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- W2076280983 abstract "Many enzyme-catalyzed reactions, such as hydrolyses, give rise to two products P 1 and P 2 which are formed in different reaction steps. The second product P 2 is frequently formed by hydrolysis of an intermediate such as an acyl-enzyme or a phosphoryl-enzyme. An alternative nucleophile N introduced into the system forms an additional product P 3 . The present paper is concerned with the kinetics of formation of P 1 , P 2 , and P 3 in the presence of added nucleophiles. A number of alternative mechanisms are considered, and equations are derived for the rates of formation of the three products, and the Michaelis constant, as functions of nucleophile concentration. Graphs are presented showing the variations of these parameters with the concentration of N, for a variety of special cases. Special attention is given to the possibility of specific binding sites for the water and the nucleophile molecules.The data for a number of enzyme systems are discussed with reference to the treatment. For reactions catalyzed by alkaline phosphatase it is concluded that only one mechanism (mechanism VI) is consistent with the results." @default.
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- W2076280983 date "1972-12-01" @default.
- W2076280983 modified "2023-09-24" @default.
- W2076280983 title "Steady-State Kinetics of Enzyme Reactions in the Presence of Added Nucleophiles" @default.
- W2076280983 doi "https://doi.org/10.1139/o72-178" @default.
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