Article
Alteration of high and low spin equilibrium by a single mutation of amino acid 209 in mouse cytochromes P450.
The Journal of biological chemistry - 25 Feb 1991
Iwasaki M, Juvonen R, Lindberg R, Negishi M
Abstract excerpt
The identities of the amino acid at position 209 are most critical in determining specific coumarin 7- and steroid 15 alpha-hydroxylase activity in P450coh and P450(15)alpha, respectively. This system, therefore, provides us with an excellent model to study the structural basis for P450 specificity as a monooxygenase. We expressed in Saccharomyces cerevisiae a series of the mutated P450s in which residue 209 was...
Topics
- Amino Acids
- Animals
- Aryl Hydrocarbon Hydroxylases
- Catalysis
- Cytochrome P-450 CYP2A6
- Cytochrome P-450 Enzyme System
- Gene Expression Regulation, Fungal
- Genes, Fungal
- Mice
- Mixed Function Oxygenases
- Mutagenesis, Site-Directed