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A: There are two MCQs so we will solve both the MCQs.
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- In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.1. If a molecule is interating with its side chains of an enzymes active site but it is not the substrate of the enzyme what kind of enzyme regulation is this? 2. What is the change in thetype of bond between Ser 80 -> Arg. 3. Will this change cause the complex to be more or less stable. Explain2. One manifestation of cytochrome oxidase deficiency in humans is severe muscle weakness. Briefly explain why. 3. Clostridium bacteria are killed in the presence of molecular oxygen. Would you expect Clostridium to produce catalase? Briefly explain.
- 1) Explain how an enzyme could distinguish between the (now circled) equivalent positions in the above compound. Provide an illustration showing your argument.5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?8. Match each of the following amino acids with the intermediate needed for its synthesis.(a) 3-Phosphoglycerate 1. glutamate 2. serine 3. asparagine (b) oxaloacetate 1. glutamate 2. serine 3. Asparagine
- 1. Please identify the substrate and type of reaction, and explain how these reactions work for the following two enzymes Two enzymes: succinate dehydrogenase and L-amino acid reductase1. What is the difference between the lock and key model in the induced fit model enzyme-substrate binding? 1a. What factors affect an enzymes catalytic function?Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
- Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activationGTP or ATP is produced during the conversion of isocitrate into ketoglutarate succinyl CoA into succinate fumarate into malate malate into oxaloacetateThe assembly of proteins from amino acids is best described as: a. a conversion of kinetic energy to potential energy reaction. b. an entropy reaction. c. a catabolic reaction. d. an anabolic reaction. e. an energy-free reaction.
