Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Chapter 6.2, Problem 1TYK
Summary Introduction
Introduction:
The catalysts that are present in the livings cells are called enzymes. The enzymes are protein molecules that may or may not be associated with other molecules like metal ions, vitamins, and so on. The enzymes increase the efficiency of the reaction and help to turn a large number of substrate molecules into products. The enzyme is highly specific in nature and therefore reacts with only a particular type of substrate.
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An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only):
Is un-competitive, meaning the inhibitor binds to a site near the active site.
Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate.
Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate.
Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.
Amylase is an enzyme found in saliva that breaks down starch. The enzyme is currently functioning at its optimal pH of 7 and optimal temperature of 32oC.
Which of the following could result in an increase in the reaction rate?
Providing an environment with a pH of 9.
Decreasing enzyme concentration.
Placing the reactants in an environment at 10oC.
Increasing substrate concentration.
Which of the following statements is false regarding an enzyme's ability to catalyse a reaction?
an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place
an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations
an enzyme allows the reaction to go through a more stable transition state than would normally be the case
an enzyme can weaken bonds in reactants through the binding process
Chapter 6 Solutions
Principles of Biology
Ch. 6.1 - Which do you think has more entropy, an NaCl...Ch. 6.1 - Prob. 1TYKCh. 6.1 - Prob. 2TYKCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.2 - Prob. 1TYKCh. 6.2 - An inhibitor raises the Km for an enzyme but has...Ch. 6.3 - Prob. 1CCCh. 6.3 - Prob. 1TYK
Ch. 6.3 - Prob. 2TYKCh. 6.3 - Prob. 3TYKCh. 6.4 - Prob. 1CCCh. 6.4 - Prob. 1BCCh. 6.4 - Prob. 1TYKCh. 6.4 - Prob. 2TYKCh. 6.4 - Prob. 2CCCh. 6.5 - Prob. 1TYKCh. 6.6 - During the citric acid cycle, what happens to...Ch. 6.7 - Prob. 1CCCh. 6.7 - Prob. 2CCCh. 6.7 - Prob. 3CCCh. 6.7 - Prob. 1TYKCh. 6.7 - Prob. 2TYKCh. 6.7 - Prob. 3TYKCh. 6.8 - Prob. 1CCCh. 6.8 - Prob. 1TYKCh. 6 - According to the second law of thermodynamics....Ch. 6 - Reactions that release free energy are exergonic....Ch. 6 - Prob. 3TYCh. 6 - Prob. 4TYCh. 6 - Prob. 5TYCh. 6 - Prob. 6TYCh. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Prob. 10TYCh. 6 - Describe the mechanism and purpose of feedback...Ch. 6 - What causes the rotation of the y subunit of ATP...Ch. 6 - PRINCIPLES A principle of biology is that living...Ch. 6 - Discuss how life can maintain its order in spite...Ch. 6 - Prob. 2CBQ
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- Enzymes are biological catalysts that enhance the rate of a reaction by: stabilizing the transition state. decreasing the amount of free energy released. increasing the activation energy. increasing the amount of free energy released. O increasing the energy in the transition state.arrow_forwardWhich of the following are effects of catalyst that cause an increase in the rate of reaction? (This is a multi-select question. Select all that apply). a decrease in DG‡. an increase in DG. an increase in temperature. an increase in the energy of the molecules/ions of reactant. an increase in the number of molecules/ions of reactant with enough energy to overcome the activation energy barrier.arrow_forwardWhich of the following is correct regarding enzymes? Enzymes can speed up the rate of reaction by shifting the equilibrium of the reaction forward. Enzymes can make a nonspontaneous reaction spontaneous. Most enzymes are made up of DNA and RNA and are named based on the reaction that they catalyze. Enzymes can increase the rate of a reaction, but do not shift the equilibrium of a reaction.arrow_forward
- Enzymes are key components in biological reactions. Which of the following statements about enzyme function in biological systems is FALSE? Enzymes are key components in biological reactions. Which of the following statements about enzyme function in biological systems is FALSE? Enzymes increase the rate of a reaction, but do not change the free energy of a reaction. Enzymes frequently work in metabolic pathways, such that the activity of one enzyme can affect the activity of a second enzyme in the pathway by altering the concentration of a substrate or product of the second enzyme. Enzymes will alter the equilibrium of a reaction such that the enzyme increases the exergonic reaction relative to the endergonic reaction. Even if the enzyme forms a bond with a substrate during a reaction, the enzyme returns to its original form at the end of the reaction.arrow_forwardExplain with an example the statement: Enzymes enhance reactions but are not consumed in the reaction.arrow_forwardWhich of the following is NOT true about enzymes? Enzyme inhibitors interact reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values. Enzymes typically act under milder conditions of temperature and pH than non-enzyme chemical catalysts. Zymogens are the inactive precursors of enzyme. Nucleophilic groups can catalyze reactions through the transient formation of covalent bonds with the substrate. Transition state stabilization can significantly increase the activation energy for a reaction.arrow_forward
- Use the following graph to diagram the energetics of a chemicalreaction, with and without an enzyme. Be sure to position reactantsand products at appropriate points and to indicate the stages in thereaction and the energy levels.arrow_forwardWe can increase the rate of a reaction by decreasing the activation energy. And, we can do it by using an enzyme. Explain how enzyme decrease the activation energy.arrow_forwardWhich statements are true? The transition state is the highest free energy that a reaction reaches during its progress from reactants to products. Enzymes alter the free energy of the transition state but not its chemical nature. High affinity binding of substrate by enzymes alters the equilibrium between reactants (substrates) and products. High affinity binding of substrate by enzymes can impede reaching the transition state. Steric and electrostatic interactions between the enzyme and substrate usually disfavor the ground state of substrate and favor the formation of the transition state. If ∆G‡(catalyzed) is less positive than ∆G‡(uncatalyzed) then the enzyme is enhancing the rate of the reaction. Low affinity binding of substrate by the enzyme must always lead to a slower rate of reaction compared to the uncatalyzed rate. There is no barrier to substrate binding to an enzyme, only to the chemical step.arrow_forward
- The Michaelis constant: depends on the concentration of the enzyme. displays the maximal rate of the reaction, when it is much less than the substrate concentration. displays the maximal rate of the reaction, when it is equal to the substrate concentration. displays zero-order kinetics, when the it is equal to the substrate concentration. describes the properties of the enzyme.arrow_forwardWhich of the following will occur if there is an increase in enzyme or substrate concentration? interfere with the reaction. increase the rate of reaction. decrease the rate of reaction. not change the rate of product produced reduce the rate of product produced.arrow_forwardAn enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…arrow_forward
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