3. A biochemistry lab wants to developa method to measure a biochemical transformation in acell by energy consumption that is coupled to the system NAD*/NADH (see below). The HOMO-LUMO gaps (energy needed for the n>n* transition) for the two forms were calculated to be3.12eV and 4.14eV. Based on their structure assign the HOMO-LUMO gaps to either form andassign their UV bands.ADPRibADPRibReductionOxidation0.2NH2ннNH2NAD*NADH250300350400450a (nm)

Here in question, HOMO is Highest Occupied Molecular Orbital and LUMO is Lowest Unoccupied MO…

Answered: 3. A biochemistry lab wants to develop…

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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3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?
4
1. Start with the Michaelis-Menten equation and convert it to a double-reciprocal equation. Show how you would make a linear Lineweaver-Burk plot using this equation. 2. Based on th chart make a Lineweaver-Burk plot and later use the plot to complete the information in the table.
4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
3. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. -1 v, μmol s¹ mg-¹ 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00+ 0 100 → WT 200 300 [s], mM 400 500 → V105A (a) Estimate the Km and Vmax for the wild-type and mutant enzyme from the graph. (b) Calculate the Keat and Keat/Km for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd
7. An enzyme is discovered that catalyzes the chemical reaction : SAD + HAPPY A team of motivated researchers sets out to study the enzyme, which they call happyase. They find that the kcat for happyase is 600 s -1 and carry out several additional experiments. When [Et] = 20 nM and [SAD] = 40 µM, the reaction velocity is 9.6 µM s-1. Calculate KM for the substrate SAD. 8. In a separate enzyme happyase experiment using [Et] = 10 nM, the reaction velocity is measured at 3 µM s-l. What is the [S] used in this experiment?
7. A study of hypothetical reaction 2A + B -----> C + D gave these results: Experiment Initial Concentration (mol/L) Initial Rate (mol L-1 s-1) [A] [B] 1 0.10 0.050 6.0 × 10-3 2 0.20 0.050 1.2 × 10-2 3 0.30 0.050 1.8 × 10-2 4 0.20 0.150 1.1 × 10-1 a) What is the rate law for this reaction? b) Calculate the rate constant k and express it in appropriate units. 8. The reaction 2 NO(g) + 2 H2(g) -------> N2(g) + 2 H2O(g) is found to be first-order in H2(g). Which rate equation cannot be correct? a) Rate = k[NO]2[H2] b) Rate = k[H2] c) Rate = k[NO]2[H2]2 9. When phenacyl bromide and pyridine are both dissolved in methanol, they react to form phenacylpyridinium bromide. When equal concentrations of reactants were mixed with methanol at 35°C, these data where obtained: Time (min) [Reactant] (mol/L) Time (min) [Reactant] (mol/L) 0 0.0385 500 0.0208 100 0.0330 600 0.0191 200 0.0288 700 0.0176 300 0.0255 800 0.0163 400 0.0220 1000 0.0143 a) What is…
4.2
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
5.4. If 32P labeled (radioactive phosphate) inorganic phosphate were introduced to erythrocytes undergoing glycolysis which of the following molecules would you expect to detect 32P in Glycolytic intermediates? A. Fructose 1-6 bisphosphate B. 3-Phosphoglyceraldehyde C. Dihydroxyacetone phosphate D. 2-Phosphoglycerate E. 1-3 bisphosphoglycerate F. Phosphoenolpyruvate G. 3-Phosphoglycerate H. Pyruvate I. None of the above is it E?

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