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N-oxidation of phentermine to N-hydroxyphentermine by a reconstituted cytochrome P-450 oxidase system from rabbit liver

JD Duncan and AK Cho

Previous studies in our laboratory have indicated that the cytochrome P- 450 system is involved in the oxidation of phentermine (2-methyl-1- phenyl-2-aminopropane) to N-hydroxyphentermine by liver microsomal preparations. In the present study, a reconstituted system which consisted of cytochrome P-450 and NADPH cytochrome P-450 reductase purified from liver microsomes of phenobarbital-induced rabbits was found to oxidize phentermine to N-hydroxyphentermine. The reaction was NADPH-dependent and required the presence of both the cytochrome P-450 and reductase preparations. N-Hydroxyphentermine was formed 3 times more rapidly in incubation mixtures which contained dilauroyl phosphatidylcholine than in those without added phospholipid. The reaction was inhibited several-fold by octylamine. It is concluded that the cytochrome P-450 system is able to catalyze the oxidation of phentermine to N-hydroxyphentermine.

Volume 22, Issue 2, pp. 235-238, 09/01/1982
Copyright © 1982 by American Society for Pharmacology and Experimental Therapeutics






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Copyright © 1982 by the American Society for Pharmacology and Experimental Therapeutics