1. Hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase is 99% complete atequilibrium (i.e., 1% of the substrate remains). Which of the following statements is most nearlycorrect? (R= 8.315 J/mol-K; T = 298 K)A AG" is-11 kl/mol.B) AG" is +5 kJ/mol.C) AG" is 0 kJ/mol.DAG" is +11 kJ/mol.E) AG" cannot be determined from the information given.Explain your choice in one line:-2.16x298 (2)- 11386.15-> 11.4 КТ5The high state conculto alle My negative and st" positive (either for D) thenonditions, one

Standards free energy change calculated at biochemical standards is called biochemical standard free…

Answered: 1. Hydrolysis of 1 M glucose…

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.
In glycolysis, fructose 1,6-bisphosphate is converted to two products with a standard free- energy change (AG) of 23.8 kJ/mol. Under what cellular conditions will the free-energy change be negative, enabling the reaction to proceed spontaneously to form products? O In a cell where the concentrations of products and reactants yield a low value of the mass-action ratio Q ○ The reaction will not go to the right spontaneously under any conditions because the AG is positive ○ The reaction will proceed spontaneously to the right if there is a high concentration of products relative to the concentration of fructose 1,6-bisphosphate ○ The reaction will proceed spontaneously to the right if there is a high concentration of enzyme to catalyze the reaction O None of these conditions is sufficient
Consider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 23.7, and the temperature is 37.0 °C? AG" for the reaction is -16.7 kJ/mol. The constant R = 8.3145 J/(mol-K) AG= Number kJ/mol
24. Hexokinase catalyzes the phosphorylation of glucose from ATP, yielding glucose-6-P and ADP. The standard-state free energy change for hydrolysis of glucose-6-P is -13.9 kJ/mol. Calculate the standard-state free energy change and equilibrium constant for the hexokinase reaction. AG" for ATP hydrolysis -31.5 kJ/mol
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
The standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alanine
By what factor is sample A2 more concentrated than sample A1?
Explain how running a reaction with the enzyme aldolase at a pH of 14 affects its activity Enzyme Activity e Activity 765432TO Factors Affecting Enzyme Activity 0 6543 2 6 Solution pH 8 a) It significantly diminishes activity because enzyme is denatured b) It significantly diminishes activity because the enzyme becomes too reactive Oc) It will quadruple its activity because enzyme is denatured and free Question 9 (5 points) Estimate the optimum pH required for maximum enzyme activity 10 d) It will double its activity because enzyme now has more active sites 12 Factors Affecting Enzyme Activity

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