title: Kinetics of the hydrolysis of synthetic substrates by horse urinary kallikrein and trypsin.
abstract: The kinetic constants for horse urinary kallikrein and trypsin hydrolysis of BAEE, TAME, bradykinin methyl ester and bradykinyl-Ser-Val-Gin-Val-Ser were determined. The values of the ratio kcat/Km show that (1) kallikrein is catalytically less efficient than trypsin for all the substrates (2) the three esters are equally good substrates for trypsin while horse urinary kallikrein is 100-fold more effective on bradykinin methyl ester than on the other substrates (3) for both enzymes the ester of bradykinin is a better substrate than the tetradecapeptide.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001920:Bradykinin; D004952:Esters; D006736:Horses; D006868:Hydrolysis; D007610:Kallikreins / Q000652:urine*; D007700:Kinetics; D010443:Peptide Chain Termination, Translational; D010455:Peptides; D014357:Trypsin / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D004952:Esters; D010455:Peptides; D007610:Kallikreins; D014357:Trypsin; D001920:Bradykinin