Article
Use of chimeric enzymes and site-directed mutagenesis for identification of three key residues responsible for differences in steroid hydroxylation between canine cytochromes P-450 3A12 and 3A26.
Molecular pharmacology - 1 Feb 1999
Fraser D J, He Y Q, Harlow G R, Halpert J R
Abstract excerpt
Canine cytochromes P-450 3A12 and 3A26 differ by 22 out of 503 amino acid residues. Chimeric constructs and site-directed mutants were used to identify the residues responsible for the much higher rates of steroid hydroxylation by 3A12. Six initial 3A12/3A26 hybrids were generated using convenien...
Topics
- Androstenedione
- Animals
- Aryl Hydrocarbon Hydroxylases
- Binding Sites
- Cloning, Molecular
- Cytochrome P-450 CYP3A
- Cytochrome P-450 Enzyme System
- Dogs
- Humans
- Hydroxylation
- Isoenzymes
- Mixed Function Oxygenases
- Mutagenesis, Site-Directed
- Mutation
- Oxidoreductases, N-Demethylating