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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Döhr, O. Paine, M. J. Friedberg, T. Roberts, G. C. Wolf, C. R.
Description	Author Affiliation: Döhr O ( Biomedical Research Center, University of Dundee, and Imperial Cancer Research Fund Molecular Pharmacology Unit, Ninewells Hospital and Medical School, Dundee, DD1 9SY, United Kingdom.);
Abstract	A functional human NADH-dependent cytochrome P450 system has been developed by altering the cofactor preference of human NADPH cytochrome P450 reductase (CPR), the redox partner for P450s. This has been achieved by a single amino acid change of the conserved aromatic amino acid Trp-676, which covers the re-side of the FAD isoalloxazine ring in the nicotinamide-binding site. 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. 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. The apparent K(M)(NADPH) and K(M)(NADH) values of W676A are 80- and 150-fold decreased, respectively. In accordance with structural data, which show a bipartite binding mode of NADPH, substitution of Trp-676 does not affect 2'-AMP binding as seen by the inhibition of both wild-type CPR and the W676A mutant. Furthermore, NADPH was a potent inhibitor of the W676A NADH-dependent cytochrome c reduction and CYP1A2 activity. Overall, the results show that Trp-676 of human CPR plays a major role in cofactor discrimination, and substitution of this conserved aromatic residue with alanine results in an efficient NADH-dependent cytochrome P450 system.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	NADPH-Ferrihemoprotein Reductase Chemistry Metabolism NAD Protein Engineering Amino Acid Substitution Binding Sites Cytochrome c Group Enzyme Inhibitors Pharmacology Escherichia Coli Ferricyanides Kinetics Models, Biological Mutation NADP Antagonists & Inhibitors Genetics Oxazines Protein Binding Recombinant Proteins Spectrophotometry Substrate Specificity Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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