title: The lysine-specific proteinase from Armillaria mellea is a member of a novel class of metalloendopeptidases located in Basidiomycetes.
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.
authors.affiliation: Department of Biochemistry, University College Cork, Lee Maltings, Prospect Row, Cork, Ireland. v_healy@hotmail.com
authors.forename: V
authors.initials: V
authors.lastname: Healy
authors.forename: J
authors.initials: J
authors.lastname: O'Connell
authors.forename: T V
authors.initials: TV
authors.lastname: McCarthy
authors.forename: S
authors.initials: S
authors.lastname: Doonan
mesh_terms: D000595:Amino Acid Sequence; D001487:Basidiomycota / Q000201:enzymology* / Q000254:growth & development; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005656:Fungal Proteins / Q000302:isolation & purification / Q000378:metabolism; D008666:Metalloendopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
chemical_list: D005656:Fungal Proteins; D010450:Endopeptidases; D008666:Metalloendopeptidases; C028084:Armillaria mellea neutral proteinase