If the rate of binding of an enzyme to its substrate is inhibited, would this affect the catalytic efficiency of an enzyme? If so, how?
The rate of binding of an enzyme to a substrate has very small but significant effect upon the reaction kinetics of the enzyme-catalyzed reaction. In this regard, it is important to understand that the enzyme-catalyzed reaction is uniquely distributed into reaction co-ordinates in order to minimize the input energy and maximize the output energy so that the reaction becomes feasible and thermodynamically stable in nature. Thus, the rate of substrate binding to the enzyme determines how fast the reaction takes place in a sense that easy and quick binding of the substrate would tend to frequent bio-conversion of substrate into product.
Thus, slower is the rate of binding of enzyme to substrate, slower is the overall rate of reaction.
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