Carboxylesterase

carboxylesterase
Identifiers
EC no.3.1.1.1
CAS no.9016-18-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:[1]

a carboxylic ester + H2O an alcohol + a carboxylate

Most enzymes from this group are serine hydrolases belonging to the superfamily of proteins with α/β hydrolase fold. Some exceptions include an esterase with β-lactamase-like structure (PDB: 1ci8​).

Carboxylesterases are widely distributed in nature, and are common in mammalian liver. Many participate in phase I metabolism of xenobiotics such as toxins or drugs; the resulting carboxylates are then conjugated by other enzymes to increase solubility and eventually excreted. The essential polyunsaturated fatty acid arachidonic acid (AA C20H32O2; 20:4, n-6), formed by the synthesis from dietary linoleic acid (LA: C18H32O2 18:2, n-6), has a role as a human carboxylesterase inhibitor.[2]

The carboxylesterase family of evolutionarily related proteins (those with clear sequence homology to each other) includes a number of proteins with different substrate specificities, such as acetylcholinesterases.

  1. ^ Aranda, Juan; Cerqueira, N. M. F. S. A.; Fernandes, P.A.; Roca, M.; Tuñon, I.; Ramos, M. J. (2014). "The Catalytic Mechanism of Carboxylesterases. A Computational Study". Biochemistry. 53 (36): 5820–5829. doi:10.1021/bi500934j. PMID 25101647.
  2. ^ PubChem. "Arachidonic acid". pubchem.ncbi.nlm.nih.gov. Retrieved 2022-11-24.

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