Resynthesis by Trypsin of the Cleaved Peptide Bond in Modified Soybean Trypsin Inhibitor

Enzymic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitor

“…If this solution is rapidly (<2 sec) titrated to pH 2, the complex immediately dissociates, as one expects from the thermodynamics of the system, but the initial distribution between virgin and modified inhibitor is kinetically controlled (eq 4b, Finkenstadt and Laskowski, 1967). If the inhibitor is quickly isolated by selective ammonium sulfate precipitation, it is found to be >90% virgin.…”

“…The product of this reaction is synthetic trypsin-inhibitor complex. It has been shown (Finkenstadt and Laskowski, 1967) that authentic trypsin-inhibitor complex, prepared with modified inhibitor, can be dissociated to trypsin and virgin inhibitor as follows. At neutral pH a solution of trypsinmodified inhibitor complex contains essentially only complex, although the formal equilibria of eq 4a apply.…”

KLK4 Inhibition by Cyclic and Acyclic Peptides: Structural and Dynamical Insights into Standard-Mechanism Protease Inhibitors

“…Standard-mechanism (or Laskowski-mechanism) inhibitors interact with proteases as tight-binding substrates and behave following the reaction mechanism: where E is the protease, I is the inhibitor, I* is the cleaved inhibitor, and C is a tight-binding complex …”

“…where E is the protease, I is the inhibitor, I* is the cleaved inhibitor, and C is a tight-binding complex [43].…”

“…where E is the protease, I is the inhibitor, I* is the cleaved inhibitor, and C is a tight-binding complex. 46 Subsequent kinetic studies of these inhibitors have extended this mechanism to include additional stable intermediates:…”