WriteCif only statement A is correct,Hif only statement B is correct,Eif both statements are correct,Mif both statements are incorrect.A.An inhibitor that binds somewhere in the enzyme other than the active site isan uncompetitive inhibitor.B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and itdecreases the maximum reaction velocity.

Enzymes are proteinous compounds. They act as catalysts for biochemical reactions. Like inorganic…

Answered: Write Cif only statement A is correct,…

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 is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
Which of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pH
In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor. In each batch, the inhibitor was of a different type: a.Batch 1: competitive inhibitor b.Batch 2:uncompetitive inhibitor c.Batch 3:non-competitive inhibitor Assuming that Vmax = 80 mM s', Km = 8 mM, and Kiof all three inhibitors was 10 mM, which of the inhibitors was the most efficient on Vo? Explain your answer.
WriteC if only statement A is correct, H if only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. A competitive inhibitor would bind at the enzyme's active site.B. As a result, the affinity of the substrate to the active site decreases.
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
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
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
There is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km, namely the inhibition mechanism.... A. non-competitiveB. non-competitive and uncompetitiveC. in-competitive and uncompetitiveD. in-competitiveE. uncompetitive
Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.
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