Functional Expression and Characterization of Recombinant NADPH-P450 Reductase from Malassezia globosa
- Authors
- Lee, Hwayoun; Park, Hyoung-Coo; Lim, Young-Ran; Lee, Im-Soon; Kim, Beom Joon; Seong, Cheul-Hun; Chun, Young-Jin; Kim, Donghak
- Issue Date
- Jan-2012
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Reductase; cytochrome P450; Malassezia globosa; NADPH; 7-ethoxyresorufin; coumarin
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.22, no.1, pp 141 - 146
- Pages
- 6
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 22
- Number
- 1
- Start Page
- 141
- End Page
- 146
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/20616
- DOI
- 10.4014/jmb.1107.07058
- ISSN
- 1017-7825
1738-8872
- Abstract
- 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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