Human liver debrisoquine 4-hydroxylase: test for specifity toward various monooxygenase substrates and model of the active site

Thomas Wolff, Linda M. Distlerath, Mark T. Worthington, F. Peter Guengerich

Research output: Contribution to journalArticle

Abstract

Polyclonal antibodies raised toward a debrisoquine 4-hydroxylating cytochrome P-450 species purified from rat liver (P-450UTA) were used to determine which monooxygenase reactions are linked to debrisoquine hydroxylation in human liver. Anti P-450UTA did not inhibit the oxidation of dimethylnitrosamine, morphine, diazepam, vinylidene chloride, trichloroethylene, benzo(a)pyrene and its 7.8-dihydrodiol, but was inhibitory for the hydroxylation of debrisoquine, (±)-bufuralol, lasiocarpine and monocrotaline. A model interpreting the substrate specificity of the human liver enzyme is presented.

Original languageEnglish (US)
Pages (from-to)89-90
Number of pages2
JournalArchives of Toxicology
Volume60
Issue number1-3
DOIs
Publication statusPublished - May 1987
Externally publishedYes

    Fingerprint

Keywords

  • Cytochrome P-450
  • Debrisoquine
  • Human liver

ASJC Scopus subject areas

  • Toxicology
  • Health, Toxicology and Mutagenesis

Cite this