5. Consider the metabolic pathway below.feedback inhibitionenzyme Ienzyme 2enzyme 3substrate I> substrate2> substrate 3substrate 4Which substance is responsible for inhibiting enzyme 17A substrate 1® cnzyme 2© enzyme 3substrate 4

All of our body physiological systems are regulated by different biochemical pathways. A biochemical…

Answered: anzyme I substrate I > substrate 2…

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter4: Energy And Metabolism

Section: Chapter Questions

Problem 3FIO

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In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
2. Describe the following:a. Functions of enzymesb. Benefits of enzymes on moleculesc. Environmental effects of enzymesd. Condition of enzymes after utilize
5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
1) Which of these is NOT a correct statement about enzymes? Group of answer choices Enzyme activity may require a non-protein component (cofactor). Enzymes catalyze chemical reactions and are reusable. Enzymes increase the activation energy (Eact) of reactions. Enzyme activity is affected by the environment (e.g., temperature and pH).
Describe using chemical pathways of 3 Human metabolic diseases, the effects that biosignaling pathways have in their metabolic changes.
1. How much faster is a reaction with the faster enzyme than without a catalyst? * A. Approximately 10 times faster. B. About 100 times faster. C. Approximately 1,000 times faster. D. About 10,000 times faster. E. About 10X^20 times faster. 2. For competitive inhibition * A. KM value decreases B. the value of Vmax decreases C. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate D. None of the above
1. Which of the following options is a viable way to increase the Vmax of an enzymatic reaction? Increase the amount of substrate present. Increase the amount of enzyme present. Decrease the temperature of the reaction. Decrease the Km of the enzyme.
2. Which statement accurately describes the difference between coenzymes and prosthetic groups? A) Coenzymes are covalently bound to their associated enzymes. B) Coenzymes are released from the enzymes active site during 2 reaction. C) Prosthetic groups are metal ions that are located at the enzyme's core. D) Prosthetic groups can transport functional groups between enzymes.
5. Which of the biopolymers is correctly paired with its major function? A. protein : information coding B. nucleic acid : Energy storage C. lipids : information coding D. polysaccharide : energy storage E. none of the above
Why does the substrate bind to the enzyme? 1. The shape of the active site fits the shape of the substrate 2. None are true 3. The shape of the reaction site fits the shape of the substrate 4. The shape of the allosteric site fits the shape of the substrate
1) Answer the following questions about a Vegetarian diet: a) List Pros and Cons of being on the diet. b) List any possible misconceptions that may have been verified or nullified by scientific articles for this diet. c) What biochemical pathway would this diet target?
Which of the following metabolic pathways require(s) molecular oxygen (O2)? a. aerobic respiration b. lactate fermentation c. alcoholic fermentation d. all of the above

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anzyme I substrate I > substrate 2 Which substance is responsible for inhibiting enzy O substrate 1 ® enzyme 2