Polymorphisms in human soluble epoxide hydrolase.

doi:10.1124/mol.64.2.482

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Article

Polymorphisms in human soluble epoxide hydrolase.

Molecular pharmacology - 1 Aug 2003

Przybyla-Zawislak Beata D, Srivastava Punit K, Vazquez-Matias Johana, Mohrenweiser Harvey W, Maxwell Joseph E, Hammock Bruce D, Bradbury J Alyce, Enayetallah Ahmed E, Zeldin Darryl C, Grant David F

Abstract excerpt

Human soluble epoxide hydrolase (hsEH) metabolizes a variety of epoxides to the corresponding vicinal diols. Arachidonic and linoleic acid epoxides are thought to be endogenous substrates for hsEH. Enzyme activity in humans shows high interindividual variation (e.g., 500-fold in liver) suggesting the existence of regulatory and/or structural gene polymorphisms. We resequenced each of the 19 exons of the hsEH gene...

Topics

Animals
Baculoviridae
Crystallization
Enzyme Stability
Epoxide Hydrolases
Exons
Genetic Vectors
Genotype
Humans
Kinetics
Mice
Polymorphism, Genetic
Protein Conformation
Solubility

Source

Open in PubMed

Identifiers

PMID: 12869654
DOI: 10.1124/mol.64.2.482

Genes

EPHX2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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