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• W1517505826 abstract "Abstract Certain histidine residues in bovine pancreatic ribonuclease and deoxyribonuclease react with iodoacetate about 1000 times faster than free histidine reacts. The mechanisms of these facilitated, active-site-directed reactions were investigated by study of the kinetics of carboxymethylation with reagents with varied leaving groups: chloride, bromide, iodide, and tosylate. With ribonuclease, the rate of reaction gave hyperbolic dependence on the concentration of reagent. The data fit a Michaelis-Menten mechanism, with dissociation constants of 8 to 24 mm for the various reagents. The similar magnitudes of the constants lead to the conclusion that the reagents bind (reversibly) in a common way to the enzyme. The pseudo bimolecular rate constants for reaction (after correction for the differing inherent reactivities of the reagents) were also similar, indicating that the leaving group is not very important in the mechanism. These studies support the proposal that the reaction of haloacetates with ribonuclease is facilitated by ionic attraction of the carboxylate ion by a protonated imidazole while an unprotonated imidazole displaces the halide ion. In contrast, the kinetics of carboxymethylation of the Cu2+-Tris complex of deoxyribonuclease showed that the reagents bound loosely, with dissociation constants of 130 mm or larger. Furthermore, the corrected, pseudo bimolecular rate constants increased as the size of the leaving group decreased. The larger groups may be more sterically hindered in the reaction; alternatively, the smaller groups may be attracted more to the electrophilic Cu2+. In either case, during carboxymethylation, both the carboxylate ion and the leaving group interact with DNase. While the carboxymethylation of RNase may be facilitated by the precise orientation of the reagent, the carboxymethylation of DNase may be facilitated by electrophilic catalysis. Tosylglycolate (carboxymethyl p-toluenesulfonate) was prepared and tested as an analog of the haloacetates. The reagent was about one-eighth as reactive as iodoacetate with a pyridine base and reacted with the —SH group of cysteine. It carboxymethylated histidines 119 and 12 of ribonuclease with more preference for histidine 119 than did iodoacetate." @default.
• W1517505826 created "2016-06-24" @default.
• W1517505826 creator A5015206461 @default.
• W1517505826 date "1973-07-01" @default.
• W1517505826 modified "2023-09-28" @default.
• W1517505826 title "Mechanisms of Carboxymethylation of Bovine Pancreatic Nucleases by Haloacetates and Tosylglycolate" @default.
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• W1517505826 doi "https://doi.org/10.1016/s0021-9258(19)43647-8" @default.
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• W1517505826 hasPublicationYear "1973" @default.
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