Which of the following statements are correct of enzymes that are isoenzymes ofeach other? Choose all correct answers.Iṣoenzymes are affected by the exact same allosteric effectorsIsoenzyme catalyse the same biochemical reactionsIsoenzymes are encoded by the same gene (DNA)Isoenzymes may be subject to different types and levels of regulationIsoenzymes have different primary structures. Which of the following are correct statements pertaining to the glycolytic pathway?Choose all correct statements.Glucose is a substrate for the first reaction of glycolysis,Glycolysis is an aerobic processGlycolysis takes place in the cytoplasm of the cell.Glycolysis is the process by which glucose is converted to acetyl CoAMajor products of glycolysis include pyruvate, ATP and NADHDagoNext PagePage 31 of 36

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
Which of the following statements are true about enzyme regulation via noncovalent interactions? Select all that apply. Molecules can cause a change in enzyme shape because they're able to bind to the enzyme somewhere other than the active site The function of an enzyme is altered by a chemical change in its primary structure, which is called phosphorylation Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to the enzyme's active site Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to a location other than the active site
What are the effects of different light colors in photosynthesis? Different light colors will change the rate of photosynthesis Light color does not affect photosynthesis Carbohydrates are metabolized by light Photosynthesis does not require light
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site
Another of the six enzyme classes is which of the following? enzymes catalyze. These classes include the transferases, isomerases, and ligases. All enzymes can be categorized in one of six major classes based on the reactions the proteases kinases hydrolases phosphatases endonucleases An important factor that influences the rate of a biochemical reaction is the temperature. Raising the temperature of a biochemical reaction has which effect upon the kinetics of the reaction? a) b) c) d) e) increases the free energy of the reactants increases the free energy of the transition state decreases the free energy of the reactants decreases the free energy of the transition state decreases the free energy of the products
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acetyl A-ase Acetate A-ase Deacetylase A-ase B-ase ABC- Isoenzymes Protease Inhibition What is the mechanism of regulation of A-ase? Reversible Covalent modification Isoenzymes What is the mechanism of regulation of A-ase? C-ase Reversible Covalent modification Proteolytic Activation Feedback Inhibition Positive allostery
If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:
An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %
Please select all of the following statements that are true. Cofactors involve the use of vitamins to assist enzymes Competitive inhibitors bind to the same active site as the substrate. When the substrate binds to the enzyme the reaction rate increases. Non-competitive inhibitors can act as both inhibitors and activators.
Which of the following is true of all allosteric enzymes? They have more than one active site on each subunit. They consist of proteins only. They have a nonprotein portion. Binding at one site affects the protein function at a second site. Which of the following explains why glycosides do not undergo mutarotation? There are no longer any stereocenters. There is no longer an anomeric carbon. The ring structure does not open to become the open-chain structure. None of the above is correct.
Which of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site
One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000 How many molecules of urea can one molecule of urease act on in 12.0 min ?

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