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where + (forward rate constant), (reverse rate constant), and (catalytic rate constant) denote the rate constants, [14] the double arrows between A (substrate) and EA (enzyme-substrate complex) represent the fact that enzyme-substrate binding is a reversible process, and the single forward arrow represents the formation of P (product).
Thus the product formation rate depends on the enzyme concentration as well as on the substrate concentration, the equation resembles a bimolecular reaction with a corresponding pseudo-second order rate constant /. This constant is a measure of catalytic efficiency.
Substrate inhibition of enzymatic product production will inhibit the enzyme's activity, which will lower the reaction rate and reduce the rate of product formation. However, if a product is being produced by cells, then substrate inhibition will narrow product formation by limiting the growth of cells.
The rate of reactant consumption and/or product formation may be abstracted from the change of absorbance over time (by application of Beers' Law). Even when reactant and product spectra display some degree of overlap, modern instrumentation software is generally able to accurately deconvolute the relative contributions provided there is a ...
It differs from competitive inhibition in that the binding of the inhibitor does not prevent binding of substrate, and vice versa, but simply prevents product formation for a limited time. This type of inhibition reduces the maximum rate of a chemical reaction without changing the apparent binding affinity of the catalyst for the substrate (K m ...
The rate of product formation is dependent on both how well the enzyme binds substrate and how fast the enzyme converts substrate into product once substrate is bound. For a kinetically perfect enzyme, every encounter between enzyme and substrate leads to product and hence the reaction velocity is only limited by the rate the enzyme encounters ...
The rate equation for the rate of formation of product P may be obtained by using the steady-state approximation, in which the concentration of intermediate A* is assumed constant because its rates of production and consumption are (almost) equal. [8] This assumption simplifies the calculation of the rate equation.
But the overall rate of reaction is the rate of formation of final product (here CO 2), so that r = r 2 ≈ r 1. That is, the overall rate is determined by the rate of the first step, and (almost) all molecules that react at the first step continue to the fast second step.