Non-sterol structural probes of the lanosterol 14 alpha-demethylase from Saccharomyces cerevisiae
1990
Wright, G.D. | Parent, T. | Honek, J.F.
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 11 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.
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书目信息
卷
1040
期
1
页码
95
- 110
ISSN
0006-3002
其它主题
Sterol 14-demethylase; Circular dichroism; Magnetic resonance spectroscopy; Cytochrome p-450 enzyme system; Isolation & purification; Enzyme structure; Analogs; Active site; Substrate analogs; Lanosterol; Structure-activity relationship; Indicators and reagents
语言
英语
类型
Journal Article; Text
2024-02-28
MODS