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KMID : 0545120120220010141
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Journal of Microbiology and Biotechnology
2012 Volume.22 No. 1 p.141 ~ p.146
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Functional Expression and Characterization of Recombinant NADPH-P450 Reductase from Malassezia globosa
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Lee Hwa-Youn
Park Hyoung-Goo
Lim Young-Ran
Lee Im-Soon
Kim Beom-Joon
Seong Cheul-Hun
Chun Young-Jin
Kim Dong-Hak
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Abstract
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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.
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KEYWORD
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Reductase, Cytochrome P450, Malassezia globosa, NADPH, 7-Ethoxyresorufin, Coumarin
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