Review Article Cytochromes P450 in fungi

@article{Bossche1998ReviewAC,
  title={Review Article Cytochromes P450 in fungi},
  author={Hugo F. Vanden Bossche and Lucien M. H. Koymans},
  journal={Mycoses},
  year={1998},
  volume={41}
}
Summary. The article gives an overview on the history of the discovery of P450 cytochromes and on their occurrence in nature, especially on their interactions with metabolic pathways in fungi. The significance of the P450 cytochromes in the ergosterol synthesis as well as in the inhibitory mechanisms caused by imidazole and triazole antimycotics is described is detail. 
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Although no crystal structure is available yet for any fungal CYP51, homology modeling using structures from other origins as template allowed deducing models for fungal orthologs and served to map amino acid changes known from clinical and field isolates to explain CYP 51-based azole resistance.
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This account describes structure and activities of selected agents isolated from various natural sources, including a number of potent antifungals originated fromVarious natural sources.
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Docking study of the newly synthesized compounds showed that all new compounds have similar binding mode in the active site of fungal enzyme P450 cytochrome lanosterol 14α‐demethylase.
Contribution of mutations in the cytochrome P450 14alpha-demethylase (Erg11p, Cyp51p) to azole resistance in Candida albicans.
TLDR
The cytochrome P450 14alpha-demethylase, encoded by the ERG11 (CYP51) gene, is the primary target for the azole class of antifungals and mutations found in the two N-terminal regions only Y132H was demonstrated to be of importance for azole resistance.
Design, Synthesis and Evaluation of New Azoles as Antifungal Agents: a Molecular Hybridization Approach
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Compound 9 containing 2-methyl-5-nitroimidazole moiety proved to be the most potent compound and was more active than the reference drugs fluconazole and ketoconazole against S. cerevisiae.
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