ArachidonicRate of formationRate of formation of PGG2 with 10 mg/mlacid (mM)of PGG2 (mM/min)ibuprofen (mM/min)0.31012.77.920.37214.39.120.55818.012.20.9302.1722.829.616.824.6The kinetic data given in the table are for the reaction catalyzed by a mutant of prostaglandin endoperoxide synthase. Focusinghere on the first two columns, determine the Vmax and Km of the enzyme.Vmax=TOOLSKm =x10xmM/minmMPublisher: WH Fre

Vmax and Km are the two important parameters in enzyme kinetics.Vmax is the maximum rate of an…

Answered: Vmax Km x10 TOOLS

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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For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142
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?
The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)
Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/mol
explain in quantitative terms the circumstances under which the following reaction can porceed; L-malate + NAD+ (forward arrow) oxaloacetate + NADH + H+ delta G' standard = +29.7 KJ/mol
You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).
The redox half reaction Oxaloacetate + 2H+ + 2e− → Malate has a standard reduction potential value of 0.166 V. Calculate the free energy (ΔG°′) for the following reaction: Malate + NAD+ → Oxaloacetate + NADH + H+
Suppose that the data shown in the margin are obtained for an enzyme -catalyzed reaction. [S] (mM) V (mmol/ml min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.00 1.0 8.33 2.0 9.09 a.) Determine the Km and Vmaxb.) Assuming htat the enzyme present in the system had a concentration of 10-6M, calculate the turn -over number
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
The following data were obtained for a reaction that catalyzed by an enzyme: Initial concentration of 0.141 0.109 0.077 0.040 0.028 0.020 0.016 the enzyme [S], mol L- Relative velocity, V 22.0 20.5 19.0 12.5 9.0 7.0 6.0 For this reaction, the rate is found experimentally to follow the Michaelis-Menten equation: Vmax[S] Vo = Км+[S] (1) Transform the above equation into a straight-line equation. By plotting a suitable graph, determine the Michaelis constant (KM) and the maximal velocity (Vmax) for the above reaction. Determine the Vmax value when [S] = KM.
What is the actual change in free energy at 37°C for the phosphoglycerate mutase reaction converting 3-PGA to 2-PGA in erythrocytes if after drinking a glass of orange juice the [3-PGA] = 8 mM and the [2-PGA] = 0.08 mM? The standard change in free energy for the reaction is +4.5 kJ/mol. +16.3 kJ/mol O-6.5 kJ/mol O-7.3 kJ/mol -16.3 kJ/mol +7.3 kJ/mol
Calculate the standard free energy change (AG) for the transfer of electrons from succinate to ubiquinone: Succinate + ubiquinone O-2.7 kJ/mol O2.7 kJ/mol O-8.7 kJ/mol O 14.7 kJ/mol succinate dehydrogenase relevant half-reactions and standard reduction potentials: fumarate + 2 H* + 2 e succinate ubiquinone + 2H + 2 e -6.0 kJ/mol 11 Fumarate + ubiquinol ubiquinol E = 0.031 V E = 0.045 V

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