6533b82efe1ef96bd1293e12
RESEARCH PRODUCT
Isolation of a Putative Hydroxyacyl Enzyme Intermediate of an Epoxide Hydrolase
Bruce D. HammockJeffrey K. BeethamFranck PinotMichael ArandDavid F. GrantFranz Oeschsubject
Epoxide HydrolasesEpoxide hydrolase 2chemistry.chemical_classificationReaction mechanismStereochemistryAcylationBiophysicsSubstrate (chemistry)Cell BiologyReaction intermediateHydrogen-Ion ConcentrationTritiumBiochemistryRecombinant ProteinsKineticsMiceEnzymechemistryBiochemistryCovalent bondAnimalsHumansEpoxide hydrolaseMolecular BiologyIncubationdescription
A putative covalent, alpha-hydroxyacyl intermediate was isolated by the brief exposure of murine soluble epoxide hydrolase to its substrate. The reaction was reversed by time and blocked by competitive inhibitors. The formation of the intermediate was dependent upon the concentration of the enzyme and was increased by incubation under acidic conditions. The structure of the intermediate was supported by microchemical methods.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1994-02-01 | Biochemical and Biophysical Research Communications |