24. Researcher X did a series of experiments and determined the following about Enzyme Aand its substrate (S).KM - 4 mMVmax 100 mM/saxis. (.a) Draw the Michealis-Menton plot with all the above information shown. Be sure to labelVmaxRate of neation (mm)rate of reactin mm.supstratiate concentration MM/Sb) Convert the Michealis-Menton plot into a Lineweaver-Burk plot below, Label the axis.VmaxRate of reaction(MM)810090Go10080 - tmax30201c) Using a dotted line, add in how á uncompetitive inhibitor how the rate would look with(S) (MM/S) x 1|San uncompetitive inhibitor added.100KOMIKeVmaxVmarSun competiti6• substante (MMIS)

Enzyme kinetics is the study of how enzymes catalyze chemical reactions. Enzymes are biological…

Answered: 24. Researcher X did a series of…

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

See similar textbooks

Similar questions

1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
The enzyme triosephosphate isomerase (TIM) catalyzes the following reaction in glycolysis, where it converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (GAP). CH₂OH C=O CH₂OPO²- DHAP triose phosphate isomerase [DHAP] (MM 1.00 2.00 3.00 6.00 O V. (mM/s) 3.700 6.727 9.250 14.800 = H HCOH CH₂OPO²- Kinetics experiments were performed on TIM. Enzyme activity (initial velocity, V.) was measured at varying concentrations of DHAP. The enzyme kinetics were also measured in the presence of two inhibitors, A and B. The enzyme concentration used in all experiments was 25.00 μM. The data are shown below. GAP V. (mM/s) + A 1.452 2.794 4.038 7.281 V₁ (mM/s) + B 0.755 1.379 1.905 3.077
I need help with parts d-g a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1 For ATP: catalytic efficiency = 12.1 x 107 M-1s-1 b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion c.) Line weaver Burk equation for AdoK enzyme with Ado substrate: y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
8 7- 6 2- 180 225 270 315 [Substrate] (nM) 45 90 135 360 405 450 495 540 58! What is the KM of the enzyme data shown above? rate (nM/sec) 3.
For an enzyme-catalyzed reaction, the velocity was determined at two different concentrations of the substrate. Estimate the value of Vmax. [S] (MM) 10 20 88 nmol/min 79 nmol/min 67 nmol/min V(nmol/min) 51 nmol/min 27 Not enough information is given to form a reasonable estimation. 48
Two enzyme catalyzed reactions, RA (red) and Rp (blue), have kinetic profiles shown below. Report which reaction has the higher maximal rate and which reaction has the smaller Km. в A 1/ [S] Higher Vm [ Select ] Lower Km [ Select ] A/T
For an enzyme following Michaelis-Menten kinetics, the following Vo vs. S data were obtained in steady state experiments using 2 micromolar enzyme for all measurements: [S] Vo 1 mM 4.0 mM/min 2 mM 4.8 mM/min 4 mM 4.9 mm/min 8 mM 4.95 mM/min Estimate the value of kcat for the reaction. Be sure to include the appropriate units.
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
1. Enzyme X has a molecular weight of 35,000 Da. When this enzyme is assayed for enzyme activity, the corresponding line of the double reciprocal plot has the equation y = 75,253X + 102,392. The substrate concentration was in mM and the velocity was measured in mM min". From these data calculate the following: a. KM and Vmax b. kcat if the enzyme concentration was 2 mg/mL. 2. When you run enzyme X from question one on an SDS-PAGE you find that, after Coomassie staining, there is only one band on the gel that runs just below the 20,000 Dalton molecular weight marker. What does this result tell you about the nature of the quaternary structure of your enzyme?
For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS