Metabolism of analogues of coproporphyrinogen-III with modified side chains: implications for binding at the active site of coproporphyrinogen oxidase

Bioorg Med Chem Lett. 2002 Feb 11;12(3):451-6. doi: 10.1016/s0960-894x(01)00774-0.

Abstract

Porphyrinogens with modified propionate side chains bearing methyl substituents were found to be modest substrates for coproporphyrinogen oxidase; the results indicate that alteration of the substituents involved in secondary binding interactions has a comparable affect to modifying the side chain that undergoes degradation at the catalytic site.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Catalysis
  • Chickens
  • Chromatography, High Pressure Liquid
  • Coproporphyrinogen Oxidase / drug effects*
  • Coproporphyrinogens / chemistry*
  • Erythrocytes / drug effects
  • Erythrocytes / enzymology
  • In Vitro Techniques
  • Kinetics
  • Methylation
  • Protein Binding
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Coproporphyrinogens
  • coproporphyrinogen III
  • Coproporphyrinogen Oxidase