Dihydrodiol Dehydrogenase: Substrate Specificity, Inducibility and Tissue Distribution

  • K. Vogel
  • K.-L. Platt
  • P. Petrovic
  • A. Seidel
  • F. Oesch
Part of the Archives of Toxicology book series (TOXICOLOGY, volume 5)

Abstract

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.

Key words

Dihydrodiol dehydrogenase Tissue distribution Induction Substrate specificity 

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References

  1. Billings RE, Sullivan HR, McMahon RE (1971) The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver. J Biol Chem 246: 3512–3517PubMedGoogle Scholar
  2. Felsted RL, Gee M, Bachur NR (1974) Rat liver daunorubicin reductase; an aldo-keto reductase. J Biol Chem 249: 3672–3679PubMedGoogle Scholar
  3. Felsted RL, Richter DR, Bachur NR (1977) Rat liver aldehyde reductase. Biochem Pharmacol 26: 1117–1124PubMedCrossRefGoogle Scholar
  4. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193: 265–275PubMedGoogle Scholar
  5. Oesch F, Glatt HR, Schmassmann HU (1977) The apparent ubiquity of epoxide hydratase in rat organs. Biochem Pharmacol 26: 603–607PubMedCrossRefGoogle Scholar
  6. Sawada H, Hara A, Nakayama T, Kato F (1980) Reductases for aromatic aldehydes and ketones from rabbit liver. J Biochem 87: 1153–1165PubMedGoogle Scholar
  7. Vogel K, Bentley P, Platt KL, Oesch F (1980) Rat liver cytoplasmic dihydrodiol dehydrogenase: purification to apparent homogeneity and properties. J Biol Chem 255: 9621–9625Google Scholar
  8. Wermuth B, Munch JDB (1978) Reduction of biogenic aldehydes by aldehyde reductase and alcohol dehydrogenase from human liver. Biochem Pharmacol 28: 1431–1433CrossRefGoogle Scholar
  9. Wermuth B, Munch JDB, Von Wartburg JP (1977) Purification and properties of NADPH-dependent aldehyde reductase from human liver. J Biol Chem 252: 3821–3828PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • K. Vogel
    • 1
  • K.-L. Platt
    • 1
  • P. Petrovic
    • 1
  • A. Seidel
    • 1
  • F. Oesch
    • 1
  1. 1.Department of PharmacologyUniversity of MainzMainzFederal Republic of Germany

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