Solve correctly please,need all part for any helpful ratings. 9. Classify the enzyme catalyzing the following reactionA.oxidatio/reductaseB. lyaseC. kinaseD. transferaseCooC=0A. oxido/reductaseB. lyaseC. kinaseD. transferaseCH₂CH₂H-C10. Classify the enzyme catalyzing the following reactionA. oxido/reductaseB. lyaseC. kinaseD. transferasecooOH₂C-OH-PO,¹Coo+H-C-NH3+.CH₂Coo11. Classify the enzyme catalyzing the following reactionCOO-H-C-HH-C-HCOO™(=H₂CCOOPH-CNH3+CH2CH2coo+-PO,¹сооd=0CH₂cooCOO-C-HH-CCOO-

Protein-based biological entities known as enzymes serve as catalysts in a variety of chemical…

9. Classify the enzyme catalyzing the following reaction A. oxidatio/reductase B. lyase C. kinase D. transferase COOⓇ ć=o CH2 H-C. 10. Classify the enzyme catalyzing the following reaction A. oxido/reductase B. lyase C. kinase D. transferase CH2 Coo O H₂C-OH С009 + H-C-NH3+ PO,¹ CH₂ coo 11. Classify the enzyme catalyzing the following reaction A. oxido/reductase B. lyase C. kinase D. transferase COO- H-C-H H-C-H COO™ H₂C coo I H-C-NH3* CH2 CH₂ Coo + Coo d=0 CH₂ Coo COO- C-H H-C COO-

9. Classify the enzyme catalyzing the following reaction A. oxidatio/reductase B. lyase C. kinase D. transferase COOⓇ ć=o CH2 H-C. 10. Classify the enzyme catalyzing the following reaction A. oxido/reductase B. lyase C. kinase D. transferase CH2 Coo O H₂C-OH С009 + H-C-NH3+ PO,¹ CH₂ coo 11. Classify the enzyme catalyzing the following reaction A. oxido/reductase B. lyase C. kinase D. transferase COO- H-C-H H-C-H COO™ H₂C coo I H-C-NH3* CH2 CH₂ Coo + Coo d=0 CH₂ Coo COO- C-H H-C COO-

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 6TYK: Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent...

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5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
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 activation
In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
Which of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.
1. Which of the following options is a viable way to increase the Vmax of an enzymatic reaction? Increase the amount of substrate present. Increase the amount of enzyme present. Decrease the temperature of the reaction. Decrease the Km of the enzyme.
1. Demonstrate your understanding whether carrier-free biocatalysts should or should not be considered as good biocatalysts. You discussion must be in detail and related to biocatalysis. You can provide detail explanation or provide example. 2. Compare and contrast the following pairs of terms. Relate their similarities and differences to applications in biocatalysis. Zymonomas sp. and Saccharomyces sp.
1. The enzyme that catalyzes the conversion of CH4 + 02 to CH3OH is likely to be classified asa. Isomeraseb. Ligasec. Transferased. Lyasee. Hydrolasef. Oxidoreductase
9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
6. If inhibitor X changes lactase activity to a Vo of 0.333333333333 mM per minute when [S] = 2.0 mM, and a Vo of 0.50 mM per minute when [S] = 3.33333333333 mM, calculate the new Vmax. 1.0 mM per minute 2.0 mM per minute 2.5 mM per minute 5.0 mM per minute 10.0 mM per minute 7. Calculate the new Km of the lactase reaction with inhibitor X. 1.0 mM 2.0 mM 2.5 mM 5.0 mM 10.0 mM 8. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. 1.0 per minute 2.0 per minute 2.5 per minute 5.0 per minute 10.0 per minute Inhibitor X exerts which of the following effects on the above enzyme (lactase)? uncompetitive inhibition mixed noncompetitive inhibition competitive inhibition pure noncompetitive inhibition all of the above
3. How does changes in enzymatic factors affect the native conformation of enzymes? What happens to the enzyme’s native conformation once it is denatured? What structural organization are destroyed by this process? Answer thoroughly.
5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?
6. When a concentrated alkali solution acts on the purine cycle, it breaks down? A. Ester group B. Imidazole nucleus C. Dioxopyrimidine nucleus D. Lactone cycle.