Enzyme kinetics and mechanisms by Kenneth B Taylor

By Kenneth B Taylor

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The steady-state approximation specifies that the rates of all three steps are equal to each other. 19). 20. 21. 22. 23). 24. 24 expresses the initial velocity as the reciprocal of the sum of the reciprocals of the net rate constants. Now it is necessary to examine the implications of reversibility. Each of the irreversible rate constants is actually the rate constant of the flux through that step that actually completes the cycle or goes on to product. The relationship of the irreversible and the actual rate constant is simple, because the step is already irreversible.

There is a general correlation between the formal class of enzyme and the number of substrate and product species, but, of course there are individual exceptions, particularly with enzymes whose formal classification is somewhat ambiguous. Isomerases, for example, have one substrate and one product. In the nomenclature of Cleland [1] they are called uni:uni reactions. Hydrolases as a class of enzymes kinetically also have one substrate but two products, since the concentration of water does not vary in most experiments.

G. metal ions. 5). In such a model the enzyme complex with A, EA, dissociates back to free enzyme, E, and substrate, A, faster than the complex adds the second substrate, B. 5) can be treated as a single enzyme form, the equation is derived, and then the concentration of the individual species comprising the equilibrium segment are related to the total of the equilibrium segment by its equilibrium constant. 13). 14. The convention is that any rate constant in the velocity expression of a step leading away from the rapid-equilibrium segment should be multiplied by an expression describing the fraction of the total concentration of the enzyme species in the segment that is the individual subspecies reacting in that step.

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