Pancreatic trypsin inhibitor and a1-antiproteinase are examples of protease inhi
ID: 15364 • Letter: P
Question
Pancreatic trypsin inhibitor and a1-antiproteinase are examples of protease inhibitors thatA. dramatically decrease the activation barrier for catalysis by binding tightly to the protease.
B. bind a transition state extremely tightly (show significant stabilization of the transition state).
C. are covalent “suicide” inhibitors of the proteases they inhibit, i.e., they form covalent adducts
in the active sites of the target proteases.
D. are bound so tightly as a substrate that they are only very slowly acted upon by the protease
they inhibit and thus act at very low concentrations and are effective for very long time.
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Explanation / Answer
Pancreatic trypsin inhibitor and a1-antiproteinase are examples of protease inhibitors that
A. dramatically decrease the activation barrier for catalysis by binding tightly to the protease.
B. bind a transition state extremely tightly (show significant stabilization of the transition state).
C. are covalent “suicide” inhibitors of the proteases they inhibit, i.e., they form covalent adducts
in the active sites of the target proteases.
D. are bound so tightly as a substrate that they are only very slowly acted upon by the protease
they inhibit and thus act at very low concentrations and are effective for very long time.
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