Maitake, Hen of the Woods · 1999 · Journal Article
Low relevanceThe lysine-specific proteinase from Armillaria mellea is a member of a novel class of metalloendopeptidases located in Basidiomycetes.
Grifola frondosa
Key points
- 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
Metadata-grounded summary
Citation 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.
Citation
Healy V, O'Connell J, McCarthy TV, Doonan S (1999). The lysine-specific proteinase from Armillaria mellea is a member of a novel class of metalloendopeptidases located in Basidiomycetes. Biochemical and biophysical research communications https://doi.org/10.1006/bbrc.1999.1151 PMID: 10448068
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