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

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

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter3: Cells And How They Work

Section: Chapter Questions

Problem 8SQ: Enzymes _______. a. enhance reaction rates b. are affected by pH c. act on specific substrates d....

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If an enzyme has a maximal activity of pH 6.8 and your reaction buffer is a pH 5.8, what do you need to do to increase the activity of the enzyme? add a dilute solution of sodium hydroxide to the reaction buffer to decrease the pH. add a dilute solution of sodium hydroxide to the reaction buffer to raise the pH. add a dilute solution of acid to the reaction buffer to raise the pH. add a dilute solution of acid to the reaction buffer to decrease the pH.
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
Two substrates (A and B) are used to produce a certain biological product in an enzyme- catalyzed reaction. It is found that both substrates must bind to the enzyme, first Substrate A, then Substrate B before the product is produced. What kind of kinetic mechanism is described? Linear Reaction Ordered Sequential Reaction Random Sequential Reaction Ping Pong Reaction
Please select all of the following statements that are true. Cofactors involve the use of vitamins to assist enzymes Competitive inhibitors bind to the same active site as the substrate. When the substrate binds to the enzyme the reaction rate increases. Non-competitive inhibitors can act as both inhibitors and activators.
Enzymes catalyze the rapid formation of product by: lowering the Gibbs free energy of the product raising the Gibbs free energy of the substrate lowering the activation energy between the substrate and the product raising the activation energy between the substrate and the product changing the AG (the change in Gibbs free energy) of the reaction
When the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increases
Which of the following steps should be followed when performing kinetics experiments? the michaelis constant must be known the enzyme and substrate should not be mixed until just before the absorbance readings are taken reaction rates must be taken until reaction completion enzyme concentration must remain constant
Which of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.
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.
Enzymes are biological catalysts that fulfill the following general reaction mechanism: E+S [ES] [EP] E + P Where E is enzyme, S is substrate, and P is product. Briefly describe how an enzyme is able to speed of the rate of a reaction:
Which of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
Indicate whether each of the following statements about enzyme terminology is TRUE or FALSE. All conjugated enzymes contain a cofactor. An apoenzyme has both a protein and nonprotein part. Metal ions cannot be present in a cofactor. An apoenzyme is present in all holoenzymes. Simple enzymes cannot contain cofactors. A holoenzyme has both a protein and nonprotein part. Metal atoms are present in all conjugated proteins. A cofactor is present in some, but not all, conjugated enzymes.