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The enzyme could become spatially distorted, thus reducing the ability of the active site to catalyze the reaction. Tight enzyme-substrate binding will reduce the forward rate constant for the reaction. Tight binding of the enzyme to its substrate will pull the substrate out of solution, thus decreasing the driving force for the forward reaction. Tight binding of the enzyme to its substrate will result in the enzyme-transition state complex being higher in energy than with weaker binding. All of the above.

Respuesta :

Answer:

All of the above.

Explanation:

All the given options are the potential disadvantage of an enzyme that have a very high affinity for its substrate.

The enzyme can be distorted spatially and thus reduces the ability to catalyze the reaction of the active site.

The tight binding of an enzyme to a substrate results in enzyme transition state complex which is higher in energy.

The tight binding also pulls the substrate out of the solution and decreases a driving force in the forward reaction.

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