6533b873fe1ef96bd12d4aff

RESEARCH PRODUCT

Dihydrodiol Dehydrogenase: Substrate Specificity, Inducibility and Tissue Distribution

K. VogelA. SeidelFranz OeschKarl-ludwig PlattP. Petrovic

subject

chemistry.chemical_classificationchemistry.chemical_compoundEnzymechemistryBiochemistrypolycyclic compoundsInducerGlutathioneMonooxygenaseXenobioticDihydrodiol dehydrogenaseEpoxide hydrolaseHormone

description

The present study shows that: Dihydrodiol dehydrogenase activity is present in the 100,000 g supernatant fraction of extrahepatic tissues. Dihydrodiol dehydrogenase is able to oxidize the hydroxy group and to reduce the keto group of a number of xenobiotics including quinones derived from polycyclic aromatic hydrocarbons. Dihydrodiol dehydrogenase was not inducible by various substances including hormones, polycyclic aromatic hydrocarbons, substrates of the enzyme and potent inducers of monooxygenases, epoxide hydrolase and glutathione S-transferases. Only in the case of thyroxine was a weak induction with a high dose of the hormone observed.

yearjournalcountryeditionlanguage
1982-01-01
https://doi.org/10.1007/978-3-642-68511-8_67