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- W2082093622 abstract "Three features of activation diagrams applied to enzyme catalysis are discussed. The quantities which should be plotted in the ordinate of activation energy diagrams are the standard state quantities. This is called for by transition state theory (H. Eyring). Small molecule catalysts sometimes afford models for studying certain aspects of enzyme catalysis, but there are features of enzyme catalysis which are seldom emphasized in such studies; most of them concentrate on acceleration. One of these other features is the control which enzymes exert through the activation steps. They utilize multi-barrier mechanisms, and probably maintain near reversibility in these steps. The result is that enzymes catalyze reactions with virtually no side products. Non-macromolecular catalysts are fully expected to, and in fact do, allow formation of side products. Equilibrium constants of reactions in the bound state are sometimes unequal to those in solvent only (Jencks, 1963). This fact, and an analysis of activation diagrams, leads to the conclusion that enzymes may be ground state energy transducers, besides catalysts." @default.
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- W2082093622 date "1969-09-01" @default.
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- W2082093622 title "Activation diagrams in enzyme catalysis" @default.
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- W2082093622 doi "https://doi.org/10.1016/s0022-5193(69)80050-0" @default.
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