Conformation and activity of chymotrypsin: the pH-dependent, substrate-induced proton uptake.
Hydrogen ion uptake by chymotrypsin during reversible binding of specific substrate is shown to be due to an ionizing group of the enzyme with a pK(apparent) approximately 9 in the free enzyme. This pK(apparent) is shifted to higher value in the enzyme-substrate complexes. Previous results indicating an equilibrium, controlled by this ionizing group, between active and inactive conformational forms of chymotrypsin are confirmed.
D000577:Amides; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D006863:Hydrogen-Ion Concentration; D007700:Kinetics
D000577:Amides; D002918:Chymotrypsin