Title : Engineering of a functional human NADH-dependent cytochrome P450 system.

Pub. Date : 2001 Jan 2

PMID : 11136248






3 Functional Relationships(s)
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1 Of the mutations made, the substitution of Trp-676 with alanine (W676A) resulted in a functional NADH-dependent enzyme, which catalyzed the reduction of cytochrome c and ferricyanide as well as facilitated the metabolism of 7-ethoxyresorufin by CYP1A2. NAD cytochrome c, somatic Homo sapiens
2 Kinetic analysis measuring cytochrome c activity revealed that the NADH-dependent k(cat) of W676A is equivalent (90%) to the NADPH-dependent k(cat) of the wild-type enzyme, with W676A having an approximately 1,000-fold higher specificity for NADH. NAD cytochrome c, somatic Homo sapiens
3 Furthermore, NADPH was a potent inhibitor of the W676A NADH-dependent cytochrome c reduction and CYP1A2 activity. NAD cytochrome c, somatic Homo sapiens