Article
Kinetic properties of aromatase mutants Pro308Phe, Asp309Asn, and Asp309Ala and their interactions with aromatase inhibitors.
The Journal of steroid biochemistry and molecular biology - 1 Dec 1992
Kadohama N, Yarborough C, Zhou D, Chen S, Osawa Y
Abstract excerpt
Mutant forms of aromatase cytochrome P-450 bearing modifications of amino acid residues Pro308 and Asp309 and expressed in transfected Chinese hamster ovary cells were subjected to kinetic analysis and inhibition studies. The Km for androstenedione for expressed wild type (11.0 +/- 0.3 nM SEM, n = 3) increased 4-, 25- and 31-fold for mutants Pro308Phe, Asp309Asn and Asp309Ala, respectively. There were significant...
Topics
- Animals
- Aromatase
- Aromatase Inhibitors
- Cells, Cultured
- Cricetinae
- Cricetulus
- DNA Mutational Analysis
- Kinetics
- Microsomes
- Mutation
- Transfection