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• W2034674216 abstract "Salting-out (salting-in) effects in the kinetics of enzymatic reactions are discussed. The importance of careful consideration of these effects in pKa's and other equilibrium constants is stressed. Particular attention is given to the kinetic salting effect which reflects enzyme molecule changes upon reaction that affect interactions of the molecule with the surrounding medium. In acyl-chymotrypsin deacylation, the kinetic salting effect depends on whether the substrate acyl group is situated in the substrate binding center (the hydrophobic slit) or not. A new effect, the salt-dependent promotion, has been found; it is caused by a change in the kinetic salting effect upon modifier binding: the bound modifier mimics the substrate acyl group in the hydrophobic slit. These results are explained by the hypothesis that the hydrophobic slit is compressed in the transition state. The observed salt effect also depends on pH. This is explained by salt dependence of pKa's and individual rate constants. In the neutral pH region the kinetic salting effect, as well as the salting effect in the catalytic center deprotonation constant, Ka1, must be considered. At high pH's a conformational change occurs: the group with pKa 8.8 in the free enzyme displays in acyl-chymotrypsins pKa values above 11." @default.
• W2034674216 created "2016-06-24" @default.
• W2034674216 creator A5054699929 @default.
• W2034674216 date "1990-06-01" @default.
• W2034674216 modified "2023-09-25" @default.
• W2034674216 title "Kinetic salting effect as a promising tool in the investigation of enzyme molecule changes upon reaction: Deacylation of acyl-chymotrypsins" @default.
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• W2034674216 doi "https://doi.org/10.1016/0045-2068(90)90045-7" @default.
• W2034674216 hasPublicationYear "1990" @default.
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