Inhibition and substrate specificity of yeast delta 22-desaturase

Biochem Biophys Res Commun. 1990 Nov 30;173(1):60-6. doi: 10.1016/s0006-291x(05)81021-6.

Abstract

Using yeast microsomes, 23-hydroxysterols were tested as intermediates in the formation of the sterol side delta 22-double bond. No evidence could be found supporting a two-stage mechanism of desaturation via hydroxylation and dehydration. Sterols with various side chains were tested as substrates. Those with alkyl substituents in the 24-alpha position were poor substrates. A series of sterols, including cyclopropyl sterols, were tested as mechanism-based inhibitors without success. Inhibition was observed with an isocyano-sterol.

Publication types

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

MeSH terms

  • Cytochrome P-450 Enzyme System / isolation & purification
  • Cytochrome P-450 Enzyme System / metabolism*
  • Isotope Labeling / methods
  • Microsomes / enzymology
  • Molecular Structure
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins
  • Sterols / chemical synthesis
  • Sterols / metabolism
  • Sterols / pharmacology*
  • Substrate Specificity
  • Tritium

Substances

  • Saccharomyces cerevisiae Proteins
  • Sterols
  • Tritium
  • Cytochrome P-450 Enzyme System
  • Oxidoreductases
  • ERG5 protein, S cerevisiae