Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme?
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Which of the following is NOT a way in which an enzyme can speed up the reaction that it catalyzes? The binding of two substrates in the active site provides the correct orientation for them to react to form a product. Binding of the substrate to the active site can stretch bonds in the substrate that need to be broken. The active site can provide heat from the environment that raises the energy content of the substrate. The enzyme binds a cofactor that interacts with the substrate to facilitate the reaction. The active site of the enzyme can provide a microenvironment with a different pH that facilitates the reaction.
Dominador T.
The enzyme-catalyzed reaction rate will be increased if the energy level of ES can be increased by all EXCEPT: destabilization of ES by strain loss of entropy due to binding of E and S destabilization of ES by distortion destabilization of ES by solvation destabilization of ES by electrostatic effects
Suman K.
The concept of "induced fit" refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water from the substrate.
Adedamola O.
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