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  • Title: The lysine-specific proteinase from Armillaria mellea is a member of a novel class of metalloendopeptidases located in Basidiomycetes.
    Author: Healy V, O'Connell J, McCarthy TV, Doonan S.
    Journal: Biochem Biophys Res Commun; 1999 Aug 19; 262(1):60-3. PubMed ID: 10448068.
    Abstract:
    The fruiting body of the basidiomycete fungus Armillaria mellea produces a lysine-specific proteinase which exhibits both potent fibrinolytic activity and a remarkable resistance to denaturing agents. An improved purification protocol has been developed for this enzyme and the sequence of the 26 N-terminal amino acid residues of the pure protein has been determined by gas-phase sequencing. Searches of the SwissProt database showed that the N-terminal sequence of A. mellea proteinase is highly similar to those of lysine-specific metalloendopeptidases from the basidiomycetes Grifola frondosa and Pleurotus ostreatus. These results support the view that the A. mellea proteinase is a member of a novel class of lysine-specific metalloendopeptidases which may be exclusive to basidiomycete fungi.
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