The use of the novel substrate-heme complex approach in the derivation of a representation of the active site of the enzyme cholesterol side chain cleavage

Biochem Biophys Res Commun. 2000 Aug 11;274(3):821-4. doi: 10.1006/bbrc.2000.3209.

Abstract

The previously reported substrate-heme complex approach is used to study the binding of type II inhibitors of the enzyme cholesterol side chain cleavage (CSCC), a cytochrome P-450 dependent enzyme involved in the oxidative cleaveage of the C(20)-C(22) bond of cholesterol. Using the derived model, we have rationalised the inhibitory activity of a number of compounds including aminoglutethimide and pyridoglutethimide and the enantiomers of ketoconazole.

MeSH terms

  • Animals
  • Cholesterol / metabolism*
  • Cytochrome P-450 Enzyme System / metabolism*
  • Heme / metabolism
  • Humans
  • Oxidation-Reduction
  • Substrate Specificity

Substances

  • Heme
  • Cytochrome P-450 Enzyme System
  • Cholesterol