An enzyme with a high affinity for its substrate will require more energy to generate an enzyme-transition state complex (the activation energy of the forward reaction) because the energy of the enzyme-substrate complex will be reduced.
Since the ES complex would be in a "energy trough," the activation energy for the transition state would be quite high.
In contrast to the situation where the substrate-enzyme binding is weaker, a tight binding of the substrate to the enzyme will alter the amounts of free substrate and free enzyme. This little modification won't have much of an impact on the reaction kinetics because the substrate concentration is often higher than the enzyme concentration.
It is unlikely that tight binding would result in the active site being altered. Since the enzyme is significantly bigger than the substrate, it is unlikely that it will change shape.
The reaction's forward rate constant will decrease with tight enzyme-substrate binding. It is conceivable that a substrate that is securely bonded would not easily change its shape as it passes from the transition state to the products.
High enzyme substrate affinities will result in a decrease in the energy of the enzyme-substrate complex and an increase in the energy needed to generate the enzyme-transition state complex (the activation energy of the forward reaction).
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