6. Using graph C:a. Explain what happens when hypothermia sets in(when enzymes get too cold!)Reaction Rate vs Substrate ConcentrationISubstrate Concentuationb. Does the same thing happen when enzymes get toohot? Why or why not?7. Explain why graph D levels off. Use enzyme and substratein your explanation. Then tell how you could prevent graphD from leveling off.Rate of Reaction - Enzyme Concentration8.Why doesn't it matter if enzymes keep gettingadded to graph E? What would it take to increase the rate of enzyme activity?Then answer the following questions:1. Transfer of Energy and Matter: Is an enzyme used up in a chemical reaction?Explain.2. Transfer of Energy and Matter:How would your diagram be different if the enzyme activity was anabolicinstead of catabolic? (E.g., an enzyme to build muscle proteins).a.Rate of Reaction

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Answered: 6. Using graph C: a. Explain what…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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4. Based on Figure 4, at B, further increase substrate concentration produce no change in rate of reaction. Identify the term suitable at B. * C. Rate of reaction A Substrate c onc entration Figure 4 O A. Optimum temperature O B. Optimum rate of reaction O C. Denaturation D. Point of saturation B.
2. Draw a graph showing a downhill (spontaneous) reaction, that requires some activation energy to get it going. Then draw and clearly label on the graph b. The activation energy for the reaction (use a bracket to indicate the upper and lower limits) c. The free energy change for the reactions (use a bracket to indicate the upper and lower limits) d. How an enzyme will change the energetics of the reaction. I suggest you use a dotted line for the enzyme.
9. Given the Km and Vmax values of three enzymes, A, B and C: Enzyme Km Vmax A 2.0 x 10-3 M 4.0 B 4.2 x 104М 1.8 C 1.0 x 10-3 M 2.5 Which enzyme would have the highest activity? Why?
Choose the correct effect. * increase decrease not change Raising the temperature slightly will... the rate of reaction Boiling temperature will... the rate of reaction Changing the pH toward the optimal pH will... the rate of reaction Introducing a competitive inhibitor will... the rate of reaction
A. How does each of the following irreversible inhibitors interact with the Enzymes? IV. 1. Cyanide 2. Heavy-metal ions B. List an antidote for each of these two poisons and describe how each functions.
3. At what substrate concentration would an enzyme with a keat of 25.0 s¹ and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
V 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km. Estimate the Km from this graph giving the correct units. v/Vmax 1.0 0.5 0.0 0.0 vs [S] for an enzyme. Enzyme Activity vs [Substrate] :0.2 0.4 Substrate (HM): 0.6 (b) If the Vmax = 25 mmoles per minute per µmole of enzyme calculate the Keat and the specificity constant."
3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…
22
The effect of an inhibitor I on the rate of a single-substrate, enzyme-catalyzed reaction was investigated and gave the following results (See table below). a. What is the mode of action (pure competitive, mixed competitive, uncompetitive or noncompetitive) of the inhibitor? Briefly explain your answer. b. Estimate the value of Km and Vmax for uninhibited reaction.
1. The most commonly used method in measuring LD because it produces a positive rate (NADH) and not affected by product inhibition a. Oliver-Rosalki b. Wrecker Method c. Wroblewski Ladue d. Tanzer-Gilbarg 2. most chemistry enzyme tests follow the zero order reaction where the sufficient amount of substrate is availbale the only limiting factor is the enzyme's substrate a. first statement is true and second statement is false b. both statements are true c. first statement is false and second statement is true d. both statements are true 3. any absorbance change per minute of activity when exceeds must be a. double the measurement and analyze again b. repeat analysis c. discared the reagent and open new one d. dilute sample and repeat analysis and multiply the dilution
6. An enzyme catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM/s. What is the reaction velocity when the substrate concentration is (a) 0.25 mM (b) 1.5 mM, and (c) 10 mM?

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6. Using graph C: a. Explain what happens when hypothermia sets in (when enzymes get too cold!) Reaction Rate vs. Substrate Concentration D I Substrate Concentration b. Does the same thing happen when enzymes get too hot? Why or why not? Rate of Reaction-