6533b834fe1ef96bd129d86b
RESEARCH PRODUCT
Vitamin K epoxide reductase activity in the metabolism of epoxides
Franz OeschT. GuenthnerW. WörnerI. Liptay-reuterK. Dosesubject
MaleStereochemistryEpoxideIn Vitro TechniquesReductaseBiochemistryMixed Function Oxygenaseschemistry.chemical_compoundMenadioneEthers CyclicVitamin K Epoxide ReductasesAnimalsEpoxide hydrolaseTrichloroepoxypropaneEpoxide HydrolasesPharmacologyRats Inbred StrainsVitamin K 1MetabolismRatschemistryBiochemistryMicrosomal epoxide hydrolaseMicrosomes LiverMicrosomeEpoxy CompoundsVitamin K epoxide reductasedescription
Abstract The importance of vitamine K epoxide reductase for the metabolism of a range of structurally diverse epoxides has been investigated. Vitamin K 1 epoxide is reduced by rat liver microsomes at a rate of 0.47 nmoles/g liver/min. The rate of menadione oxide reduction is not significantly higher than the non-enzymatic reduction rate. No measurable reduction of benzo[ a ]pyrene 4,5-oxide, benzo[ a ]pyrene 7,8-oxide, phenanthrene 9,10-oxide, styrene 7,8-oxide, and dieldrin has been detected, nor could trichothecene T-2 toxin inhibit reduction of vitamin K 1 epoxide. Thus, vitamin K epoxide reductase is very specific for vitamin K 1 epoxide. Taking into account the range of structurally diverse epoxides investigated and the high specific activities of microsomal epoxide hydrolase and cytosolic glutathione transferase for these epoxides it may be concluded that vitamin K epoxide reductase, in all likelihood, generally does not significantly contribute to the control of epoxides metabolically formed from xenobiotics.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1985-08-01 | Biochemical Pharmacology |