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

Abstract:

:Polyclonal antibodies raised toward a debrisoquine 4-hydroxylating cytochrome P-450 species purified from rat liver (P-450UT-A) were used to determine which monooxygenase reactions are linked to debrisoquine hydroxylation in human liver. Anti P-450UT-A 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.

journal_name

Arch Toxicol

journal_title

Archives of toxicology

authors

Wolff T,Distlerath LM,Worthington MT,Guengerich FP

doi

10.1007/BF00296955

subject

Has Abstract

pub_date

1987-01-01 00:00:00

pages

89-90

issue

1-3

eissn

0340-5761

issn

1432-0738

journal_volume

60

pub_type

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