The N-oxidation of benzamidines in vitro.
The enzymic N-oxidation of a series of N-unsubstituted basic benzamidines (I) to a new type of metabolite, the amidoximes (II), is reported. Rabbit liver homogenates (9000 g supernatant) were used as enzyme source, and metabolites were identified by t.l.c. and mass spectral analysis using synthetic reference compounds. The microsomal NADPH- and oxygen-dependent hydroxylation of benzamidines was not detected after incubation of benzamidine in the presence of SKF 525-A, a known inhibitor of cytochrome P-450. Neither benzamidine or p-methoxybenzamidine is a good substrate for purified microsomal FAD-containing mono-oxygenase.
D000578:Amidines / Q000378:metabolism*; D000818:Animals; D001550:Benzamidines / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D011335:Proadifen / Q000494:pharmacology; D011817:Rabbits
D000578:Amidines; D001550:Benzamidines; D009249:NADP; D011335:Proadifen; D006899:Mixed Function Oxygenases