4AI. Refer to the figure below and answer the following questions:45555665PH7758.5010B1520253035Temperature (°C)4045Legend: Blue - wild-type ß-galactosidase; Red - mutant ß-galactosidasea. What is the optimum pH of wild type ß-galactosidase?b. What is the optimum temperature of mutant ß-galactosidase?c. Which enzyme has the greater activity at pH 7.2?d. Which enzyme has the greater activity at a temperature of 42.5°C?e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4?f. Which enzyme has greater activity if temperature increases from 40°C to 41 °C?5055

Enzyme activity refers to the general catalytic activity of an enzyme. It can be affected by:…

Answered: a. What is the optimum pH of wild type…

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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2. A 500µl reaction containing 0.5 pmol of an enzyme following Michaelis -Menten kinetics with saturating substrate concentration is studied. For this enzyme kl = 1 x 10° M-1 s', k-1 = 2 x 10's', and k2 = 1 x 10° s'. a. What is the Vmax for the enzyme considering that it has only one substrate binding site? b. What are the values of Km and Ks? Is this a rapid equilibrium enzyme or does it follow steady state kinetics? Explain why. c. What is the substrate concentration needed to achieve half maximal velocity? Explain the basis for your answer. d. If the substrate concentration in part e is doubled, how many fold will the initial velocity increase? e. What is the Km is the concentration of the enzyme is doubled? f. What is the efficiency of this enzyme? g. Would this enzyme be considered a perfect enzyme? Explain. h. If 0.25 pmol of an irreversible or classic non-competitive inhibitor is added before starting the reaction. What is the resulting Km for the enzyme? i. A reversible…
The substrate has been represented bound to the enzyme pocket. 20 Zn Part A: Part B: Substrate Part C: lle Val A Increasing V Arg 1451 (1)=0 Carboxypeptidase A A. Competitive inhibitor B. Irreversible inhibitor C. Allosteric inhibition D. Uncompetitive inhibition E. Non-competitive inhibitor F. -1/KM Benzylsuccinic acid Propose the types of biochemical interactions by which benzylsuccinic acid interacts with the carboxypeptidase A active site. 1. Hydrogen bond II. Ionic bond III.Hydrophobic interactions (Choose from options G-L) Which of the shown Lineweaver-Burk plots would you expect observe when benzylsuccinic acid I used to inhibit Carboxypeptidase A enzymatic activity? (Choose from options N-R) Increasing [1] Benzylsuccinic acid (shown below) has been identified as an inhibitor of carboxypeptidase A. Based on your understanding of enzyme- inhibitor interactions, identify a likely mechanism of inhibition by benzylsuccinic acid. (Choose from options A-E) in-o CH3 1/S) O V.(min) 20…
A. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?
Various concentrations of recombinant human insulin were prepared for use standards for an HPLC method. To verify the prepared concentrations, the samples were analyzed by measuring the absorbance at 280 nm in a short path length (5 mm) cuvette. The molar absorption coefficient for human insulin is approximately 5.875 x 10³ M-¹cm-¹. a. Calculate the extinction coefficient in mL mg-¹cm-¹. b. Calculate the concentrations of the following human insulin standards if the measured absorbances and dilutions used are: Standard 1 Standard 2 Abs. (at 280 nm) of Diluted Sample 0.305 0.685 Dilution 145.0 µL sample, 25.0 μL buffer 130.0 µL sample, 40.0 μL buffer
Please dont provide handwrittin solution.../.
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
What is the optimal substrate concentration for the enzymatic reaction presented in the Lineweaver-Burk plot below? a. -0.3211 units/mL b. –3.114 units/mL c. None of these values represent the optimal substrate concentration shown in the Lineweaver-Burk plot d. 3.114 units/mL e. 0.3211 units/mL
In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor. In each batch, the inhibitor was of a different type: a.Batch 1: competitive inhibitor b.Batch 2:uncompetitive inhibitor c.Batch 3:non-competitive inhibitor Assuming that Vmax = 80 mM s', Km = 8 mM, and Kiof all three inhibitors was 10 mM, which of the inhibitors was the most efficient on Vo? Explain your answer.
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
Which of the following is true about a mixed type inhibition? a. None of these is true b. A Lineweaver-Burk plot will give parallel lines c. The lines of a Lineweaver-Burk graph will cross in the top left quadrant d. The KM will change but not the Vmax

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