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The esterases: perspectives and problems

¹Robens Institute of Health and Safety, University of Surrey, Guildford, UK.

Chemico-Biological Interactions

|June 1, 1993

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Biological esterases, enzymes that break down esters, have diverse functions. This review explores their properties, focusing on inhibitors and reaction mechanisms, particularly for carboxylesterases and A-esterases.

Area of Science:

Biochemistry
Enzymology

Background:

Ester-hydrolyzing proteins, known as esterases, are ubiquitous across all biological domains.
While some esterases exhibit specific functions, many possess broad substrate specificity, suggesting diverse biological roles.

Purpose of the Study:

To review esterase properties, with a focus on inhibitors.
To explore similarities and differences among esterases.
To discuss advancements in understanding A-esterases.

Main Methods:

Literature review of esterase properties and mechanisms.
Analysis of substrate specificity and distribution.
Emphasis on inhibitor interactions, particularly organophosphate (OP) compounds.

Main Results:

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Carboxylesterases (B-esterases) have well-established hydrolysis mechanisms, often elucidated through reactions with OP compounds.
Mechanisms for esterases hydrolyzing OP compounds or carboxyl esters insensitive to OP inhibition remain largely speculative.

Conclusions:

Significant knowledge gaps exist regarding the reaction mechanisms of certain esterase classes.
Further research is needed to elucidate the functional diversity and mechanisms of A-esterases.