Non-sterol structural probes of the lanosterol 14 alpha-demethylase from Saccharomyces cerevisiae.
A number of non-sterol iron-liganding molecules were used to probe the active site of the lanosterol 14 alpha-demethylase from Saccharomyces cerevisiae. Simple bi- and tricyclic aromatic amines were found to exhibit Type II binding spectra with the demethylase. Stereochemical and positional effects appear to play critical roles in the binding of these compounds to the demethylase. These compounds have been used to generate additional active-site structural information on this enzyme, currently a target for the development of new antifungal agents.
Department of Chemistry, University of Waterloo, Ontario, Canada.
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Wright
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Parent
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Honek
D000588:Amines / Q000138:chemical synthesis / Q000494:pharmacology*; D001665:Binding Sites; D002942:Circular Dichroism; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification / Q000378:metabolism*; D007202:Indicators and Reagents; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008861:Microsomes / Q000201:enzymology; D010088:Oxidoreductases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D058886:Sterol 14-Demethylase; D013329:Structure-Activity Relationship
D000588:Amines; D007202:Indicators and Reagents; D008024:Ligands; D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; D058886:Sterol 14-Demethylase