Complete the sentences to explain why is it important that ES is not too much more stable than E + S by filling the blanks with appropriate words given below. Determine how this is related to the lock and key versus induced fit models of enzyme function.

lock and key, enzyme-substrate complex, induced fit, transition state, decreases, remains about the same, substrate, increases

Enzymes catalyze reaction by stabilizing the . If the enzyme binds to the substrate too well, the activation energy for the catalyzed reaction . Thus, the enzyme binds best to the and the activation energy .
In the model, the enzyme binds to the most efficiently.
In the , both the enzyme and change their structure upon binding in a way that favors the formation of the enzyme-substrate complex .
Thus, when comparing the models, the model lowers the energy of the transition state more.

Explanation:

Enzymes catalyze reaction by stabilizing the _transition state. If the enzyme binds to the substrate too well, the activation energy for the catalyzed reaction ___increases. Thus, the enzyme binds best to the _substrate and the activation energy decreases.

In the _lock and key model, the enzyme binds to the _substrate most efficiently.

In the __induced fit, both the enzyme and _substrate change their structure upon binding in a way that favors the formation of the _enzyme-substrate complex _.

Thus, when comparing the models, the _lock and key model lowers the energy of the transition state more.

The lock and key model suggests that enzyme and substrate are like complementary shapes and when the bind they fit into each other.

The induced fit model proposed that when the active site of an enzyme binds to a substrate, it changes it conformation (shape) and as such other molecules cannot bind.

ya the other dude is right

69 is the correct math for the amino acids