Brain mitochondrial cytochrome P-450scc: spectral and catalytic properties.
Article Details
- CitationCopy to clipboard
Walther B, Ghersi-Egea JF, Minn A, Siest G
Brain mitochondrial cytochrome P-450scc: spectral and catalytic properties.
Arch Biochem Biophys. 1987 May 1;254(2):592-6. doi: 10.1016/0003-9861(87)90142-1.
- PubMed ID
- 3579320 [ View in PubMed]
- Abstract
The cytochrome P-450-dependent cholesterol side chain cleavage system of the brain has been studied using nonsynaptic mitochondria as the source of enzymatic activity. The system has been found to bind cholesterol and 11-deoxycorticosterone, producing type I difference spectra, whereas the binding of pregnenolone induced a reverse type I difference spectrum. Inhibitors of cytochrome P-450-linked monooxygenase activities produced type II spectra. The formation of labeled pregnenolone after incubation of brain mitochondria with [4-14C]cholesterol has been obtained, and this formation was inhibited by glutethimide, a specific inhibitor of cytochrome P-450scc. The functional significance of this enzymatic activity is discussed.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Glutethimide Cholesterol side-chain cleavage enzyme, mitochondrial Protein Humans UnknownInhibitorDetails