Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 18, Problem 16P
Energetics of the Hexokinase Reaction The standard-state free energy change.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Do not give handwriting solution
PRESSURE
OF A
WHAT IS THE asmoTIC
SOLUTION
OF BOVINE insuLIN (MOLAR MASS,
5700g mol - 1 ) aT
18 °C
IF 100.0 ML
OF
THE SOLUTION
conTains
0.103 a OF
THE INSULIN?
Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate
+ NADH Lactate + NADH+H+.
Note the temperature of this reaction will not affect the standard reducton potential delta E° in the table 13-7b.
Chapter 18 Solutions
Biochemistry
Ch. 18 - Characterizing Glycolysis List the reactions of...Ch. 18 - Radiotracer Labeling of Pyruvate from Glucose...Ch. 18 - Effects of Changing Metabolite Concentrations on...Ch. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - The Reactions and Meehanisms of the Leloir Pathway...Ch. 18 - The Effect of lodoacetic Acid on the...Ch. 18 - Prob. 8PCh. 18 - Comparing Glycolysis Entry Points for Sucrose...Ch. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Energetic of Fructose-1 ,6-bis P Hydrolysis...Ch. 18 - Prob. 15PCh. 18 - Energetics of the Hexokinase Reaction The...Ch. 18 - Prob. 17PCh. 18 - Distinguishing the Mechanisms of Class I and Class...Ch. 18 - Prob. 19PCh. 18 - Understanding the Mechanism of Hemolytic Anemia...Ch. 18 - Prob. 21PCh. 18 - Based on your residing of this chapter, what would...Ch. 18 - Examine the ActiveModel for alcohol dehydrogenase...Ch. 18 - Based on your knowledge of the structure of NAD+...Ch. 18 - Using the ActiveModel for phosphofructokinase...
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
- Having trouble with thisarrow_forwardInitial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.arrow_forwardTABLE 3-LACTATE PRODUCTION IN FORTIFIED HEMOLYSATES OF HUMAN ERYTHROCYTES* Substrate Glucose Glucose Lactate production† No. of experiments pH 6 7.1 2.03 ± 0.91 6 7.8 4.76 ± 1.09 7-1 10-73 +1-88 5 7.8 12.34 ±2.92 5 7.0 7-15±0.73 5 7-7 (b)( ) In mature erythrocytes (red blood cells) the end product of glycolysis is lactate because of the absence of mitochondria. On the right is a table comparing the rate of lac- tate production in hemolysates (lysed cells) of human RBCs as a function of pH with dif- ferent substrates introduced into the glyco- lytic pathway. The hemolysate was fortified with 30 μmoles substrate, 7.5 μmoles MgCl2, 10 μmoles disodium phosphate, 1.5 μmoles NAD and 5 μmoles ATP in a volume of 5 mL. The rate of lactate production is given as μmoles of lactate/g Hb/hr at 37° C, buffered to either pH 7.1 or 7.8, as indicated. According to the results in the table which glycolytic enzyme is rate-limiting? Explain. Glucose-6-phosphate Glucose-6-phosphate Fructose-1,6-diphosphate…arrow_forward
- 6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?arrow_forwardCalculation about delta standard G, delta H, detla S. Question attached as photo below. And my answer attempted. Need my answer verified and corrected if neccesary. Please let me know where I got wrong and what key ideas I had miss. Thanks.arrow_forwardWhat is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?arrow_forward
- The molar absorption coefficient of cytochrome P450. an enzyme involved in the breakdown of harmful substances in the liver and small intestine. at 522 nm is 291 dm3 mol-1 cm-1. When light of that wavelength passes through a cell of length 6.5 mm containing a solution of the solute. 39.8 percent of the light was absorbed. What is the molar concentrat ion of the solute?arrow_forwardKINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?arrow_forwardEffects of Changing Metabolite Concentrations on Glycolysis In an erythrocyte undergoing glycolysis what would be the effect of a sudden increase in the concentration of a. AΤP? b. AMP? c. fructose-1.6-bisphosphate? d. fructose-2, 6-bisphosphate? e. citrate? f. glucose-6-phospthate?arrow_forward
- Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.arrow_forwardCharacterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under standard-stale conditions), b. are energy yielding (under standard-state conditions), c. consume ATP. d. yield ATP e. are strongly influenced by changes in concentration of substrate and product because of their molecularity. f. are at or near equilibrium in the erythrocyte (see Table 18.2).arrow_forwardcalculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00775 mM ATP, 0.00027 mM ADP and 0.00418 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 43.0oC. Calculate your answer as kJ/mol to two decimal places.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