Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km isknown to have a value of 1 mmol L-1.[S] (mmol L-1)Vo (umol L-1 min-1)0.5501.02.03.010.0

The Michaelis–Menten equation is used for characterizing the enzymatic rate at various substrate…

Answered: Use the Michaelis-Menten equation to…

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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At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate at one-tenth of its maximum rate? Assume the enzyme obeys Michaeli s-Menten kinetics.
please include all data in answer set
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?
Vo 60 50 40 30 20 mm/sec 0100 0 O 0 0 50 100 150 200 250 300 Substrate (mM) Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the enzyme catalyzed reaction (square data points)? (choose the one best answer) 10
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
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-
Sample pH vs Initial Velocity (AA450/60 seconds) a bo16 0.0014 0.0012 o.001 0.0008 0.0006 0.0004 0 0002 pH Sample what does it mean? Does it agree with what we know about enzyme kinetics and why or why nol? If there were anomalies, what were they and what are some possible reasons for this occurring? Was an optimal pH identifiable? Why or why not? Initial Velocity (AA450/60seconds)
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
If 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24
Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
How many net molecules of nucleoside triphosphate (ATP and equivalent molecules) are produced by complete aerobic catabolism of a glucose going through glycolysis, the pyruvate dehydrogenase complex and the citric acid cycle (TCA cycle)? Do not count the ATP eventually generated by re-oxidation of reduced coenzymes, just the number of NTPs produced in reactions of these pathways. Choose the one best answer. 02 03 04 05 06 8
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.

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Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol L-1. [S] (mmol L-1) Vo (umol L-1 min-1) 0.5 50 1.0 2.0 3.0 10.0