Literature summary for 3.3.2.9 extracted from

Lewis, D.F.V.; Lake, B.G.; Bird, M.G.
Molecular modelling of human microsomal epoxide hydrolase (EH) by homology with fungal (Aspergillus niger) EH crystal structure of 1.8 A resolution: structure-activity relationships in epoxides inhibiting EH activity (2005), Toxicol. In Vitro, 19, 517-522.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modelling of human enzyme by homology with the crystal structure of the Aspergillus niger enzyme at 1.8 A resolution, structure-activity relationships in epoxides inhibiting EH activity	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
H139R	mutant shows increased activity compared to the wild-type enzyme, molecular modelling	Homo sapiens
R43T	mutant shows reduced activity compared to the wild-type enzyme, molecular modelling	Homo sapiens
T275A	mutant shows similar activity compared to the wild-type enzyme, molecular modelling	Homo sapiens
Y113H	mutant shows similar activity compared to the wild-type enzyme, molecular modelling	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	quantitative structure-activity relationships in epoxides inhibiting EH activity, molecular modelling, kinetics, overview	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
microsome	-	Homo sapiens	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
cis-stilbene oxide + H2O = (1R,2R)-1,2-diphenylethane-1,2-diol	active site structure, quantitative structure-activity relationships, molecular modelling	Homo sapiens	a

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Release 2023.1 (January 2023)