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- W2039001871 abstract "The stability of acyl-chymotrypsins, in particular O-[β-(3-indole)acryloyl]-Ser195-α-chymotrypsin, towards (aqueous) solvent denaturants has been studied by examining the composition of final products and the kinetics of their formation following incubation in particular denaturing solvents. Near neutral pH, the originally “native” acylenzyme might, a priori, be anticipated to undergo either intramolecular catalytic hydrolysis yielding carboxylate anion, or denaturation yielding the unreactive “denatured” acylenzyme. Near neutral pH, both these processes occur at relatively low velocity (half-lives of the order of minutes or hours) in solvents in which denaturation of “native” unsubstituted enzyme is a rapid process (half-lives of the order of milliseconds or seconds). The partitioning of product between carboxylate anion (the catalytic product) and denatured acylenzyme is a function of the composition of the particul r denaturing solvent. Over a restricted but catalytically significant pH range, the total rate of product formation is unaffected by the particular (solvent-dependent) partitioning ratio, suggesting a common rate-determining intermediate for catalysis and for denaturation. Changes in the catalytic velocity (vp), which can be effected either by the addition of competitive nucleophiles (such as hydroxylamine), or by the introduction of acyl derivatives with different reactivities, lead to corresponding changes in the velocity of denaturation (vp) and hence have little effect on the partitioning ratio (vpvd). This latter result indicates that a covalently modified acylenzyme-nucleophile complex is an obligatory intermediate in both catalysis and denaturation of the acylenzyme, and that catalysis and (variable) conformation of the polypeptide are intimately related. The nature of the structural and chemical changes occurring during catalysis are considered." @default.
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- W2039001871 date "1971-01-01" @default.
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- W2039001871 title "On the relationship between the conformation and the catalyzed reactivity of acyl-chymotrypsin" @default.
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- W2039001871 doi "https://doi.org/10.1016/0022-2836(71)90193-8" @default.
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