Different primary specificity of porcine pancreatic beta-kallikrein-B and bovine beta-trypsin. A comparative steady-state and pre-steady-state study.
P Ascenzi, E Menegatti, M Guarneri, M Bolognesi, G Amiconi
Index: Biochim. Biophys. Acta 789(1) , 99-103, (1984)
Full Text: HTML
Abstract
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.
Related Compounds
Related Articles:
1994-02-01
[Bioorg. Khim. 20(2) , 182-9, (1994)]
1983-12-01
[Biochem. J. 215(3) , 555-63, (1983)]
1986-01-25
[J. Biol. Chem. 261(3) , 1248-52, (1986)]
1998-11-01
[Biochim. Biophys. Acta 1388(1) , 84-92, (1998)]
2000-09-01
[J. Agric. Food Chem. 48 , 3795-3800, (2000)]