Article
Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1.
Biochemistry - 29 Sept 1992
He Y A, Balfour C A, Kedzie K M, Halpert J R
Abstract excerpt
Two allelic variants and eight site-directed mutants of cytochrome P450 2B1 differing at residue 478 have been expressed in COS cells and assayed for androstenedione hydroxylase activities. The 478Gly and 478Ala variants and five mutants (Ser, Thr, Val, Ile, and Leu) exhibited 16 beta-OH:16 alpha...
Topics
- Alleles
- Animals
- Aryl Hydrocarbon Hydroxylases
- Base Sequence
- Cell Line
- Chloramphenicol
- Cytochrome P-450 CYP2B1
- Cytochrome P-450 Enzyme System
- Genetic Variation
- Kinetics
- Microsomes
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Oligodeoxyribonucleotides
- Oxidoreductases
- Recombinant Proteins
- Steroid Hydroxylases
- Substrate Specificity