One theoretical model of enzyme-substrate interaction explains enzyme catalysis as a function of the stabilization of the transition state by the enzyme active site. This is an example of the:A.catalysis mechanism.B.lock and key mechanism.C.Michaelis-Menten mechanism.D.induced-fit mechanism.

Enzymes facilitate chemical reactions that result in changes to a substrate. How does the induced-fit model of enzymes and substrates explain their function?A. The substrates attach to the enzyme, and the chemical reaction proceeds.B. The enzyme changes shape to fit the substrate, causing the transition state to occur.C. The enzyme induces a change in the substrate but is not changed itself during the reaction.D. Both enzymes and substrates undergo dynamic changes, inducing the transitions state of the substrate.

For an enzyme to be able to catalyze a reaction, the active site must —Ask Studybuddy (Login to use)Group of answer choicesbe occupied by an inhibitorincrease the activation energy levelhave a complementary shape to the substrateD cause the enzyme to be destroyed in the reaction

Which statement explains why the induced fit model is a more accurate description of enzyme/substrate bonding than the lock and key model? Enzymes have active sites that fit most substrates. Enzymes do not need active sites to bond to substrates. Enzymes have rigid active sites with flexible sites for co-factors. Enzymes do have flexible active sites that mold to substrates.

What enables an enzyme to bind specifically to its substrate?

In the _______________ model of enzyme action, the enzyme is restricted to have a fixed conformation accommodating only substrates with complementary geometry.Question 6Select one:a.lock-and-keyb.induced fit