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Literature summary for 1.14.14.154 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
Search for more literature for 1.14.14.154

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
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
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
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
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae A6ZSR0
-
-
Saccharomyces cerevisiae YJM789 A6ZSR0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Synonyms

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