Molybdophyllysin, a toxic metalloendopeptidase from the tropical toadstool, Chlorophyllum molybdites

Mina Yamada, Naoko Tokumitsu, Yoko Saikawa, Masaya Nakata, Junpei Asano, Kazuo Miyairi, Toshikatsu Okuno, Katsuhiro Konno, Kimiko Hashimoto

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


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 °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.

Original languageEnglish
Pages (from-to)6583-6588
Number of pages6
JournalBioorganic and Medicinal Chemistry
Issue number22
Publication statusPublished - 2012 Nov 15


  • Agaricaceae
  • Aspzincin motif
  • Chlorophyllum molybdites
  • Deuterolysin family
  • Isolation and structure determination
  • Metalloendopeptidase
  • Molybdophyllysin
  • Mushroom poisoning
  • Toxic protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


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