Corpus ID: 7133640

Inactivation of Escherichia coli-expressed rabbit cytochrome P-450 2C enzymes by 17 beta-substituted steroids.

@article{Klekotka1995InactivationOE,
  title={Inactivation of Escherichia coli-expressed rabbit cytochrome P-450 2C enzymes by 17 beta-substituted steroids.},
  author={Paul A. Klekotka and Toby H. Richardson and Eric F Johnson and James R. Halpert},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1995},
  volume={274 3},
  pages={
          1450-5
        }
}
The specific inactivation of rabbit cytochromes P-450 2C by 17 beta-substituted steroids has been investigated by using purified, Escherichia coli-expressed enzymes. The expressed P-450s provided a means to characterize accurately the effects of 21,21-dichloroprogesterone, 21,21-dichloropregnenolone, 21-chloro-21-fluoropregnenolone, pregn-5,20-diene-3 beta-ol and pregn-4,20-diene-3-one on progesterone hydroxylation by P-450 2C5, 2C4, 2C3 and 2C3v. Previous studies using rabbit liver microsomes… Expand
2 Citations
Homology modeling and substrate binding study of human CYP2C9 enzyme
TLDR
A 3D model of CYP2C9 was built, assessed, and used to characterize explicit enzyme‐substrate complexes using methods previously developed in the laboratory, and each substrate was found to bind to the enzyme with a favorable interaction energy and to remain in the binding site during unconstrained molecular dynamics. Expand
The first synthesis of Krempene B
TLDR
The synthesis of Krempene B, which can be isolated from the marine soft coral Cladiella krempfi, is achieved in 23.9% overall yield from commercially available 3β-acetoxy-5-pregnen-20-one by 11 steps using dienone-phenol rearrangement of steroids and Wittig reaction. Expand