Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi

J Biol Chem. 1980 Feb 10;255(3):839-40.


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.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Humans
  • Myoglobin
  • Peptide Fragments / analysis
  • Peptide Hydrolases / metabolism*
  • Pseudomonas / enzymology*
  • Ribonucleases
  • Substrate Specificity
  • Whales


  • Amino Acids
  • Myoglobin
  • Peptide Fragments
  • Ribonucleases
  • Peptide Hydrolases