Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 16, Problem 9P
Interpretation Introduction
Interpretation:
The advantage for the liver to have two enzymes, hexokinase, and glucokinase to phosphorylate glucose should be determined.
Concept introduction:
Glycolysis is the conversion of one molecule of glucose into two molecules of pyruvate. During this process, two molecules of ATP and two molecules of NADH are produced. Glycolysis is divided into two phases, the preparatory phase, and payoff phase. In the preparatory phase, ATP is consumed, while in the payoff phase ATP is produced.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Please ASA. Thanku.
In the reaction Na + Cl à Na+ + Cl-, which component is said to become ‘oxidized’ and which is considered reduced?
Na, Cl
Cl, Cl
Na, Na
Cl, Na
Fo-F1 ATPase. The energy for ATP synthesis from ADP and Pi is provided by the downhill transport of protons through the rotary FoF1 ATP synthase (lecture 22). The enzyme has 3 a-b and 12 ‘c’ subunits. The mitochondrion maintains Df=180 mV (negative inside), pHin = 8, pHout=7, [Pi] = 3 mM and ADP is present as well.
How much energy is available (from the proton electrochemical gradient) for ATP synthesis under these conditions (in kJ/mol)?
What [ATP]/[ADP] ratio will be established at steady-state under these conditions?
What would be the [ATP]/[ADP] ratio if the enzyme had only 9 ‘c’ subunits? Remember that full revolution of the crank (gamma subunit) produces 3 ATP.
Tracing glucose. Glucose labeled with 14 C at C-6 is added to a solution containing the enzymes and cofactors of the oxidative phase of the pentose phosphate pathway. What is the fate of the radioactive label?
Chapter 16 Solutions
Biochemistry
Ch. 16 - Prob. 1PCh. 16 - Prob. 2PCh. 16 - Prob. 3PCh. 16 - Prob. 4PCh. 16 - Prob. 5PCh. 16 - Prob. 6PCh. 16 - Prob. 7PCh. 16 - Prob. 8PCh. 16 - Prob. 9PCh. 16 - Prob. 10P
Ch. 16 - Prob. 11PCh. 16 - Prob. 12PCh. 16 - Prob. 13PCh. 16 - Prob. 14PCh. 16 - Prob. 15PCh. 16 - Prob. 16PCh. 16 - Prob. 17PCh. 16 - Prob. 18PCh. 16 - Prob. 19PCh. 16 - Prob. 20PCh. 16 - Prob. 21PCh. 16 - Prob. 22PCh. 16 - Prob. 23PCh. 16 - Prob. 24PCh. 16 - Prob. 25PCh. 16 - Prob. 26PCh. 16 - Prob. 27PCh. 16 - Prob. 28PCh. 16 - Prob. 29PCh. 16 - Prob. 30PCh. 16 - Prob. 31PCh. 16 - Prob. 32PCh. 16 - Prob. 33PCh. 16 - Prob. 34PCh. 16 - Prob. 35PCh. 16 - Prob. 36PCh. 16 - Prob. 37PCh. 16 - Prob. 38PCh. 16 - Prob. 39PCh. 16 - Prob. 40PCh. 16 - Prob. 41PCh. 16 - Prob. 42PCh. 16 - Prob. 43PCh. 16 - Prob. 44PCh. 16 - Prob. 45PCh. 16 - Prob. 46PCh. 16 - Prob. 47PCh. 16 - Prob. 48PCh. 16 - Prob. 49PCh. 16 - Prob. 50PCh. 16 - Prob. 51PCh. 16 - Prob. 52PCh. 16 - Prob. 53PCh. 16 - Prob. 54PCh. 16 - Prob. 55PCh. 16 - Prob. 56PCh. 16 - Prob. 57PCh. 16 - Prob. 58PCh. 16 - Prob. 59PCh. 16 - Prob. 60PCh. 16 - Prob. 61P
Knowledge Booster
Similar questions
- Fill in the blanks. Acetaminophen toxicity can occur at high doses in the liver. because ___________ (what type of molecules?) can become saturated and other routes of metabolism take over.Please explain to me what the correct molecule(?) is and why it is correct. I understand that the glucuronidation and sulfation conjugation pathways become saturated, but am not understanding what molecule(s) it is/are that is/are becoming saturated leading to the other routes of metabolism and acetaminophen toxicity.arrow_forwardDraw Gluconeogenesis. Please make sure to state all the enzymes and co-factors for each step of the pathway.arrow_forwardHow Is Metabolism Regulated? (Integrates with Chapter 15.) Metabolic regulation is achieved via regulating enzyme activity in three prominent ways: allosteric regulation, covalent modification, and enzyme synthesis and degradation. Which of the.se three modes of regulation is likely to be the quickest; which the .slowest? For each of these general enzyme regulatory mechanisms, cite conditions in which cells might employ that mode in preference to either of the other two.arrow_forward
- The Energetic Cost of Nitrogen Excretion via the Urea Cycle How many ATP equivalents are consumed in the production of 1 equivalent of urea by the urea cycle?arrow_forwardUse your knowledge of fat metabolism. glycolysis, the TCA cycle, and axidative phosphorylation to determine how many molecules of ATP eauvalents are produced when glycerol undergoes biochemical combustion. Assume that each molecule of NADH produces 2.5 ATP and that each molecule of FADH2 produces 1.5 molecules of ATP during oxidative phosphorylation. Note that GTP is an ATp "equivalent." OA 14.5 OB. 17 OC. 19.5 OD. 20.5arrow_forwardBIOCHEMISTRY. Could glycerol be used to regenerate the OAA for maintenance of TCA cycle activity? Yes or No? Explain.arrow_forward
- Fo-F1 ATPase. The energy for ATP synthesis from ADP and Pi is provided by the downhill transport of protons through the rotary FoF1 ATP synthase . The enzyme has 3 alpha-beta and 12 ‘c’ subunits. The mitochondrion maintains change in membrane potential=180 mV (negative inside), pHin = 8, pHout=7, [Pi] = 3 mM and ADP is present as well. . What [ATP]/[ADP] ratio will be established at steady-state under these conditions? What would be the [ATP]/[ADP] ratio if the enzyme had only 9 ‘c’ subunits? full revolution of the crank (gamma subunit) produces 3 ATP.arrow_forwardin human 2. Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout. several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 kJ.mol to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?arrow_forwardWhat is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1arrow_forward
- Metabolic regulation (Ch. 15) 1. The Vmax of the enzyme glycogen phosphorylase from skeletal muscle is much greater than the Vmax of the same enzyme from liver tissue. (a) What is the physiological function of glycogen phosphorylase in skeletal muscle? In liver tissue? (b) Why does the Vmax of the muscle enzyme need to be larger than that of the liver enzyme?arrow_forwardTrue/Flase? Substrate level phosphorylation is a process that produces ATP and other nucleoside triphosphates via direct transfer of a phosphate group from a donor molecule.arrow_forwardphosphorylation/dephosphorylation 5. Diagram the cascade that regulates glycogen metabolism. Please use key enzyme names and arrows to show how glycogen phosphorylase and glycogen synthase are inversely activated/deactivated.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning