Metabolic flux is regulated by both availability of substrates and level ofenzyme activity. Match the mechanism by which enzyme activity is regulated(A, B, C) with a specific example of this type of regulation (1, 2, 3, 4, 5, 6).Each mechanism is associated with two specific examples.Mechanism of RegulationA. Catalytic activityB. CompartmentationC. Enzyme levelsA:1,5; B:3,4; C:2,6OA:1,5; B:3,6; C:2,4A:2,5: B:3.4. C.16Example ofRegulation1. covalentmodification4. subcellularlocalization2. protein synthesis 5. allosteric control3. tissuelocalization6. gene transcription

Enzymes are proteins which increase the rate of biochemical reactions. They carry out the quick…

Answered: Metabolic flux is regulated by both…

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter7: Energy And Metabolism

Section: Chapter Questions

Problem 7TYU

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Similar questions

A certain metabolic pathway can be diagrammed as (see pic1), where A, B, C, and D are the intermediates, and X, Y, and Z are the enzymes that catalyze the reactions. The physiological free energy changes for the reactions are (see pic.2). Solve, (a) Which reaction is likely to be a major regulatory point for the pathway? (b) If your answer in Part a was in fact the case, in the presence of an inhibitor that blocks the activity of enzyme Z, would the concentrations of A, B, C, and D increase, decrease, or not be aff ected?
Enzymes have similar responses to both changes in temperature and pH. The effect of both is on the a. rate of movement of the substrate molecules. b. strength of the chemical bonds within the substrate. c. three-dimensional shape of the enzyme. d. rate of movement of the enzyme.
Which of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.
Select all the true statements about sequential versus concerted models of allostery. a. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme b. No conformational changes occur in either model c. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding d. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable form
Discuss the role of enzymes in metabolic regulation by describing the following mechanisms.11.1Cellular compartmentalization 11.2 Covalent modification11.3 Zymogens
(a) Give the substrate for each of the following enzymes: (i) urease (ii) fructose oxidase (b) What is the difference between competitive and noncompetitive inhibition? (c) In feedback control, what type of regulator slows down the catalytic activity of the reaction series? Why aren't intermediate products in a reaction sequence used in feedback control?
The synthesis of enzymes in response to changing metabolicneeds is referred to as _____________________.
The Michaelis constant: depends on the concentration of the enzyme. displays the maximal rate of the reaction, when it is much less than the substrate concentration. displays the maximal rate of the reaction, when it is equal to the substrate concentration. displays zero-order kinetics, when the it is equal to the substrate concentration. describes the properties of the enzyme.
An enzyme has 10 times greater affinity for substrate "A" than for substrate "B". Which of the following is true? a.) KM of A is 10 times the KM of B b.) The concentration of B is 10 times that of A c.) Vmax of A is 1/10 the Vmax of B d.) KM of A is 1/10 the KM of B e.) Vmax of A is 10 times the Vmax of B
When substrate concentration [S] << Km, the rate of an enzymatic reaction is increased by A. increasing kcat/Km B. increasing total enzyme concentration C. increasing [S] D. A and B E. A, B and C increasing kcat/Km increasing total enzyme concentration increasing [S] A and B A, B and C
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 (desolvation) from the substrate.
Choose the False statement about the parameters that quantitate enzyme catalysis A. V max is the velocity of enzymetic traction at high substrate concentration. B. V max is attained when all enzyme moleculesare present in the form of complex with substrate C. Rate of the reaction is different from the rate constant D. under the certain conditions, michaelis constant Km charatertizes potency of substrate binding. E rate constant is higher at larger substrate concentration

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