TY - JOUR
T1 - Molybdophyllysin, a toxic metalloendopeptidase from the tropical toadstool, Chlorophyllum molybdites
AU - Yamada, Mina
AU - Tokumitsu, Naoko
AU - Saikawa, Yoko
AU - Nakata, Masaya
AU - Asano, Junpei
AU - Miyairi, Kazuo
AU - Okuno, Toshikatsu
AU - Konno, Katsuhiro
AU - Hashimoto, Kimiko
N1 - Funding Information:
This work was supported by Grant-in-Aid for the 21st Century COE program ‘KEIO Life Conjugate Chemistry’ (Y.S.), Frontier Research Program (K.H.), and the 21st Century COE Program ‘Development of Drug Discovery Frontier Integrated from Tradition to Proteome’ (K.H.) from the Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT).
PY - 2012/11/15
Y1 - 2012/11/15
N2 - 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.
AB - 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.
KW - Agaricaceae
KW - Aspzincin motif
KW - Chlorophyllum molybdites
KW - Deuterolysin family
KW - Isolation and structure determination
KW - Metalloendopeptidase
KW - Molybdophyllysin
KW - Mushroom poisoning
KW - Toxic protein
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U2 - 10.1016/j.bmc.2012.09.036
DO - 10.1016/j.bmc.2012.09.036
M3 - Article
C2 - 23063519
AN - SCOPUS:84867875766
SN - 0968-0896
VL - 20
SP - 6583
EP - 6588
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
IS - 22
ER -