1. Determine the Michaelis-Menten parameters of Vmax and Kỵ for the reactionS+EE.SE.S+WP+EThe rate of reaction is given as a function of substrate:[S]0.20.020.01kmol/m³-I'Skmol/m³.sE.Sk₂E+S0.540.280.190.0050.10.0020.045

For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Answered: 1. Determine the Michaelis-Menten…

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

Perform the calculations to make a master mix for 20 1.0 mL reactions each composed of 165 uL of 6 mM NAD+ 165 uL of 0.15M Lactate and 630 uL of 0.15M CAPS pH 10.5 per reaction. Report your answers in units of milliliters.
The experiment is about testing the ideal gas law (magnesium ribbon experiment)
Your current Vmax (4x10-3 A/S) from the Michaelis-Menten plot has the units of A/s and was determined using 0.1 mg of ADH in a total volume of 1.25 mL. Use the Beer-Lambert equation followed by simple conversion to express your estimated Vmax in (mol )/s per 1 mg ADH. The molar absorptivity of NADH at 340 nm is 6220 L/(mol*cm).
A doctor wants to prescribe a 70 kg patient a drug to be taken PO. In order to achieve an average steady-state plasma concentration (Css) of this drug in its therapeutic range, the patient needs to have a of Css of 597 μg/L. The VD of this drug is 2.3 L/kg, the F of this drug is 0.70, and the half-life of this drug is 12.9 hours. What is the necessary dosing regimen needed to achieve the desired Css? (units: mg/day, i.e., mg/24 h))
24. Determine equilibrium constants for the hydrolysis of phosphoenolpyruvate (AG" is 61.9 kJ/mol) at pH 7 and 25°C: nariw (d)
Calculate for rate constant(k)
12. Find the ΔH for the reaction below, given the following reactions and subsequent ΔH values: b. FeO(s) + CO(g) ⟶⟶ Fe(s) + CO2(g) ΔH = __________ 3Fe2O3(s) +CO(g) ⟶⟶ 2Fe3O4 +CO2 (g) ΔH = -68.26 kJ Eq 1 Fe2O3(s) + 3CO(g) ⟶⟶ 2Fe(s) + 3 CO2(g) ΔH = -23.44 kJ Eq 2 Fe3O4(s) + CO(g) ⟶⟶ 3FeO(s) + CO2(g) ΔH = +21.79 kJ Eq 3
How is this equation derived? from pre-existing michaelis menten kinetics assumptions?
3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?
Complete the following reaction by filling in the necessary reagents. NH₂ S. 1) Br 2) Draw the product for the following reaction. Η N|H CH 3 1. CH3I (excess) 2. Ag₂O 3. A F Br
3. Show the calculation of (1) the expected grams of alum (KAI(SO4)2 12 H2O) formed from the reaction of 1.4 grams of aluminum metal and then show the calculation of (2) the % yield if the actual yield of alum is 21.31 grams. Overall reaction is shown below: 2 Al + 2 KOH + 10 H2O + 4 H2SO4 →2 KAI(SO4)2 12 H2O + 3 H2(g)T
22. For the process, A B, Keq is 0.02 at 37°C. For the process, BC, Keq 1000 at 37°C. A. Determine Keq (AC), the equilibrium constant for the overall process A C, from Keq (AB) and Keq (BC). B. Determine standard-state free energy changes for all three processes and use AG'(AC) to determine Keq (AC). Make sure that this value agrees with that determined in part A of this problem.

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

1. Determine the Michaelis-Menten parameters of Vmax and K for the reaction S+E E.S₂E+S E.S E.S+W P+E The rate of reaction is given as a function of substrate: [S] 0.2 0.02 0.01 kmol/m³ -I'S kmol/m³.s 0.54 0.28 0.19 0.005 0.1 0.002 0.045