Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10771525 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
The regulation mechanism for expression of versatile peroxidase MnP2 by the basidiomycete fungus Pleurotus ostreatus was examined using chemically defined synthetic media. Expression of MnP2 was down-regulated at the transcription level by nutrient nitrogen, e.g., NH4+, arginine or urea. As is often the case with other fungal manganese peroxidases, active MnP2 was not detected when Mn2+ was omitted from the culture, while mnp2 transcription was barely affected by Mn2+. However, Mn2+ can be substituted by an MnP2 substrate, Poly R-478, since active MnP2 was detected extracellularly when the compound was added to the culture without Mn2+. Enzyme stability assays with the purified MnP2 indicated an indispensable requirement for a substrate that can be used to complete the catalytic cycle, and avoid inactivation resulting from an excess H2O2. This report is the first of the Mn2+-independent production of an active versatile peroxidase by P. ostreatus.
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Authors
Hisatoshi Kamitsuji, Yoichi Honda, Takashi Watanabe, Masaaki Kuwahara,