Active site-directed inhibition of rabbit cytochrome P-450 1 by amino-substituted steroids.

@article{Johnson1986ActiveSI,
  title={Active site-directed inhibition of rabbit cytochrome P-450 1 by amino-substituted steroids.},
  author={E. F. Johnson and G. Schwab and J. Singh and L. Vickery},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 22},
  pages={
          10204-9
        }
}
  • E. F. Johnson, G. Schwab, +1 author L. Vickery
  • Published 1986
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • A variety of amino-substituted steroids were investigated as inhibitors of the rabbit hepatic, steroid 21-hydroxylase, cytochrome P-450 1. We reasoned that a steroid analog of pregnenolone capable of mimicking the binding of C21-steroids to the enzyme at the active site and bearing an amine moiety on the 17 beta-side chain would be a potent inhibitor if the amine were free to interact with the heme iron. Our studies reveal that 22-amino-23,24-bisnor-5-cholen-3 beta-ol (22-ABC) is a tightly… CONTINUE READING
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