Microsomal N- and C-oxidations of carcinogenic aromatic amines and amides.
Date on N-oxidation (activation step) and C-oxidation (inactivation step) of various carcinogenic aromatic amines and amides by liver microsomes from several species are reviewed. Cytochrome P450 involvement in both N-and ring-hydroxylation of N-2-fluorenylacetamide (2-FAA) is discussed. Data on reconstitution studies with rat and hamster liver microsomes indicated that all 3 components, cytochrome P450, NADPH-cytochrome P450 reductase, and a lipid are required for N-and ring-hydroxylation of 2-FAA. Specificity in these oxidations is in the cytochrome P450 fraction.
D000577:Amides / Q000378:metabolism*; D000588:Amines / Q000378:metabolism*; D000818:Animals; D001711:Biotransformation; D002273:Carcinogens / Q000378:metabolism*; D006224:Cricetinae; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D006168:Guinea Pigs; D051379:Mice; D008862:Microsomes, Liver / Q000378:metabolism*; D051381:Rats; D013045:Species Specificity; D013329:Structure-Activity Relationship
D000577:Amides; D000588:Amines; D002273:Carcinogens; D003577:Cytochrome P-450 Enzyme System