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- FoF1 ATPase is the enzyme that catalyzes ATP synthesis. The enzyme itself is deactivated by ATP. What mode of enzyme regulation is being exemplified? Select the correct response: Trasncriptional control Covalent modification Proteolytic modification Allosteric regulation CompartmentationWhich of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that applyFor the electron transport chain, all are inhibitors except: Select one: O a. Antimycin A O b. fluoroacetate Oc. Amytal O d. NaN2
- Match each reaction description to the type of enzyme that catalyzes the reaction. 1. Oxidation and reduction of compounds 2. Transfers a functional group from one compound to another compound 3. Utilizes water to break bonds within a compound 4. Addition/removal of a group of atoms and bonds within a compound 5. Forms a bond between two compounds A. Ligase B. Transferase C. Hydrolase D. Oxidoreductase E. Isomerase F. LyaseAn 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…Potassium cyanide is a poison which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? c. Competitive inhibition D. Uncompetitive inhibition A. Irreversible inhibition B. Noncompetitive inhibition 10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase В. Нydrolase C. Isomerase D. Ligase 11. Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? C. Isomerase D. Ligase A. Kinase В. Нydrolase
- Which of the following best characterizes ANABOLISM? 1.It is largely exergonic reaction because it releases energy in the form of heat 2.It is involved in the building up process from polymers to monomers 3.Reactions are usually oxidative and degradative 4.Plays a crucial role in growth repair and maintenance of body structuresWhich of the following statements is true of all enzymes? A They are soluble in water. B They have a quaternary structure. They have only one active site. D They catalyse anabolic reactions. CWHAT MAY HAPPEN IF THE FOLLOWING ENZYMES IS ABSENT? answer briefly. 1. Oxidoreductases 2. Transferases 3. Hydrolases 4. Lyases 5. Isomerases 6. Ligases
- Which of the following statement/s is/are TRUE of enzymes? 1. They increase the rate of reaction by stabilizing the transition state. II. They raise activation energy to shift the equilibrium to favor the products. . They lower activation energy by altering the products of a reaction. O l and III O Il and III O III only o l onlyMatch the enzyme name to the description of the type of reaction that it catalyzes. Each choice can only be used once. 1. Transfers a hydride ion in a redox reaction and decarboxylates. 2. Forms a double bond through a dehydration reaction. 3. Combines an aldose and a ketose together in the first step and then cleaves the intermediate molecule into a new aldose and new ketose. Is NOT sensitive to a Vitamin B1 deficiency. 4. Acts as both an enzyme and a scaffold for the formation of a glucose homopolymer. 5. Transfers the gamma phosphoryl group from ATP to a carbohydrate. answer choices: a. glycogen synthase b. glycogenin c. enolase d. PFK-1 e. G6P f. transketolase g. transketolase h. glyceraldehyde 3 phosphate dehydrogenase i. 6 phosphogluconate dehydrogenase Please answer completely will give rating surelyWhich of the following statements is correct about Cytochromes? Select one: O a. Cytochrome a + a3 called cytochrome oxidase O b. Coenzyme Q is members of the cytochromes. c. the cytochrome iron atom is reversibly converted from its ferric (Fe*) to its ferrous (Fe2+) O d. Each contains a heme group
