of Auxiliary Activity redox enzymes involved in the breakdown of lignocellulose.
The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) catalyses the hydrolysis of ester linkages of triglycerides:
The enzyme pyrethroid hydrolase (EC 3.1.1.88, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolysing esterase, pyrethroid-hydrolyzing esterase, pyrethroid-selective esterase, pyrethroid-cleaving enzyme, permethrinase, PytH, EstP; systematic name pyrethroid-ester hydrolase) catalyses the reaction
The enzyme MHETase is a hydrolase, which was discovered in 2016. It cleaves 2-hydroxyethyl terephthalic acid, the PET degradation product by PETase, to ethylene glycol and terephthalic acid. This pair of enzymes, PETase and MHETase, enable the bacterium Ideonella sakaiensis to live on the plastic PET as sole carbon source.