Article
Structural flexibility and functional versatility of cytochrome P450 and rapid evolution.
Mutation research - 19 Feb 1996
Negishi M, Iwasaki M, Juvonen R O, Sueyoshi T, Darden T A, Pedersen L G
Abstract excerpt
P450 represents a large group of heme-thiolate enzymes that exhibit remarkably diverse activities for the metabolism of numerous endogenous and exogenous chemicals. Recent site-directed mutagenesis studies indicate that a single mutation at any of the key residues can be enough to alter the subst...
Topics
- Animals
- Aryl Hydrocarbon Hydroxylases
- Base Sequence
- Binding Sites
- Cytochrome P-450 CYP2A6
- Cytochrome P-450 Enzyme System
- Evolution, Molecular
- Iron-Sulfur Proteins
- Liver
- Mice
- Mixed Function Oxygenases
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Recombinant Proteins
- Steroid Hydroxylases
- Structure-Activity Relationship