Article
Engineering of a functional human NADH-dependent cytochrome P450 system.
Proceedings of the National Academy of Sciences of the United States of America - 2 Jan 2001
Döhr O, Paine M J, Friedberg T, Roberts G C, Wolf C R
Abstract excerpt
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...
Topics
- Amino Acid Substitution
- Binding Sites
- Cytochrome c Group
- Enzyme Inhibitors
- Escherichia coli
- Ferricyanides
- Humans
- Kinetics
- Models, Biological
- Mutation
- NAD
- NADP
- NADPH-Ferrihemoprotein Reductase
- Oxazines
- Protein Binding
- Protein Engineering
- Recombinant Proteins
- Spectrophotometry