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Functional expression and characterization of CYP51 from Candida albicans
Author(s) -
Park HyoungGoo,
Han Songhee,
Lim YoungRan,
Eun ChangYong,
Kim Donghak
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.512.4
Subject(s) - lanosterol , demethylase , candida albicans , fluconazole , biology , corpus albicans , ketoconazole , microbiology and biotechnology , chemistry , gene , biochemistry , antifungal , sterol , epigenetics , cholesterol
An opportunistic fungal pathogen, Candida albicans contains the 10 putative cytochrome P450 (CYP) genes. They seem to play important roles for fungal survival and virulence. Here, we report the identification and characterization of CYP51, a putative lanosterol demethylase. The recombinant CYP51 protein containing a 6×(His)‐tag has been expressed in Escherichia coli and purified. The purified proteins showed the tight binding spectra with lanosterol. It exhibited a lanosterol demethylase activity in reconstitution with rat P450‐NADPH reductase to produce de methylated product in HPLC analysis. Azole compounds affinities of CYP51 enzyme was calibrated with econazole, itraconazole, ketoconazole and fluconazole. All four azoles showed Type II spectra with tight binding affinities to C. albicans CYP51. This study of functional characterization of CYP51 from C. albicans could provide the critical understanding of its role in the processing of pathogenesis. This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2009‐0088150).