Kinesiology 2230A/B Lecture Notes - Lecture 3: Acetyl-Coa, Manganese, Reaction Rate

29 views6 pages

byzantiumsalmon12

15 Jan 2019

School

Department

Course

Professor

For unlimited access to Class Notes, a Class+ subscription is required.

Document Summary

80% of the time it is low intensity. The effect of the catalyst (enzyme) is to lower the free energy of activation for the reaction a. Enzyme changes structure of substrate so it fits better. Raising the temperature raises the average energy of a molecules increases reaction rate. In contrast, the average free energy of a molecules remains the same in uncatalyzed versus catalyzed reactions (conducted at the same temperature) a. b. Increases in temperature change the attraction between different compounds (charges, polarity) i. Enzymes unravel and don"t fit anymore --> cant assist in reaction. Enables fit between enzyme and substrate to be much closer. Coenzyme: organic - derived from vitamins (acetyl coa) Cofactors/coenzymes have a non protein component necessary for particular reaction. Coenzymes have identical functions to cofactors but are organic. Affinity of the enzyme for substrate (greater/lesser attraction of enzyme for particular substrate) a. b. Will affect the rate of an enzyme catalyzed reaction.

Related Questions

26. An enzymatic reaction proceeds with maximal velocity (Vmax) when A. the enzyme is in excess of the substrate. B. allosteric activators are present. the reaction is proportional to substrate concentration. D. the substrate concentration exceeds that of a noncompetitive inhibitor. E. the enzyme is saturated with substrate 27- An enzymatic reaction proceeds with maximal velocity (Vmax) when A. the substrate concentration is equal to that of a competitive inhibitor B. allosteric effectors are present. C. the enzyme substrate complex is maximal. D. the substrate concentration exceeds that of a noncompetitive inhibitor. E. all of the substrate is bound to the enzyme. 28. An enzyme affects the rate of a chemical reaction by A. decreasing the free energy change of the reaction. B. increasing the free energy change of the reaction. C. lowering the energy of activation of the reaction. D. displacing the equilibrium constant. E. raising the energy of activation of the reaction. 29. Which statement is CORRECT? A. Enzymes are small molecules that are heat stable. B. Enzymes affect rates of reactions in the forward and reverse direction. C. Enzymes will determine whether a reaction will take place. D. Enzymes are permanently altered following the conversion of substrate to product. 30. Which of the following statements is TRUE? Enzyme catalysis of a chemical reaction: A. increases the energy of the transition state. B. decreases the change in free energy of the reaction. C. increases the change in free energy of the reaction. D. decreases the change in the free energy of activation. 31. Which of the following statements about enzyme substrate complexes is TRUE? A. At high substrate concentration the rate of the reaction is first order. B. The enzyme concentration is higher than the substrate concentration under physiological conditions. C. Alteration in the conformation of the enzyme may occur when substrate binds. D. Increase in enzyme concentration does not affect the rate of the reaction. 32. All of the following statements about enzymes are correct EXCEPT A. enzymes are usually protein in nature and cause reactions to occur B. enzymes form complexes with substrates and products C. enzymes affect the rate of reactions and are not permanently altered during a reaction D enzymes can undergo structural modification during a reaction E. enzyme specificity requires specific functional groups on the enzyme and substrate

33-To stabilize the transition state complex, which of the following must be lowered? A) Initial energy state B) Activation energy C) Net energy change D) The Vmax B) Final energy state 34- Which of the following statements about allosteric enzymes is CORRECT? A The binding of substrate to any active site affects the other active sites B The plot of initial velocity vs. substrate concentration is a straight line C The Keq of the reaction is increased when allosteric activator is bound D The enzymes contains only one polypeptide chain E Allosteric activators bind to all active sites equally 35. Which statement about the two different models proposed to explain enzyme specificity is CORRECT. a. The substrate changes shape when enzyme binds in the Lock and Key Model. b. The enzyme undergoes a covalent modification when bound to substrate in the Lock and Key Model. c. The active site of the enzyme alternates in conformation between opened and closed in the Induced Fit Model. d. The enzyme changes conformation after binding the substrate in the Induced Fit Model. eÂ·The product structure is altered after it has bound to the enzyme in the Induced Fit Model. 36. An enzymatic reaction proceeds with maximal velocity (Vmax) when A. the substrate concentration is equal to that of a competitive inhibitor. B. allosteric effectors are present. C. the enzyme substrate complex is maximal. D. the substrate concentration exceeds that of a noncompetitive inhibitor. E. all of the substrate is bound to the enzyme. 37. Which of the statements below are incorrect? A With all other factors that modify the rate of the enzyme catalyzed reaction remaining constant as we raise the temperature of an enzyme catalyzed reaction there is an initial increase of velocity with temperature. B. The rate of reaction increases with temperature because there is an increasing number of molecules with sufficient energy to pass over the energy barrier which we call the energy of activation C. Reaction rate increases with temperature until a maximum is reached, when the rate of the reaction will suddenly suddenly fall to zero because the enzyme will be denatured and therefore inactive. D. The reaction rate initially increases as temperature rises owing to increased kinetic energy of the reacting molecules E. Enzymes in crease reaction rates due to their ability to lower the energy barriers for reactions F. None of the above 38- Which of the following is true for the induced fit theory of enzyme action? A. The conformation of the substrate changes before binding to the enzyme. B. The active site changes shape during binding of the substrate C. The substrate fits into a preformed active site through a lock-and-key mechanism. D. Enzymes alternate between conformations where the active site is either open or closed. E. The substrate causes a cleft to form in the enzyme where it subsequently binds

Kinesiology 2230A/B Lecture Notes - Lecture 3: Acetyl-Coa, Manganese, Reaction Rate

Document Summary

Get access

Related Documents

Kinesiology 2230A/B Lecture Notes - Lecture 3: Coenzyme A, Manganese, Reaction Rate

Kinesiology 2230A/B Lecture Notes - Lecture 3: Endergonic Reaction, Exergonic Process, Phosphate

Kinesiology 2230A/B Lecture Notes - Lecture 3: Activation Energy, Citrate Synthase, Phosphofructokinase

Related Questions