Abstract
The ability of aminoglutethimide to inhibit cholesterol conversion to pregnenolone was lost upon acetylation of the arylamine nitrogen. This appears to be due to failure of N-acetyl-d-aminoglutethimide to bind to cytochrome P-450scc, since it does not produce the altered low spin form of the enzyme formed upon binding of d-aminoglutethimide. These findings provide further evidence for a role of the free arenamine function in aminoglutethimide and related inhibitors.
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