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- 45. Which of the following is/are true? (MARK ALL THAT APPLY) Group of answer choices Enzymes lower the activation energy of the reaction Enzymes bind more strongly to the substrates than the transition state of the reaction Enzymes alter the standard free energy of the reaction. Enzymes force reactions to proceed in only one direction. Enzymes alter the equilibrium of the reaction. PreviousNext1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)26. AN ORGANIC COFACTOR IN A CONJUGATED ENZYME?A. NEITHER VITAMINS NOR MINERALSB. MINERALS C. VITAMINSD. BOTH VITAMINS AND MINERALS 27. WHICH OF THE FOLLOWING STATEMENTS CONCERNING COFACTORS IS INCORRECT?A. VITAMINS CANNOT BE COFACTORSB. SOME COFACTORS ARE METAL IONS C. COFACTOR IS THE NON-PROTEIN PORTION OF ENZYME D. CONJUGATED ENZYMES CONTAIN COFACTORS 28. WHICH OF THE FOLLOWING VITAMINS IS NOT A FAT SOLUBLE VITAMIN? A. VITAMIN E B. VITAMIN C C. VITAMIN A D. VITAMIN D 29. WHAT HAPPENS TO SUBSTRATE MOLECULES AT AN ENZYME ACTIVE SITE?A. ALWAYS REACT WITH OXYGEN B. UNDERGO CHANGE TO A DESIRED PRODUCTS C. BECOME CATALYST C ALWAYS REACT WITH OXYGEN B UNDERGO CHANGE TO A DESIRED PRODUCT D. BECOME COVALENTLY BONDED TO THE ENZYME D. BECOME COVALENTLY BONDED TO THE ENZYME 30. ACTION OF CHEMICAL WARFARE AND ORGANOPHOSPHATE INSECTICIDE ARE BASED ON?A. REVERSIBLE ENZYME INHIBITOR B. IRREVERSIBLE ENZYME INHIBITOR C. REVERSIBLE ENZYME ACTIVATOR D. IRREVERSIBLE ENZYME ACTIVATOR
- ?? = ??A + log [? -]/[??] An enzyme uses histidine as a general acid catalyst. If the active site histidine has a pKa of 6.0, what percentage of the enzyme is active at pH 7.0? a. 1.0 %b. 9.1 % c. 45 %d. 55 % e. 91 %f. 99 % Please break down every step of the HH equation in as much detail as possible and explain why the answer is correct from a logical standpoint.11. Metabolism include catabolic and anabolic reactions. Which of the followings describe anabolic reactions? a) Smaller molecules are generated from the breakdown of larger molecules and nutrients b) Larger molecules are synthesized from small catabolic products c) One molecule transfers a monomer to another molecule to build components of cell d) Anabolic reactions are main source of harvesting electrons and production of ATP1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false 2. These are catalyst that can be used in the monitoring and diagnosis of disease and their remarkable properties make them sensitive indicators of pathologic changes. a. enzymes b. electrolytes c. substrate d. none of these 3. ALT is stavle in serum at refrigirator or temp for up to 3 weeks, indefinitely if frozen AST has the same stability but markedly decreases with freezing a. both statement are true b. both statement are false c. first statement is true second is false d. second statement is true first statement is false
- 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. LyaseWhat are enzymes? What distinguishes enzymes from regular chemical catalysts? On the specificity of enzyme action, please comment. Which factor accounts for their specificity the most? Describe the enzyme catalysis mechanism.Reaction 25.2 Glucose (aq) + PO43- (aq) ⇄ Glucose-PO43- (aq) Reaction 25.2 is nonspontaneous and very slow. Use this information to sketch a reaction diagram for Reaction 25.2. Clearly label the x axis, y axis, products, reactants, and activation energy.
- 22. What is a major benefit of calculating catalytic efficiencies? Group of answer choices It determines whether a catalytic reaction is cooperative It allows you to compare different substrate preferences for an enzyme It tells you the rate of an enzyme reaction It allows you to determine the efficiency of the enzyme being studied47. Which of the following is true under the following conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 mM. (1 nM = 10-9 M, 1 μM=10-6 M, 1 mM = 10-3 M) Group of answer choices Between 0% and 50% of active sites have substrate bound 0% of active sites have substrate bound 50% of active sites have substrate bound 100% of active sites have substrate bound Between 50% and 100% of active sites have substrate bound1. Which of the following terms best describes the progress of the reaction with respect to free energy change?