Properties of proteolytic enzymes isolated from a thermophilic strain of Micromonospora vulgaris 42.
Two proteolytic enzymes, protease A and protease B, were isolated in homogeneous state from the cultural broth of the thermophilic actinomycete Micromonospora vulgaris 42. Their physicochemical properties were studied, i.e., molecular weight (50 000 for protease A and 30 000 for protease B), amino acid composition, N-terminal amino acids (phenylalanine for protease A and alanine for protease B). The specificity of the action of these enzymes was assayed by splitting the B chain of oxidized insulin. Both enzymes are neutral proteases of the thermolysine type.
D000409:Alanine / Q000032:analysis; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000378:metabolism; D008847:Micromonospora / Q000201:enzymology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis / Q000378:metabolism; D010649:Phenylalanine / Q000032:analysis; D013696:Temperature
D000596:Amino Acids; D007328:Insulin; D010649:Phenylalanine; D010447:Peptide Hydrolases; D000409:Alanine