Purification and characterization of a soybean flour-induced cytochrome P-450 from Streptomyces griseus
| Autor: | D P O'Keefe, M K Trower, F. S. Sariaslani |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Cytochrome
Blotting Western Heme Microbiology Peptide Mapping Xenobiotics Cytochrome P-450 Enzyme System Oxidoreductase Isoelectric Point Amino Acids Molecular Biology Ferredoxin Biotransformation chemistry.chemical_classification biology Cytochrome c peroxidase Cytochrome c Spectrum Analysis Streptomyces griseus Cytochrome P450 biology.organism_classification Molecular Weight Biochemistry chemistry Enzyme Induction biology.protein Spinach Soybeans Research Article |
| Zdroj: | Journal of bacteriology. 171(4) |
| ISSN: | 0021-9193 |
| Popis: | A soybean flour-induced, soluble cytochrome P-450 (P-450soy) was purified 130-fold to homogeneity from Streptomyces griseus. Native cytochrome P-450soy is a single polypeptide, with a molecular weight of 47,500, in association with one ferriprotoporphyrin IX prosthetic group. Oxidized P-450soy exhibited visible absorption maxima at 394, 514, and 646 nm, characteristic of a high-spin cytochrome P-450. The CO-reduced difference spectrum of P-450soy had a Soret maximum at 448 nm. When reconstituted with spinach ferredoxin and spinach ferredoxin:NADP+ oxidoreductase, purified cytochrome P-450soy catalyzed the NADPH-dependent oxidation of the xenobiotic substrates precocene II and 7-ethoxycoumarin. In vitro proteolysis of cytochrome P-450soy generated a stable and catalytically active cytochrome P-450, designated P-450soy delta. |
| Databáze: | OpenAIRE |
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