Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Question
Chapter 8, Problem 20P
Interpretation Introduction
Interpretation:
The values of
Concept introduction:
When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Enzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that:
a Glu residue on the enzyme is involved in the reaction.
a Tyr residue on the enzyme is involved in the reaction.
a His residue on the enzyme is involved in the reaction
the enzyme uses NADH has a cofactor.
the enzyme uses coenzyme A has a cofactor.
Consider a general reaction
enzyme
A(aq)
B(aq)
The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C.
Keg =
What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is
0.50 M?
9:26 PM
35%
77°F
6/14/2021
G6P(ag)
F6P(aq)
AG°=+1.7kJ/mol at 25 °C
Consider the reaction:
Estimate the fraction of F6P (Fructose 6 Phosphate) in equilibrium with G6P
(Glucose 6 Phosphate) at 25 °C, where the fraction is defined as
[F6P]/([F6P]+[G6P]). Show ALL your work.
Chapter 8 Solutions
Biochemistry (Looseleaf)
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
Knowledge Booster
Similar questions
- fructose-6-phosphate + ATP fructose-1,6- biphosphate + ADP AG° = 30.5 and 16.3 respectively Standard Free Energy change: -14.2 kj/mol ATP: 3mM, ADP: 0.4mM, fructose-1,6-biphosphate: 7mM %3D At what concentration of fructose-1,6-biphosphate would the reaction proceed backwards at 35°C?arrow_forwardplease help me identify these huhu thank youarrow_forward- The phosphate transfer potentials for glucose-1-phosphate and glucose- 6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? CH,OH CH,OPO,2- H H H H OH H ОН Н 6-PO,2- HO OH н он Glucose-6-phosphate H OH Glucose-1-phosphate (b) If a mixture was prepared containing 1 M glucose-6-phosphate and 1 x 10M glucose-1-phosphate, what would be the thermodynami- cally favored direction for the reaction? 1arrow_forward
- 13. Calculate the equilibrium constant K'eg, for each of the following reactions at pH 7.0 and 25°C. glucose + Pi a. Glucose 6-phosphate + H20 enz. Glucose 6-phosphatase; AG'O=-13.8kJ/molarrow_forward8arrow_forwardConsider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·molarrow_forward
- The teal line of the following reaction is representing, PNPP -----> PNP +P (in the presence of alkaline phosphatase.) Choose the correct answer - Average rate of the reaction - The reaction rate at equilibrium - Instantaneous rate of the reaction at time zero - Vmaxarrow_forwardFind the net ΔG° of the reaction.arrow_forwardSelect the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the abovearrow_forward
- Calculate the equilibrium concentration of H2O for the following esterification reaction performed in ethanol(C2H5OH) C2H5OH + CH3CO2H ⇌CH3CO2C2H5 + H2O KC= 4.0 At equilibrium: [CH3CO2H] = 0.75 M; [CH3CO2C2H5 ]= 2.2 Marrow_forwardConsider the following reaction: Glucose 6-phosphate + Glucose 1-phosphate After reactant and product were mixed and allowed to reach equilibrium at 25C, the concentration of each compound was measured: (Glucose 1-phosphate] - 0.002 M [Glucose 6-phosphate 0.05 mM Calculate the Keg and the AG knot prime (e.g. standard free energy change). O Keg- 40: AG knot prime 9.14 kJ/mol O Ken- 19: AG knot prime -7.3 kJ/mol O Keg" 0.04: AG knot prime-7.98 kJ/mol Kea 4: AG knot prime -914 kJ/mol O Keg 40: AG knot prime - 9.14 k/molarrow_forwardCarbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON