Need help, please. For the reactionglutamate¯ (aq) + oxaloacetate²- (aq)a-ketoglutarate²- (aq) + aspartate¯ (aq)the equilibrium constant at standard temperature is Kea = 2.82. Suppose theconcentrations of glutamate and oxaloacetate are 10 mM and the concentration of a-ketoglutarate is 25 mM at equilibrium. What is the value of AG' (in units of kJ/mol)under these conditions?Answer:✓ Choose...kJ/mol

When temperature and pressure are held constant, the amount of work that can be done in a…

Answered: For the reaction glutamate (aq) +…

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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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 effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
Determine the values of Km and Vmax for the decarboxylation of β-keto acid given the following data. Please show and label your plot. Show your calculations and box your final [S] in mol/l V in mM/ min 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256
Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. You have to plot the graph by using excel. Please include slope Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)
The reactionPyruvate-(aq) + NADH(aq) + H+(aq) → lactate-(aq) + NAD+(aq)where NAD+ is the oxidized form of nicotinamide adenine dinucleotide, occurs in muscle cells deprived of oxygen during strenuous exercise and can lead to cramp. Calculate the biological standard Gibbs energy, ΔrG⊕, for the reaction at 310 K given that the thermodynamic standard reaction Gibbsenergy ΔrGΘ = -66.6 kJ mol-1.
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). [S], M V w/o inhibitor, M/s V w/ inhibitor, M/s 1x10-4 0.0259 0.0098 5x10-4 0.0917 0.040 1.5x10-3 0.136 0.086 2.5x10-3 0.150 0.120 5x10-3 0.165 0.142 In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.
The equilibrium constant Kc for the reaction fructose-1,6-diphosphate ⇋ glyceraldehyde-3-phosphate + dihydroxyacetone phosphate is 8.9 x 10-5 M at 250C and the behavior is assumed to be ideal. Calculate .for the process (standard state: 1M) Suppose that we have a mixture that is initially 0.010 M in fructose-1,6-diphosphate and 1.0 x 10-5 M in both glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. What is ?
Determine the values of KM and Vmax for the decarboxylation of a β-keto acid given the following data.
The absorption of ketoconazole has been shown to be impaired in patients with drug-induced achlorhydria. The drug absorption was increased significantly to approximately 65% when the drug was taken with an acidic beverage such as Coca-Cola (pH 2.5). Ketoconazole is a synthetic azole antifungal agent and a weakly dibasic compound with pKa of 2.9 and 6.5. Using the information provided and the pH partition hypothesis, justify the use of Coca-Cola to improve the absorption of this antifungal agent.
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

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