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
Concept explainers
Question
Chapter 16, Problem 47P
Interpretation Introduction
Interpretation:
If lactate along with CO2 labeled with 14C is allowed to form glucose, then the carbon that would be labeled in the glucose should be determined.
Concept introduction:
Glycolysis is the process that occurs in the cytoplasm of the cell. It is the breakdown of one molecule of glucose into two molecules of pyruvic acid. During this process, energy is released in the form of two moles of ATP. The purpose of glycolysis is to maintain the blood glucose level.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Tracing carbon atoms 2. If cells synthesizing glucose from lactate are
exposed to CO2CO2 labeled with 14C,“C, what will be the
distribution of label in the newly synthesized glucose?
1. pH Effects
a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52
and Glu35, are critical for catalytic activity. If we assume normal side chain pKa
values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of
enzyme molecules will have both Asp52 and Glu35 in the correct ionization
state at pH 5.0 (the pH optimum for lysozyme)?
b. Are the traditional pKa values likely to be correct within the protein? What pKa
changes might be present within lysozyme?
The allosteric site
1). Draw a representation of an allosteric binding site of an enzyme.
must bind an allosteric modifier that maintains three hydrophobic regions, a polar
charged region and two regions of hydrogen bonding. You choose the order or
organization of the characteristics in the allosteric site - label all regions.
Details
the allosteric site is composed of faces of two separate beta sheets and two
separate alpha helices. You might decide that each beta sheet or each alpha helix
contributes one amino acid R group to the allosteric site or you may decide that one of
the beta sheets or one of the alpha helixes contributes two or more amino acid R groups
to the allosteric organization. Your choice but please show R group structure in the
allosteric site!
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
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- NH2 Part A N- N. Which of the following is found in the coenzyme FAD? 'N Check all that apply. V two heterocyclic rings O ADP OH HO OH O a substituted benzene ring O a phosphate anhydride bond Submit Previous Answers Request Answer X Incorrect; Try Again; 6 attempts remaining NH Provide Feedbackarrow_forwardEnergetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?arrow_forward16-24 diastereomers? Explain your answer. Both? when the motecue hasonly che stereocenter then the epiners are encintomers. When the molecule hastwo umor ster Draw Haworth projection formulas for dimers of glucose having the a B1-4 linkage (both molecules of glucose in the B form) a) b) c) an a,a (1-1) linkage a B1-6 linkage between 2 ß-glucose units epime are dia sterarrow_forward
- in 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_forwardHis388 Glu357 His388 Glu357 Ring opening Proton HO HO abstraction HO но- G6P He NH- NH His388 His388 His388 Glu357 Glu357 Glu357 HO но HO но- но OH cis-enediol F6P Ring closure intermediate OH Describe the mechanism shown above for phosphoglucose isomerase. Describe the chemistry of each step • How the enzyme appears or might facilitate the chemistry How the enzyme increases the reaction rate.arrow_forwardI lea the - Oligopeptide 2 a. Give the three-letter and one-letter names of the amino acids in each oligopeptide starting from the amino terminal to the carboxyl terminal. Make sure that the amino acid names are arranged in CORRECT order for both oligopeptides. I b. After complete hydrolysis, which oligopeptide will yield more ATP molecules? How many NADH and FADH2 molecules will be theoretically produced? Show all relevant computations for each oligopeptide. Tabulate your answers to keep your answers organized. ( Oligopeptide Net ATP molecules Net NADH produced Net FADH2 produced produced Oligopeptide 1 Oligopeptide 2arrow_forward
- Glycerophospholipids Phosphatidylethanolamine 3. In case the cell is in a state requiring large amount of ATP to support energy-requiring reactions/pathways, assuming that you have 1 mole of each of the said lipids are catabolized and complete oxidized, will the total net ATP yield from these two lipids be higher or lower than the sum of the net ATPs generated from each fatty acid components? Justify your answer in biochemical terms and using 5 sentences or less.arrow_forwardSome terms will not be used. The prosthetic group of hemoglobin and myoglobin is The organic ring component of heme is Under normal conditions, the central atom of heme is In the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring system. The central atom has bonds: to nitrogen atoms in the porphyrin, one to a residue, and one to oxygen. Answer Bank Fe3+ three heme serine deoxyhemoglobin four Fe2+ oxyhemoglobin рoгphyrin histidine six cysteinearrow_forward1 of 1 3. A sample of glucose reacts in anaerobic respiration. The right- hand box below shows a particle diagram of the moles of substances present after the reaction is complete. fe On a piece of paper draw the "Before" box as shown and draw a particle diagram of the reactant molecules that produced the mixture shown on the right. Key = C2H5OH = CO2 = CgH1206 Sub Before After You will need to draw a diagram to answer this question. On a piece of paper, draw the "Before" box as shown, and then draw a particle diagram of the reactant molecules that produced the mixture shown on the right. Upload an image of your drawing by clicking "Upload files" or by dragging and dropping your file into the box. Or, use your device's camera to take a photo of your work by clicking the camera icon.arrow_forward
- . Explain what is meant by the term, “high energy compound”. Name a thioester molecule that is commonly found in biochemical reactions. Explain why thioesters are “high energy” compounds. Describe the molecular structure of cellulose. How does this structure explain why cellulose forms strong fibers? Explain why digestion of cellulose takes a long time even when catalyzed by an enzyme. The enzyme phosphofructokinase transfers a phosphate from ATP to the hydroxyl group a C1 of fructose. Similar to fructose, water also has a hydroxyl group and the concentration of water is much higher than that of fructose. Explain why the phosphate is transferred to fructose and not to water.arrow_forwardcan be 9. Compartmentation in ß Oxidation Free palmitate is activated to its coenzyme A derivative (palmitoyl-CoA) in the cytosol before oxidized in the mitochondrion. If palmitate and [ ¹4C]coenzyme A are added to a liver homogenate, palmitoyl-CoA isolated from the cytosolic fraction is radioactive, but that isolated from the mitochondrial fraction is not. Explain.arrow_forwardHi need help on this one. I need a solution for each ! Thank you ----------------------------------------------------- (e.g 200 glucose x 36 ATP =7200 ATP) 1. If there is 1944 ATP produced, how many glucose molecules were broken down? 2. 20 glucose molecules were processed, how many net ATP molecules can be produced? • A. In Glycolysis • B. In Krebs Cycle: • C. In Oxidative Phosphorylation: • D. Total net ATP yield: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
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY