IDENTIFICATION:1.In this model, the substrate still needs to fit into the enzyme like a key, but instead of simply fitting intothe "keyhole," some type of modification is induced in the substrate, enzyme, or both.2.Creatinine Kinase found in skeletal and heart muscle3.Creatinine Kinase found in heart muscle4.Creatinine Kinase found in the brain5. To overcome an energy barrier between reactants and products, energy must be provided to get thereaction started. This energy, which is recovered as the reaction proceeds, is called:A. Potential energy B. Initiation energyC. Reaction energy D. Activation energy6. The active site of the enzyme and substrate have complementary structures, hence they fit togetheras a key fits a lock.7. TRUE or FALSE. Increase concentration of substrate, Increase enzyme action.8. TRUE or FALSE. Decrease concentration of enzyme, Increase enzyme action.

Since you have posted multiple questions, we will provide the solutiononly to the first five…

Answered: 1.In this model, the substrate still…

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

See similar textbooks

Similar questions

15. When an atom or molecule loses one or more electrons, it is said to be: A. energized. B. oxidized. C. polarized. D. reduced. 16. A drug binds to the active site of an enzyme. If it is bound to the active site of the enzyme, it prevents substrate binding. This drug would be considered a(n) A. noncompetitive inhibitor. B. allosteric inhibitor. C. allosteric activator. D. competitive inhibitor. 17. If the AG of a reaction was +31.45 kJoules, which of the following is NOT true regarding this reaction? A. the products have more free energy than the reactants B. the reaction requires an energy input of 31.45 kJoules to proceed. C. The reaction is exergonic D. The reaction is endergonic 18. The large number of alveoli in lungs improve gas exchange by A. decreasing the distance for diffusion B. increasing the surface area for diffusion C. increasing the concentration difference D. changing the diffusion constant 19. Exchange of gases and metabolites between the blood and tissues occurs in…
11. Refer to the figure below. нн Н `NH2 NH2 N' N- 2e-+H* R NAD+ NADH NAD+ functions as a coenzyme in many enzyme-catalyzed reactions. The changes that take place in this coenzyme are the same for all of these reactions and are illustrated in the figure. It is likely that, in these reactions, NAD+ functions as an electron acceptor (reducing agent) in redox reactions. functions as an electron donor (oxidizing agent) in redox reactions. functions as a base in acid-base catalytic mechanisms. functions as an electron donor (oxidizing agent) in redox reactions. functions as an electron acceptor (oxidizing agent) in redox reactions. +Z-
1. define in your own words enzyme 2. explain how enzymes act on a substrate 3. explain the term catalyst 4. what is meant by optimal conditions for enzymes and what are the conditions 5. explain what catalase is: what it helps to break down and into what parts.
In drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mm
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.
3. Which of the following statements regarding enzymes and transition states is true? a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state d. formation of the transition state always assures that the reaction will proceed to product e. none of the above are true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a…
Which of the following is NOT a true statement about the diagram below? Intermediate A Intermediate B End-product Pathway operates 2019 Pearson Education, Inc. O O O O Substrate Enzyme 1- Allosteric site -Enzyme 2 Enzyme 3- Pathway shuts down Bound end-product Feedback Inhibition The end-product None of the other four answers (all are true statements) Each enzyme is specific for its substrate The product of each enzyme reaction becomes a substrate for the next enzyme The diagram shows a metabolic pathway serves as a competitive inhibitor of the substrate on Enzyme 1
4. Using a fluorescent model substrate, you study the kinetics of an enzyme-catalyzed reaction. You observe the below data. Write an equation describing reaction velocity (v) versus [S]. Define and provide a numerical value for any constants that you include in your equation. 16 14 12 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 [S] / mM `N' at 50 mM and observe the following In pilot experiments, you add the putative inhibitor imidazole Doesn't affect anything 1 reaction velocities: [S] = 1 mM5 µM min-1 [S] = 2 mM9 9 µM min-1 [S] = 4 mM 911 µM min-1 Is imidazole a competitive or non-competitive inhibitor? Provide a brief explanation. > 9 00 v/ µM min-

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS