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Background
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A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective.lysine or another nucleophilic group on the proteinase, for inhibition to be effective.
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