Involvement of liver aldehyde oxidase in conversion of N-hydroxyurethane to urethane.

Article Details

Citation

Copy to clipboard

Sugihara K, Kitamura S, Tatsumi K

Involvement of liver aldehyde oxidase in conversion of N-hydroxyurethane to urethane.

J Pharmacobiodyn. 1983 Sep;6(9):677-83.

PubMed ID

6689178 [ View in PubMed

]

Abstract

The present study provides the evidence that liver aldehyde oxidase in the presence of its electron donors can catalyze the reduction of N-hydroxyurethane to urethane under anaerobic conditions. Guinea pig liver 9000 X g supernatant and cytosol, but not liver microsomes, exhibited N-hydroxyurethane reductase activity in the presence of acetaldehyde or 2-hydroxypyrimidine. The cytosolic enzyme was precipitated with ammonium sulfate between 30 and 45% ammonium sulfate saturation. The N-hydroxyurethane reductase and aldehyde oxidase activities of the precipitate were similarly susceptible to inhibition by a variety of chemicals. When the precipitate was chromatographed on a DEAE-cellulose column, the elution peak position of N-hydroxyurethane reductase was entirely identical with that of aldehyde oxidase. Furthermore, purified rabbit liver aldehyde oxidase also exhibited a significant N-hydroxyurethane reductase activity in the presence of acetaldehyde or 2-hydroxypyrimidine.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Urethane	Aldehyde oxidase	Protein	Humans	Unknown	Substrate	Details