Different primary specificity of porcine pancreatic beta-kallikrein-B and bovine beta-trypsin. A comparative steady-state and pre-steady-state study.
The values of pre-steady-state and steady-state parameters for the beta-trypsin catalyzed hydrolysis of Z-Arg-ONp and Z-Lys-ONp are superimposable between pH 2.4 and 8. At variance, the kinetic parameters for the beta-kallikrein-B catalyzed hydrolysis of Z-Arg-ONp are more favourable than those observed for Z-Lys-ONp and depend on different pKa values. The different primary specificity and the catalytic behaviour of beta-trypsin and beta-kallikrein-B reflect structural differences at their S1 subsite, especially at level of the 226 residue as well as the 217-220 segment.
D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007610:Kallikreins / Q000378:metabolism*; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology*; D011487:Protein Conformation; D013552:Swine; D014357:Trypsin / Q000378:metabolism*
C040761:N-benzyloxycarbonylarginine 4-nitrophenyl ester; C034117:N-benzyloxycarbonyllysine 4-nitrophenyl ester; D001120:Arginine; D007610:Kallikreins; D014357:Trypsin; D008239:Lysine