Please explain your answer 13. In an enzyme-substrate reaction, the reaction is favoured becauseelag lulomonA. The transition state of the reaction is de-stabilized.B. The transition state of the reaction is stabilized.C. The activation energy of the reaction is increased.D. The free energy of the reaction to yield products is modified.E. The reaction becomes more exothermic.14. In enzyme kinetics, the turnover number, kcat, isA. Equivalent to the dissociation constant of the enzyme-substrate complex.B. The amount of enzyme available to bind substrate per unit time at the maximumvelocity.C. The amount of substrate transformed per unit time when [S] is low.D. Half the value of the Michaelis constant, KM.E. The amount of substrate transformed per unit time at the maximum velocity.

Enzymes are usually composed of proteins which decreases the activation energy and increases the…

13. In an enzyme-substrate reaction, the reaction is favoured because 1elag ulomon3 A. The transition state of the reaction is de-stabilized. B. The transition state of the reaction is stabilized. C. The activation energy of the reaction is increased. D. The free energy of the reaction to yield products is modified. E. The reaction becomes more exothermic. MKA 14. In enzyme kinetics, the turnover number, kcat, is A. Equivalent to the dissociation constant of the enzyme-substrate complex. B. The amount of enzyme available to bind substrate per unit time at the maximum velocity. C. The amount of substrate transformed per unit time when [S] is low. D. Half the value of the Michaelis constant, KM. The amount of substrate transformed per unit time at the maximum velocity.

13. In an enzyme-substrate reaction, the reaction is favoured because 1elag ulomon3 A. The transition state of the reaction is de-stabilized. B. The transition state of the reaction is stabilized. C. The activation energy of the reaction is increased. D. The free energy of the reaction to yield products is modified. E. The reaction becomes more exothermic. MKA 14. In enzyme kinetics, the turnover number, kcat, is A. Equivalent to the dissociation constant of the enzyme-substrate complex. B. The amount of enzyme available to bind substrate per unit time at the maximum velocity. C. The amount of substrate transformed per unit time when [S] is low. D. Half the value of the Michaelis constant, KM. The amount of substrate transformed per unit time at the maximum velocity.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

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