The following experimental data were obtained for the kinetics of the enzymereaction Glucose + ATP → Glucose 6-phosphate + ADP.Parameters1234[S], M1.72.33.24.38.116.7V0.210.240.270.330.410.45What is the Km and Vmax of the enzyme?

Enzyme kinetics are explained by Michaelis Menten equation shown below: V=VmaxSKm+S Here, V is…

Answered: The following experimental data were…

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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a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.
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Use the Michaelis-Menten equation to complete the enzyme kinetic data set, whenKm is known to have a value of 1 mmol L−1 [S] (mmol L−1) Vo (μmol L−1 min−1) 0.5 50 1.0 2.0 3.0 10.0
An enzyme catalyzes a reaction with a Km of 6.50 mM and a Vmax of 2.00 mM s¹. Calculate the reaction velocity, Vo, for each substrate concentration. Vo : Vo: Vo : [S] = 4.00 mM [S] = 6.50 mM [S] 14.0 mM = n. mm. s-1 mm. sl mm. s-1
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
The glucose oxidase used in this experiment has a concentration of 27 U/mg. Calculate the mass (in g) of solid glucose oxidase required to react with all the glucose in 4.00 µL of10.0- mM glucose sample assuming the reaction proceeds for 30 minutes.
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?
Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM

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The following experimental data were obtained for the kinetics of the enzyme reaction Glucose + ATP → Glucose 6-phosphate + ADP. Parameters 1 4 [S], M V 1.7 2.3 3.2 4.3 8.1 16.7 0.21 0.24 0.27 0.33 0.41 0.45 What is the Km and Vmax of the enzyme?