Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola
2013
Ueda, Mitsuhiro | Yamamoto, Naomi | Kusuda, Mizuho | Nakazawa, Masami | Takenaka, Shigeo | Miyatake, Kazutaka | Ouchi, Kenji | Sakaguchi, Minoru | Inouye, Kuniyo
A new protease was purified from the culture filtrate of a plant worm, Nomuraea atypicola. The activity of the protease was suppressed by metalloprotease inhibitors such as EDTA and 1,10-phenanthroline, suggesting that it might be a metalloprotease. Its molecular mass was estimated to be 48kDa by SDS-PAGE, and its optimal pH and temperature were pH 8.5–9.0 and 40°C, respectively. The N-terminal amino acid sequence of the metalloprotease was similar to those of fungalysin metallopeptidases of the M36 family from fungi such as Coccidioides posadasii, Pyrenophora tritici-repentis, and Arthroderma gypseum, supporting the idea that it is a fungalysin-like metallopeptidase.
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