1. For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: = ES k, and k,’ E + S ES à E and Pk,. a. Use steady state assumption, derive expression for the reaction rate. Where E is concentration of enzyme, S substrate, ES complex of E and S, E = E, – ES. (If you have difficulty in doing it, please consult lecture note) b. Assume K = 0.038 mol.L' at 25 °C, when the substrate concentration is 0.156 Mol.L', the rate of the reaction is 1.21 m mol/L.s. The maximum rate of conversion reaction is reached at high substrate concentrations. Calculate the maximum rate of this enzyme catalyzed reaction.

1. For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: = ES k, and k,’ E + S ES à E and Pk,. a. Use steady state assumption, derive expression for the reaction rate. Where E is concentration of enzyme, S substrate, ES complex of E and S, E = E, – ES. (If you have difficulty in doing it, please consult lecture note) b. Assume K = 0.038 mol.L' at 25 °C, when the substrate concentration is 0.156 Mol.L', the rate of the reaction is 1.21 m mol/L.s. The maximum rate of conversion reaction is reached at high substrate concentrations. Calculate the maximum rate of this enzyme catalyzed reaction.

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 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

See similar textbooks

Similar questions

1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.
2. The pathways for the biosynthesis of the amino acidsglutamine (Gln) and proline (Pro) involve one or morecommon intermediates. Auxotrophic yeast mutantsnumbered 1–7 are isolated that require either glutamine or proline or both amino acids for their growth,as shown in the following table (+ means growth; −no growth). These mutants are also tested for theirability to grow on the intermediates A–E. What is theorder of these intermediates in the glutamine and proline pathways, and at which point in the pathways iseach mutant blocked?Gln +Mutant A B C D E Gln Pro Pro1 + − − − + − + +2 − − − − − − + +3 − − + − − − − +4 − − − − − + − +5 − − + + − − − +6 + − − − − − + +7 − + − − − + − +
Calculate the Km of the maltase reaction with inhibitor X (If inhibitor X changes maltase activity to a Vo of 0.10 mM per minute when [S] = 0.125 mM, and a Vo of 0.25 mM per minute when [S] = 0.50 mM). 0.10 mM 0.20 mM 0.50 mM 1.0 mM 2.0 mM
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.
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.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
1. What are the effects of pH and temperature to catalase? What is the optimum pH and optimum temperature for catalase? 2. Explain why the rate of reaction initially increases with increase in temperature then gradually declines as the temperature is further increased. 3. Is the rate of enzymatic reaction always directly dependent on enzyme concentration? Explain. 4. Explain the effect of substrate concentration on enzyme activity. 5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?
An enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing 0.20 nmoles of enzyme. It is observed that Vmax = 6.6 x 10-3 M/s. What is the kcat value for the enzyme? (HINT: Keep an eye on the units)!!! a. 1.50 x 102 s-1 b. 7.56 x 10-5 min-1 c. 1.32 x 104 s-1 d. 3.3 x 106 s-1
2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.
Select the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the above
1. 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?