Involvement of liver aldehyde oxidase in conversion of N-hydroxyurethane to urethane.
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.
D042931:Aldehyde Oxidase; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D000818:Animals; D001711:Biotransformation; D003600:Cytosol / Q000201:enzymology; D006168:Guinea Pigs; D006877:Hydroxamic Acids / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D011817:Rabbits; D014520:Urethane / Q000378:metabolism* / Q000031:analogs & derivatives; D014969:Xanthine Oxidase / Q000378:metabolism
D006877:Hydroxamic Acids; D014520:Urethane; C011286:N-hydroxyurethane; D014969:Xanthine Oxidase; D000445:Aldehyde Oxidoreductases; D042931:Aldehyde Oxidase