Different substrate specificities of lanosterol 14α-demethylase (P-45014DM) of Saccharomyces cerevisiae and rat liver for 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol

This publication has 13 references indexed in Scilit:

• The 3-hydroxy group of lanosterol is essential for orienting the substrate in the substrate site of cytochrome P-45014DM (Lanosterol 14α-demethylase)
  Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1989
• Metabolism of 24,25-dihydrolanosterol analogs by partially purified cytochrome P-45014DM from rat liver microsomes.
  CHEMICAL & PHARMACEUTICAL BULLETIN, 1989
• A single amino acid substitution converts cytochrome P45014DM to an inactive form, cytochrome P450SG1: Complete primary structures deduced from cloned DNAs
  Biochemical and Biophysical Research Communications, 1988
• Primary Structure of the P450 Lanosterol Demethylase Gene fromSaccharomyces cerevisiae
  DNA, 1987
• Effects of buthiobate, a fungicide, on cytochrome P-450 of rat liver microsomes.
  Journal of Pharmacobio-Dynamics, 1985
• Sterol Biosynthesis
  Annual Review of Biochemistry, 1982
• The 14α—demethylation of lanosterol by a reconstituted cytochrome P-450 system from yeast microsomes
  Biochemical and Biophysical Research Communications, 1978
• NADPH-cytochrome P-450 reductase of yeast microsomes
  Archives of Biochemistry and Biophysics, 1978
• Investigation of an S-Adenosylmethionine:Δ24-Sterol Methyltransferase in Ergosterol Biosynthesis in Yeast
  Published by Elsevier ,1970
• Isolation and Purification of an S-Adenosylmethionine: Δ24-Sterol Methyltransferase from Yeast
  Published by Elsevier ,1969