Specificity and inhibition studies of Armillaria mellea protease.
The action of Armillaria mellea protease has been evaluated on a number of polypeptide substrates. It has been shown to split the Pro7-Lys8 bonds in both native and oxidised lysine-vasopressin and the Ser11-Lys12 bond in glucagon. No other splits were detected in these substrates. The enzyme also caused extensive degradation of S-carboxymethyl lysozyme, S-carcoxymethyl pepsinogen and oxidised ribonuclease. A. In each case the only new amino-terminal residue to appear was lysine. A. mellea protease was inhibited by the chelating agents 1,10-phenanthroline, alpha, alpha'-bipyridine and imidazole. The pK1 values (negative log10 of concentration required for 50% inhibition) for these three inhibitors were 3.9, 3.4 and 1.1, respectively. Lysine, S-2-aminoethylcysteine and short chain aliphatic amines also proved to be relatively good inhibitors of A. mellea protease while arginine was a poor inhibitor.
D000588:Amines / Q000494:pharmacology; D000596:Amino Acids / Q000032:analysis; D001487:Basidiomycota / Q000201:enzymology*; D002614:Chelating Agents / Q000494:pharmacology; D005934:Glucagon / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008236:Lypressin / Q000378:metabolism; D008239:Lysine / Q000494:pharmacology; D009113:Muramidase / Q000378:metabolism; D010435:Pepsinogens / Q000378:metabolism; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*
D000588:Amines; D000596:Amino Acids; D002614:Chelating Agents; D010435:Pepsinogens; D008236:Lypressin; D005934:Glucagon; D009113:Muramidase; D010447:Peptide Hydrolases; D008239:Lysine