Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi.
Previous studies have described the isolation of mutationally altered proteases in Pseudomonas fragi (Noreau, J., and Drapeau, G.R. (1979) J. Bacteriol, 140, 911-916. In the present study, it is shown that one of these proteases cleaves specifically the peptide bonds on the NH2-terminal side of either aspartic acid or cysteic acid residues in oxidized ribonuclease. With myoglobin as the substrate, a similar specificity was observed except that only four out of the six aspartyl bonds present were hydrolyzed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006801:Humans; D009211:Myoglobin; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D012260:Ribonucleases; D013379:Substrate Specificity; D014907:Whales
D000596:Amino Acids; D009211:Myoglobin; D010446:Peptide Fragments; D012260:Ribonucleases; D010447:Peptide Hydrolases