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We have previously described Kunitz-type serine proteinase inhibitors purified from  Bauhinia  seeds. Human plasma kallikrein shows different susceptibility to those inhibitors. In this communication, we describe the interaction of human plasma kallikrein with fluorogenic and nonfluorogenic peptides based on the  Bauhinia  inhibitors` reactive site. The hydrolysis of the substrate based on the  B. variegata  inhibitor reactive site sequence, Abz-VVISALPRSVFIQ-EDDnp ( K  m  1.42 M,  k  cat  0.06 s -1 , and  k / K  4.23 x 10 4 M -1  s -1 ), is more favorable than that of Abz-VMIAALPRTMFIQ-EDDnp, related to the  B. ungulata  sequence ( K  m  0.43M,  k  cat  0.00017 s -1 , and  k / K  3.9 x 10 2  M  -1  s  -1 ). Human plasma kallikrein does not hydrolyze the substrates Abz-RPGLPVRFESPL-EDDnp and Abz-FESPLRINIIKE-EDDnp based on the  B. bauhinioides  inhibitor reactive site sequence, the most effective inhibitor of the enzyme. These peptides are competitive inhibitors with  K  I  values in the nM range. The synthetic peptide containing 19 amino acids based on the  B. bauhinioides  inhibitor reactive site (RPGLPVRFESPL) is poorly cleaved by kallikrein. The given substrates are highly specific for trypsin and chymotrypsin hydrolysis. Other serine proteinases such as factor Xa, factor XII, thrombin and plasmin do not hydrolyze  B. bauhinioides  inhibitor related substrates.

biological chemistry

Synthetic Peptides and Fluorogenic Substrates Related to the Reactive Site Sequence of Kunitz-Type Inhibitors Isolated from  Bauhinia : Interaction with Human Plasma Kallikrein