![Bundle: General, Organic, and Biological Chemistry, 7th + OWLv2 Quick Prep for General Chemistry, 4 terms (24 months) Printed Access Card](https://www.bartleby.com/isbn_cover_images/9781305717534/9781305717534_largeCoverImage.gif)
Concept explainers
(a)
Interpretation: To draw the three-subunit block diagram for
Concept introduction: Coenzymes are non-protein organic compounds that are used along with the enzymes and help to carry forward the reaction. Coenzymes cannot perform on their own alone. Nicotinamide adenine dinucleotide
Nicotinamide adenine dinucleotide
Here,
(b)
Interpretation: To draw the six-subunit block diagram for
Concept introduction: Coenzymes are non-protein organic compounds that are used along with the enzymes and help to carry forward the reaction. Coenzymes cannot perform on their own alone. Nicotinamide adenine dinucleotide
Nicotinamide adenine dinucleotide
Here,
![Check Mark](/static/check-mark.png)
Want to see the full answer?
Check out a sample textbook solution![Blurred answer](/static/blurred-answer.jpg)
Chapter 23 Solutions
Bundle: General, Organic, and Biological Chemistry, 7th + OWLv2 Quick Prep for General Chemistry, 4 terms (24 months) Printed Access Card
- The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…arrow_forwardThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.arrow_forwardWrite the coupled reaction that would occur spontaneously for the following pairs of molecules under standard condition: Oxaloaxcetate and NAD+arrow_forward
- Indicate whether each of the following changes represents oxidation or reduction. Write: O = for oxidation ; R= for reduction Example: cyt ci (Fet) → cyt c1 (Fe2+) Answer: R Blank #1: COQH2 → CoQ Blank #2: NAD+ - NADH Blank #3: FMN → FMNH2 Blank # 4: FADH2 FAD Blank #5: Fe(III) SP → Fe(II) SP Blank # 1 Blank # 2arrow_forwardCalculate and compare the AGº' values for the oxidation of succinate by NAD and FAD. Use the data given in the table to find the E' of the NAD: NADH and fumarate:succinate couples, and assume that E' for the enzyme-bound FAD : FADH₂ redox + couple is nearly +0.05 V. Oxidant NAD + Fumarate Reductant NADH + H Succinate + AGO for the oxidation of succinate by NAD AGO for the oxidation of succinate by FAD: n 2 E'o (V) -0.32 T -0.03 + FAD is an oxidant, whereas NAD is a reductant. + Why is FAD rather than NAD the electron acceptor in the reaction catalyzed by succinate dehydrogenase? + The oxidation of succinate by NAD is not thermodynamically feasible. + The oxidation of succinate requires two NAD molecules but only one FAD molecule. + The electron-transport chain can regenerate FAD, but not NAD˚. kJ mol-¹ -1 kJ mol-¹arrow_forwardThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. Morphine is a non-competitive inhibitor of carbonic anhydrase. Draw on the same Lineweaver-Burke plot as above a graph showing the effect of a concentration of morphine that inhibits the first enzyme such that it reduces the Vmax to ½ its maximal value. Make sure to put in sample data points. Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.arrow_forward
- Decylic acid is a saturated fatty acid that occurs naturally in coconut oil and palm kernel oil. Calculate the net ATP yield when decylic acid undergoes complete B oxidation. The formula of decylic acid is shown below: (Given: The oxidation of one NADH yields 2.5 ATP; the oxidation of one FADH2 yields 1.5 ATP; and the oxidation of one acetyl CoA yields 10 ATP.) O 50 ATP O 52 ATP 66 ATP OH O 64 ATParrow_forwardGiven: Factor VIIa is a man-made protein analog to Factor VII, which is involved in coagulation. (Answer a, b, and c)a. Identify both a competitive and non-competitive inhibitor for Factor VIIa b. Draw a graph showing how both of these molecules will change the Velocity/[S] graph, and explain why this is the case. c. What would a graph look like if both inhibitors were added?arrow_forwardThe glutamate dehydrogenase (GDH) catalyses the following reaction: H +H₂N- -C -COO CH₂ CH₂ COO™ acide glutamique + NAD + H₂O GDH Time (min) A340 COO™ c=o CH₂ 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ COO + NH4+ NADH + H+ acide a-cétoglutarique The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M¹.cm7 6 7 8 9 10 1.550 1.510 1.489 1.476 1.451 Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. proteins - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. -…arrow_forward
- The following Michaelis-Menten plot shows the response of phosphofructokinase-1 (PFK-1), an enzyme in the glycolytic pathway, to the presence of ATP and AMP. Based on the data below, which of the following statements apply? Select all that apply. No inhibitors (low (ATP)) 1 mM ATP + 0.1 mM AMP 1 mM ATP 1.0 2.0 (Fructose-6-phosphate) mM Fig. : Regulation of PFK activity AMP is an allosteric modifier that enhances the binding of the substrate fructose 6-phosphate а. O b. AMP is an allosteric modifier that reduces the binding of the substrate fructose 6-phosphate ATP is an allosteric modifier that reduces the binding of the substrate fructose 6-phosphate O c. O d. ATP is an allosteric modifier that enhances the binding of the substrate fructose 6-phosphate Phosphofructokinase activityarrow_forward(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90arrow_forwarda) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) abovearrow_forward
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
![Text book image](https://www.bartleby.com/isbn_cover_images/9780134580999/9780134580999_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781947172517/9781947172517_coverImage_Textbooks.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781259398629/9781259398629_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9780815344322/9780815344322_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781260159363/9781260159363_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781260231700/9781260231700_smallCoverImage.gif)