Which statement regarding enzyme activity is CORRECTA A) Enzymes bind their substrates better than the transition state. B) Enzymes bind the transition state better than the reaction produets. C) Enzymes reduce the activation energy required for the reaction to take place. D) Enzymes bind their substrates better than the transition state and ...

Question: If you were designing a transition state analog that would mimic the transition state that occurs duringhydrolysis of a peptide bond by a protease, which of the following characteristics is likely to be important inthe design of your transition state analog?It should have the same free energy as the transition state of the reaction.It should have the same

A transition-state analog: ? a) resembles the transition-state structure of the normal enzyme-substrate complex. b) typically reacts more rapidly with an enzyme than the normal substrate. c) is less stable when binding to an enzyme than the normal substrate. d) stabilizes the transition state for the normal enzyme-substrate complex.

A transition state analog is a molecule that mimics the transition state of a chemical reaction and these compounds are potent enzyme inhibitors because they bind to enzymes with high affinity, mimicking the true transition state, but they can't be further processed thus trapping the enzyme in a non-productive complex.

Enzymes have the greatest affinity for the: (A) Substrate. (B Transition state. (C) Intermediate. (D) Product. (E)None of the above. 2.) Which of the following statements are not true about a transition state analog? (A) Transition state analogs can be used as haptens to generate catalytic antibodies, (B) Transition state analogs are potent ...

Which transition state analog would be the most effective competitive inhibitor of a serine protease such as chymotrypsin? Your solution’s ready to go! Our expert help has broken down your problem into an easy-to-learn solution you can count on.

Science; Biology; Biology questions and answers; Question 38Which of the following is true for the maximal velocity of an enzyme catalyzed reaction?Maximal velocity is reduced in the presence of a transition state analog inhibitor.Maximal velocity may be used to determine KM.

Question: Answer Question 6. A good transition-state analog: Point Received A) B) C) binds covalently to the enzyme. binds to the enzyme more tightly than the substrate. binds very weakly to the enzyme. is too unstable to isolate. D)must be alos i entica to the substrate. E) must be almost identical to the substrate.

Question: 1.) Enzymes have the greatest affinity for the 2 pts each. Enjoy (A)Substrate. 2) Which of the following statements are not true about a transition state analog (A) Transition state analogs can be used as hapiens to generatc catalytic antibodies (B) Transition state analogs are potent inhibitors (B) Transition state.

44.) A transition-state analog: (A) Has a higher K, than the normal substrate. (B) resembles the transition-state structure of the normal enzyme-substrate complex. (C) stabilizes the transition state for the normal enzyme-substrate complex. (D) typically reacts more rapidly with an enzyme than the normal substrate.