Carboxylester hydrolase

Esterases are a broad class of enzymes that catalyze the hydrolysis of ester bonds, splitting esters into acid and alcohol using water[1][3][4][7][8]. They are widely distributed in all living organisms, including animals, plants, and microorganisms. Carboxylester hydrolases (standard EC number 3.1.1.x) represent the main form, with subclasses including blood esterases, acetylcholinesterase, and microbial esterases[3]. Structurally, most cellular esterases belong to the α/β-hydrolase fold family, featuring a signature catalytic triad (Ser-Asp-His) in a consensus motif (often Gly-x-Ser-x-Gly)[1][4][7]. They play vital roles in metabolic processes (e.g., lipid breakdown, neurotransmitter inactivation), environmental detoxification (including breakdown of insecticides and drugs), and act as targets or off-targets for a variety of inhibitors, making them both a therapeutic target (e.g., inhibition in Alzheimer's disease treatment) and a source of pharmacological variability and toxicity[3][4][5][7][8]. Caveats/Limitations: "Esterase" is a broad and non-specific term—there is no single esterase protein, structure, or gene, but rather a large family of related enzymes. The actual therapeutic or pharmacological relevance depends on the specific esterase in question (e.g., acetylcholinesterase, carboxylesterase, etc.)[3][4][7]. For structured data or drug discovery, the specific subtype, organism, and context must be defined for accurate mapping. Thus, this entry is non-canonical and too generic, and "is_incorrect" should be set to true.

Other names

EsteraseCarboxylic-ester hydrolaseEC 3.1.1.xCarboxylesteraseEsterase (general)Esterase enzyme

Hydrolysis of carboxylic esters, forming acid and alcohol via nucleophilic catalysis Drugs may irreversibly or reversibly inhibit esterase catalytic serine