PaperInvestigation of the substrate-binding site of human plasmin using tripeptidyl-p-nitroanilide substrates
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Add time:09/07/2019 Source:sciencedirect.com
The hydrolysis of tripeptidyl-p-nitroanilides by human plasmin /EC 3.4.21.7./ was studied and the kinetic parameters were determined. The individual contributions of the amino acid side chains at the P1-P4 subsites to the kinetic parameters were calculated by regression analysis. The highest contributions yielded the structure of an “optimum” substrate, D-Ile-Phe-Lys-pNA. Its predicted kinetic parameters, Km = 9.6 × 10-6 M and kcat/Km = 284 789 M-1s-1, appeared to be about 40 times as good as those of H-D-Val-Leu-Lys-pNA /S-2251/ applied for the determination of the plasminogen and plasmin content of blood in various laboratories. At the S2-S4 segment in the binding site, which interacts with the P2-P4 moieties of the substrate, plasmin favoured uniformly hydrophobic substituents.
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