Functional Expression and Characterization of Recombinant NADPHP450 Reductase from Malassezia globosa

Malassezia globosa is a common pathogenic fungus that causes skin diseases including dandruff and seborrheic dermatitis in humans. Analysis of its genome identified a gene (MGL_1677) coding for a putative NADPH-P450 reductase (NPR) to support the fungal cytochrome P450 enzymes. The heterologously ex...

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Published inJournal of microbiology and biotechnology Vol. 22; no. 1; pp. 141 - 146
Main Authors Hwa Youn Lee, Hyoung Goo Park, Young Ran Lim, Im Soon Lee, Beom Joon Kim, Cheul Hun Seong, Young Jin Chun, Dong Hak Kim
Format Journal Article
LanguageKorean
Published 한국미생물생명공학회 30.01.2012
Subjects
7-ethoxyresorufin
coumarin
cytochrome P450
Malassezia globosa
NADPH
Reductase
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Summary:Malassezia globosa is a common pathogenic fungus that causes skin diseases including dandruff and seborrheic dermatitis in humans. Analysis of its genome identified a gene (MGL_1677) coding for a putative NADPH-P450 reductase (NPR) to support the fungal cytochrome P450 enzymes. The heterologously expressed recombinant M. globosa NPR protein was purified, and its functional features were characterized. The purified protein generated a single band on SDS-PAGE at 80.74 kDa and had an absorption maximum at 452 nm, indicating its possible function as an oxidized flavin cofactor. It evidenced NADPH-dependent reducing activity for cytochrome c or nitroblue tetrazolium. Human P450 1A2 and 2A6 were able to successfully catalyze the O-deethylation of 7- ethoxyresorufin and the 7-hydroxylation of coumarin, respectively, with the support of the purified NPR. These results demonstrate that purified NPR is an orthologous reductase protein that supports cytochrome P450 enzymes in M. globosa.
Bibliography:The Korean Society for Applied Microbiology
ISSN:1017-7825