Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms.
Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase.
Mechanism of soluble epoxide hydrolase. Formation of an alpha-hydroxy ester-enzyme intermediate through Asp-333.
Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase.
Primary structure and catalytic mechanism of the epoxide hydrolase from Agrobacterium radiobacter AD1.
Mechanism of microsomal epoxide hydrolase. Semifunctional site-specific mutants affecting the alkylation half-reaction.
Semifunctional site-specific mutants affecting the hydrolytic half-reaction of microsomal epoxide hydrolase.
Characterisation of a catabolic epoxide hydrolase from a Corynebacterium sp.
Catalytic triad of microsomal epoxide hydrolase: replacement of Glu404 with Asp leads to a strongly increased turnover rate.
Kinetic mechanism of the enantioselective conversion of styrene oxide by epoxide hydrolase from Agrobacterium radiobacter AD1.
Epoxide hydrolases and their synthetic applications.
Kinetic and chemical mechanism of epoxide hydrolase.
The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides.
Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase.
Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: implications for the structure and function of the mammalian microsomal class of epoxide hydrolases.
Binding of alkylurea inhibitors to epoxide hydrolase implicates active site tyrosines in substrate activation.
Biochemical evidence for the involvement of tyrosine in epoxide activation during the catalytic cycle of epoxide hydrolase.
Tyrosine residues serve as proton donor in the catalytic mechanism of epoxide hydrolase from Agrobacterium radiobacter.
3-D QSAR analysis of inhibition of murine soluble epoxide hydrolase (MsEH) by benzoylureas, arylureas, and their analogues.
New structural and chemical insight into the catalytic mechanism of epoxide hydrolases.
A theoretical examination of the acid-catalyzed and noncatalyzed ring-opening reaction of an oxirane by nucleophilic addition of acetate. Implications to epoxide hydrolases.
Microbial epoxide hydrolases for preparative biotransformations.
Reaction mechanism of soluble epoxide hydrolase: insights from molecular dynamics simulations.
Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
Quantitative structure-activity relationships for the enantioselectivity of oxirane ring-opening catalyzed by epoxide hydrolases.
Polymorphisms in human soluble epoxide hydrolase.
The E.C. was transferred from 3.3.2.3 to 3.3.2.10. This enzyme belongs to the Alpha/Beta hydrolase superfamily. Moreover, this enzyme is homologous to counterpart enzymes from fungi and bacteria (S00352 in EzCATDB). Although this enzyme binds magnesium ion, it is not involved in catalysis. According to the literature [13], [14], & [15], the catalysis proceeds through an SN2-like reaction. In the first step, Asp333 (PDB 1cqz) makes a nucleophilic attack on the epoxide to form a "glycol-monoester intermediate", whilst Tyr465 and Tyr381 (PDB 1cqz) stablize the negative charged oxygen atom in the transition-state, and act as a general acid catalyst to facilitate the epoxide ring opening, by protonating to the epoxide oxygen. In the second step, the glycol-monoester intermediate is hydrolyzed by a water molecule, which is activated through proton abstraction by the His523/Asp495 (PDB 1cqz) charge-relay system.