Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics.

Abstract The presence in the P′ 1 position relative to the LysArg doublet of either Phe, Tyr or Trp residues affects only pro-OT/Np(7–15) flexibility. This has a measurable effect on the dynamics of the peptide. Since the same modifications have a major influence on the K m and V max values of the peptide cleavage, these kinetic parameters should depend on the peptide substrate motions. Therefore, the primary kinetic contribution of substrate cleavage should arise from substrate dynamics rather than from the enzyme.