Title : Role of human liver microsomal CYP3A4 and CYP2B6 in catalyzing N-dechloroethylation of cyclophosphamide and ifosfamide.

Pub. Date : 2000 Apr 15

PMID : 10692561






4 Functional Relationships(s)
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1 Role of human liver microsomal CYP3A4 and CYP2B6 in catalyzing N-dechloroethylation of cyclophosphamide and ifosfamide. Cyclophosphamide cytochrome P450 family 3 subfamily A member 4 Homo sapiens
2 Analysis of a panel of fifteen human P450 cDNAs in the baculovirus expression system ("Supersomes") demonstrated that CYP3A4 exhibited the highest N-dechloroethylation activity toward both CPA and IFA, whereas CYP2B6 displayed high N-dechloroethylation activity toward IFA, but not CPA. Cyclophosphamide cytochrome P450 family 3 subfamily A member 4 Homo sapiens
3 Analysis of a panel of fifteen human P450 cDNAs in the baculovirus expression system ("Supersomes") demonstrated that CYP3A4 exhibited the highest N-dechloroethylation activity toward both CPA and IFA, whereas CYP2B6 displayed high N-dechloroethylation activity toward IFA, but not CPA. Cyclophosphamide cytochrome P450 family 3 subfamily A member 4 Homo sapiens
4 With CPA as substrate, CYP3A4 was shown to catalyze >/=95% of liver microsomal N-dechloroethylation, whereas with IFA as substrate, CYP3A4 catalyzed an average of approximately 70% of liver microsomal N-dechloroethylation (range = 40-90%), with the balance of this activity catalyzed by CYP2B6 (range = 10-70%, dependent on the CYP2B6 content of the liver). Cyclophosphamide cytochrome P450 family 3 subfamily A member 4 Homo sapiens