19. The AG, the standard free-energy change, for the isomerization of dihydroxyacetone phosphate(DHAP) to glyceraldehyde 3-phosphate (GAP) is +7.55 kJ/mol. The reaction shown below iscatalyzed by an enzyme called Triose Phosphate Isomerase (TPI).OHOOHDHAPOHTPIOHM+OHGAPOHThis reaction takes place in glycolysis. At equilibrium, the ratio of GAP to DHAP is 0.0475 at 25°Cand pH 7.00. Equilibrium constant, Keq = 0.0475.A) Is the above reaction endergonic or exergonic (going from left to right) under the givenexperimental conditions? Why?B) Can the above reaction occur spontaneously under the given experimental conditions? Why orwhy not?

The rate of a chemical reaction refers to how quickly reactants are converted into products over…

Answered: 19. The AG, the standard free-energy…

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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Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
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)
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…
3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATP
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
None
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?

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