Affiliation:
1. Department of Chemistry, University of Waterloo, Ontario, Canada.
Abstract
The potential inducibility of the lanosterol 14 alpha-demethylase (P-45014DM) from Saccharomyces cerevisiae Y222 by xenobiotics was investigated. This enzyme and NADPH-cytochrome P-450 reductase were unaffected by a number of compounds known to induce mammalian and some yeast cytochrome P-450 monooxygenases. Furthermore, dibutyryl cyclic AMP did not affect P-45014DM or P-450 reductase levels, while growth at 37 degrees C resulted in a slight decrease. P-45014DM was found to be specific for lanosterol and did not metabolize a number of P-450 substrates including benzo[a]pyrene.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
2 articles.
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1. Biotransformation of albendazole by fungi;World Journal of Microbiology and Biotechnology;2007-12-25
2. Flux of sterol intermediates in a yeast strain deleted of the lanosterol C-14 demethylase Erg11p;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2005-07