The use of the novel substrate-heme complex approach in the derivation of a representation of the active site of the enzyme complex 17alpha-hydroxylase and 17,20-lyase

Biochem Biophys Res Commun. 2004 Apr 9;316(3):595-8. doi: 10.1016/j.bbrc.2004.02.092.

Abstract

A novel molecular modelling technique, namely the substrate-heme complex (SHC) approach, is used to derive a representation of the overall active site of the enzyme complex 17alpha-hydroxylase (17alpha-OHase) and 17,20-lyase (lyase), a cytochrome P-450 dependent enzyme involved in the oxidative hydroxylation of the C(17) and cleavage of the C(17)-C(20) bond of the progestins (e.g., progesterone or pregnenolone). Using the derived model, we have rationalised the inhibitory activity of a number of steroidal and non-steroidal inhibitors, including miconazole and ketoconazole (the latter being a former potential treatment of hormone-dependent prostate cancer).

MeSH terms

  • Antineoplastic Agents / pharmacology
  • Binding Sites
  • Biochemistry / methods*
  • Heme / chemistry*
  • Hydrogen / chemistry
  • Hydrogen Bonding
  • Ketoconazole / pharmacology
  • Miconazole / pharmacology
  • Models, Chemical
  • Models, Molecular
  • Oxygen / metabolism
  • Steroid 17-alpha-Hydroxylase / chemistry*
  • Steroids / chemistry

Substances

  • Antineoplastic Agents
  • Steroids
  • Heme
  • Miconazole
  • Hydrogen
  • Steroid 17-alpha-Hydroxylase
  • Ketoconazole
  • Oxygen