BIOMOLECULESPlease answer the questions properly.- Multiple choice1. Which of the following choices is correct about theactive site of an enzyme?A. contains amino acids without sidechainsB. remains rigid and does not change shapeC. is found at the center of globular enzymesD. none of the above choices is correct2. The induced fit model describes one methodwhere an enzyme's active site can accept somespecific substrate. Which of the following explainsthe "induced fit" model regarding enzyme-substratebinding?A. upon binding to the enzyme, the substrate alreadyfits perfectly into the active siteB. upon binding to the enzyme, the substrate changesits own shape so that it fits perfectlyC. upon binding to the enzyme, the substrate changesthe shape of the enzyme so that it fits perfectlyD. all of these are examples of induced fit

The area of an enzyme where the substrate is bound is called the active site. It is created from…

Answered: - Multiple choice 1. Which of the…

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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11. Compound X permanently bind by covalent bonds to allosteric site of enzyme C thus completely shutdown the reaction enzyme C. Compound X is best predicted as O A. Activator O B. Competitive inhibitor C. Non competitive reversible inhibitor D. Non competitive irreversible inhibitor 12. There are some terminologies used for enzyme's component as shown in Figure 5. Choose the best term for component labelled Y. * Substite
15) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme 16) Th a. True b. False* reaction rate substrate concentration
V 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km. Estimate the Km from this graph giving the correct units. v/Vmax 1.0 0.5 0.0 0.0 vs [S] for an enzyme. Enzyme Activity vs [Substrate] :0.2 0.4 Substrate (HM): 0.6 (b) If the Vmax = 25 mmoles per minute per µmole of enzyme calculate the Keat and the specificity constant."
3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
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1. What is the difference between the lock and key model in the induced fit model enzyme-substrate binding? 1a. What factors affect an enzymes catalytic function?
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19. What is the optimal pH for catalase? Why do you think it becomes less effective at high or low pH? 20. Can you think of anywhere in the human body where enzymes would work BEST at a high pH? Please give an example and draw what that graph might look like. 21. What is the optimal temperature for catalase? Why do you think it becomes less effective at high or low temperatures? 22. Can you think of any organisms that would have enzymes specifically adapted to extreme low or high temperatures and would therefore function best at a different part of the graph? Please give an example and draw what that graph might look like.
1. Which of the following are general properties of active sites? MARK ALL THAT APPLY. Group of answer choices Multiple interactions with substrate Not very specific Always hydrophobic Small pocket within enzyme.
8. Enzyme activity can be registered by one form of covalent modification called phosphorylation. True or false 16. The ionized of all amino acids at pH (7.4) has a net charge of zero. True or false 17. Like beans, eggs would be most likely to be deficient in at least one of essential amino acid. True or false

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