Characterization of a Thermostable Lysine-Specific Metalloendopeptidase from the Fruiting Bodies of a Basidiomycete, Grifola frondosa.

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概要

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• A zinc-metalloendopeptidase, MEP, capable of catalyzing specific cleavage of acyl-lysine bonds (-X-Lys-) in polypeptides has been purified 212-fold in a yield of 24.7% from the fruiting bodies of Grifola frondosa, which is a popular edible mushroom called "MAITA-KE" in Japan. The purified enzyme consists of a single polypeptide chain with an apparent molecular mass of 20 kDa and a pl value of 7.46, contains 1 atom of zinc/molecule and can be inactivated with EDTA or 1, 10-phenanthroline. Treatment of MEP with EDTA affords an apoenzyme, whose activity can be fully restored by the addition of Mn2+, Zn2+, Ca2+, or Co2+. Prominent features of MEP are its remarkable heat stability and its high affinity for β-D-glucans and chitin. It hydrolyzes proteins maximally at pH 9-10, liberating only lysylpeptides. Polylysine and lysine copolymers with alanine, phenylalanine, or glutamic acid can serve as good substrates. Lysylalanine was liberated from bovine insulin and its oxidized B chain by the action of MEP. Mass spectrometric analysis by Frit-FAB MS of the fragments generated from horse heart cytochrome c presented unambiguous evidence to corroborate the specificity of MEP for acyl-lysine bonds.

• 社団法人 日本生化学会の論文

著者

• Dohmae Naoshi

  Division Of Biomolecular Characterization Riken

• Hashimoto Yohichi

  Department of Biochemistry, Faculty of Science, Saitama University

• Tsumuraya Yoichi

  Department Of Bilchemistry Faculty Of Science Saitama University

• Takio Koji

  Division Of Biomolecular Characterization Riken

• Nonaka Takashi

  Department Of Basic Medical Sciences Institute Of Medical Science University Of Tokyo

• Ishikawa Hiroko

  Department Of Applied Bioscience Faculty Of Agriculture Ehime University

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