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Part A.) A plot of reaction velocity (rate) as the ordinate versus pH (abcissa) for enzyme catalysed reactions most frequently yields a:

bell shaped curve

straight line of positive slope

straight line of negative slope

sigmoid curve

Part B In a case of competitive enzyme inhibition, the inhibitor:

1. binds at the same site as the substrate

2. does not actually bind to the enzyme but alters the conformation of the enzyme by introducing disulfide bonds.

3. binds at a site other than that at which the actual substrate binds

4. binds to a second subunit of the protein to which the substrate does not bind.

5. binds to the substrate and thereby reduces binding of the substrate

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Lelia LubowitzLv2

13 Dec 2019

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Related questions

A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the following descriptions and examples by sorting each item into the appropriate bin.

The bins are: irriversible inhibition, compenitive inhibition, mixed inhibition

The phrases to sort are:

-Tamiflu, a transition state analog, reversibly binds to neuraminidase

- Inhibitor may perminantely modify an enzyme

-DIPF permanently modifies the hydroxyl group of a Ser residue at the active site

- the AL3+ ion binds to acetylcholinesterase or to the acetylcholinesterase-substrate complex

- binding by the inhibitor does not affect VMax

-Binding by the inhibitor decreases VMax

33-To stabilize the transition state complex, which of the following must be lowered? A) Initial energy state B) Activation energy C) Net energy change D) The Vmax B) Final energy state 34- Which of the following statements about allosteric enzymes is CORRECT? A The binding of substrate to any active site affects the other active sites B The plot of initial velocity vs. substrate concentration is a straight line C The Keq of the reaction is increased when allosteric activator is bound D The enzymes contains only one polypeptide chain E Allosteric activators bind to all active sites equally 35. Which statement about the two different models proposed to explain enzyme specificity is CORRECT. a. The substrate changes shape when enzyme binds in the Lock and Key Model. b. The enzyme undergoes a covalent modification when bound to substrate in the Lock and Key Model. c. The active site of the enzyme alternates in conformation between opened and closed in the Induced Fit Model. d. The enzyme changes conformation after binding the substrate in the Induced Fit Model. eÂ·The product structure is altered after it has bound to the enzyme in the Induced Fit Model. 36. An enzymatic reaction proceeds with maximal velocity (Vmax) when A. the substrate concentration is equal to that of a competitive inhibitor. B. allosteric effectors are present. C. the enzyme substrate complex is maximal. D. the substrate concentration exceeds that of a noncompetitive inhibitor. E. all of the substrate is bound to the enzyme. 37. Which of the statements below are incorrect? A With all other factors that modify the rate of the enzyme catalyzed reaction remaining constant as we raise the temperature of an enzyme catalyzed reaction there is an initial increase of velocity with temperature. B. The rate of reaction increases with temperature because there is an increasing number of molecules with sufficient energy to pass over the energy barrier which we call the energy of activation C. Reaction rate increases with temperature until a maximum is reached, when the rate of the reaction will suddenly suddenly fall to zero because the enzyme will be denatured and therefore inactive. D. The reaction rate initially increases as temperature rises owing to increased kinetic energy of the reacting molecules E. Enzymes in crease reaction rates due to their ability to lower the energy barriers for reactions F. None of the above 38- Which of the following is true for the induced fit theory of enzyme action? A. The conformation of the substrate changes before binding to the enzyme. B. The active site changes shape during binding of the substrate C. The substrate fits into a preformed active site through a lock-and-key mechanism. D. Enzymes alternate between conformations where the active site is either open or closed. E. The substrate causes a cleft to form in the enzyme where it subsequently binds

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