STUDIES ON ASPARTASE .8. PROTEASE-MEDIATED ACTIVATION - COMPARATIVE SURVEY OF PROTEASE SPECIFICITY FOR ACTIVATION AND PEPTIDE CLEAVAGE

  • 1 January 1982
    • journal article
    • research article
    • Vol. 14  (4) , 391-397
Abstract
The active species of aspartase from Escherichia coli is further 3- to 5-fold activated upon limited proteolysis with trypsin releasing carboxy-terminal peptides as reported previously. A survey of the protease specificity for the activation revealed that subtilisin BPN'' and several other proteases having far broader substrate specificity than trypsin also activated the enzyme. The results of sequence analyses revealed that subtilisin BPN'' cleaved mainly the serylarginine bond near the carboxy-terminal and released an octapeptide, while trypsin cleaved mainly the arginyltyrosine bond which is adjacent to the subtilisin cleavage site. The protease-mediated activation does not necessarily require a site-specific peptidyl cleavage, but the cleavage of any bond within a certain region centered at arginine, the 8th residue from the carboxy-terminal, is sufficient.

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