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- W1580497766 abstract "Abstract Spectral changes of chymotrypsin near 290 mµ, previously observed by us in the reaction of chymotrypsin with an inhibitor and with model substrates, have now been shown to accompany the binding to the enzyme of a specific amide substrate, N-acetyl-l-phenylalaninamide. Investigations of these substrate-induced spectral changes by equilibrium experiments and kinetic measurements have yielded the following new information important to an understanding of chymotrypsin-catalyzed reactions. As in the reaction of chymotrypsin with its specific inhibitor diisopropyl fluorophosphate, these spectral changes of the enzyme observed during the amide hydrolysis are associated with an enzyme-substrate complex and not with a covalently bound enzyme-substrate compound. The process associated with these spectral changes precedes the bond-breaking step and is much faster; it has a half-time of less than 3 msec (kobs g 230 sec-1 or g1.1 x 104 m-1 sec-1 for a second order rate constant) at pH 8 and 24°, while the bond-breaking step has a kobs value less than 0.07 sec-1. The dependence of the spectral changes of the enzyme near 290 mµ on substrate concentration allowed the determination of an enzyme-substrate dissociation constant, K's. The dissociation constants pertaining to specific substrates and chymotrypsin have not previously been determined. K's values for N-acetyl-l-phenylalaninamide and δ-chymotrypsin at pH 8 and pH 10 were found to be 15 mm and 51 mm, respectively, while the catalytic rate constant was found to be pH independent in this pH region. This is consistent with our previous experiments which indicate that the pH dependence of the chymotrypsin-catalyzed hydrolysis of the specific amide substrate above pH 8 is due to the pH dependence of the formation of an enzyme-substrate complex and not due to the effect of pH on the bond-breaking step. The K's values for N-acetyl-l-phenylalaninamide and α-chymotrypsin determined from measurements of the substrate-induced spectral changes of the enzyme near 290 mµ were checked by an independent method, the proflavin-displacement method, and excellent agreement between these two methods was obtained." @default.
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- W1580497766 date "1967-09-01" @default.
- W1580497766 modified "2023-10-11" @default.
- W1580497766 title "Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific Substrates" @default.
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- W1580497766 doi "https://doi.org/10.1016/s0021-9258(18)95841-2" @default.
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