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Literature summary extracted from

  • Tyndall, J.D.; Sabherwal, M.; Sagatova, A.A.; Keniya, M.V.; Negroni, J.; Wilson, R.K.; Woods, M.A.; Tietjen, K.; Monk, B.C.
    Structural and functional elucidation of yeast lanosterol 14alpha-demethylase in complex with agrochemical antifungals (2016), PLoS ONE, 11, e0167485 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.154 recombinant hexahistidine-tagged enzyme is overexpresssed in a yeast membrane protein expression system Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.154 X-ray crystal structures of hexahistidine-tagged Saccharomyces cerevisiae lanosterol 14alpha-demethylase in complex with its substrate lanosterol, the pseudosubstrate estriol and the triazole drugs itraconazole, posaconazole, fluconazole and voriconazole Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.154 Y140F 3.3fold reduction in susceptibility to S-prothioconazole Saccharomyces cerevisiae
1.14.14.154 Y140H 4.3fold reduction in susceptibility to S-prothioconazole Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.154 difenoconazole whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae
1.14.14.154 fluquinconazole whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae
1.14.14.154 oxo-prothioconazole whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae
1.14.14.154 Prochloraz whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae
1.14.14.154 prothioconazole whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae
1.14.14.154 prothioconazole-desthio whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae
1.14.14.154 tebuconazole whole-cell antifungal activity of both the R- and S-enantiomers of tebuconazole, prothioconazole, prothioconazole-desthio, and oxo-prothioconazole as well as for fluquinconazole, prochloraz and a racemic mixture of difenoconazole are determined. In vitro binding studies with the affinity purified enzyme are used to show tight type II binding to the yeast enzyme for all compounds tested except prothioconazole and oxo-prothioconazole. Comparison with CYP51 structures from fungal pathogens including Candida albicans, Candida glabrata and Aspergillus fumigatus provides strong evidence for a highly conserved CYP51 structure including the drug binding site Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.154 Saccharomyces cerevisiae A6ZSR0
-
-
1.14.14.154 Saccharomyces cerevisiae YJM789 A6ZSR0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.154
-
 Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.14.14.154 CYP51
-
 Saccharomyces cerevisiae
1.14.14.154 ERG11
-
 Saccharomyces cerevisiae
1.14.14.154 lanosterol 14alpha-demethylase
-
 Saccharomyces cerevisiae