Somorin O, Ameghashitsi L
Chemistry Department, University of Nigeria.
Biochem Int. 1987 Dec;15(6):1189-96.
Trypsin catalyzed hydrolysis of seven new chromogenic arginine substrates, N alpha-benzyloxycarbonyl-L-arginine-3-nitro-5X-anilide (X = H, CF3, SO2CH3, F, Cl, Br and I) were studied. These substrates are suitable for studying electronic effects on trypsin activity. The Km and kcat values for the hydrolysis of each substrate were determined and found to differ significantly for the various substrates. The Hammett plot of the catalytic rate constants gave a straight line with a negative rho value (-0.82) thus indicating that electron withdrawing substituents retard the trypsin catalyzed hydrolysis of the new anilide substrates.
研究了胰蛋白酶催化水解七种新型生色精氨酸底物,即Nα-苄氧羰基-L-精氨酸-3-硝基-5X-苯胺(X = H、CF3、SO2CH3、F、Cl、Br和I)。这些底物适用于研究电子效应对胰蛋白酶活性的影响。测定了每种底物水解的Km和kcat值,发现不同底物之间存在显著差异。催化速率常数的哈米特图给出了一条直线,ρ值为负(-0.82),因此表明吸电子取代基会阻碍胰蛋白酶催化新型苯胺底物的水解。