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(a) Cleavage of a nitroanilide peptide substrate for both chymotrypsin and CypA results in two kinetic events corresponding to cleavage of trans substrate and cis–trans isomerization. (b) These events are fit to a double exponential to determine the apparent relaxation rate kobs. Plotting either CypA or acetylated CypA concentration against kobs and fitting to kobs = (kcat/KM)[CypA] gives kcat/KM.
