Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 20, Issue 22, Pages 6583-6588Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.09.036
Keywords
Chlorophyllum molybdites; Agaricaceae; Isolation and structure determination; Toxic protein; Metalloendopeptidase; Deuterolysin family; Aspzincin motif; Molybdophyllysin; Mushroom poisoning
Funding
- 21st Century COE program 'KEIO Life Conjugate Chemistry'
- Frontier Research Program
- 21st Century COE Program Development of Drug Discovery Frontier Integrated from Tradition to Proteome'
- Ministry of Education, Culture, Sports, Science and Technology, Japan
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A toxic protein, dubbed molybdophyllysin, was isolated from the tropical toadstool Chlorophyllum molybdites by following its lethal effect in mice. Analysis of the protein using SDS-PAGE revealed a single 23-kDa band. Sequence analysis of molybdophyllysin tryptic fragments showed that this protein is highly homologous to metalloendopeptidases (MEPs) obtained from edible mushrooms, such as Grifola frondosa, Pleurotus ostreatus, and Armillaria mellea. These proteins include a HEXXH+D zinc-binding motif known as aspzincin. Accordingly, molybdophyllysin is a member of the deuterolysin family of zinc proteases. Molybdophyllysin retained its proteolytic activity at temperatures up to 60 degrees C with an optimum pH of 7.0. The activity was inhibited by both 1,10-phenanthroline and N-bromosuccinimide, but molybdophyllysin exhibited strong resistance to SDS. (C) 2012 Elsevier Ltd. All rights reserved.
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