Which of the following statement is FALSE about enzymes? Enzymes are unconsumed during a biochemical reaction. Enzymes' denaturation cannot affect its biological activity. Enzymes speed up the rates of a biochemical reaction by lowering its activation energy. Enzymes do not alter the position of the equilibrium.
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- Which 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.Which of the following statements is false? Macromolecules are able to take on characteristics or functions that their building blocks do not have. Unfavourable reactions can sometimes proceed by being coupled to favourable ones. Compartmentalization is often used to separate biochemical reactions. Biomolecules in the cell exist in relative isolation from each other and rarely have an opportunity to interact. Macromolecules are often derived from smaller building blocks such as amino acids.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
- Another of the six enzyme classes is which of the following? enzymes catalyze. These classes include the transferases, isomerases, and ligases. All enzymes can be categorized in one of six major classes based on the reactions the proteases kinases hydrolases phosphatases endonucleases An important factor that influences the rate of a biochemical reaction is the temperature. Raising the temperature of a biochemical reaction has which effect upon the kinetics of the reaction? a) b) c) d) e) increases the free energy of the reactants increases the free energy of the transition state decreases the free energy of the reactants decreases the free energy of the transition state decreases the free energy of the productsWhich 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.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.
- Homeostasis is important for all of the functions of the human body. Why is maintaining homeostasis important for enzymes? Group of answer choices: To maintain their normal structure and function To prevent substrate from binding to the enzyme To allow the substrate to bind forever To cause the enzyme to fold differently for each reactionEnzymes are important biological catalysts because they: Lower the activation energy of a biochemical reaction Lower the entropy of a biochemical reaction Increase the free energy of a biochemical reaction Supply the energy to initiate a biochemical reactionEnzymes 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.
- Question 4 The main function of catalase is to break bonds between amino acids in proteins and aid in digestion break bonds between monosaccharides in starch and aid in digestion break down hydrogen peroxide into oxygen and water cause browning of fruits and vegetables when they are cut or damaged Question 5 What happens to an enzyme when it is denatured? Its 3D shape changes and it can no longer catalyze the reaction. It modifies the shape of the active site and increases the rate of reaction under optimal conditions. Its 3D shape and all levels of its structure are disrupted, so it can no longer catalyze the reaction. O Its primary structure is disrupted and the enzyme breaks down, making it unable to catalyze the reaction. 1 pts 0.75 ptsEnzymes 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.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.