Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
Question
Book Icon
Chapter 18, Problem 15P
Interpretation Introduction

(a)

Interpretation:

The standard energy change for the phosphoglycerate reaction should be calculated

Concept Introduction:

The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K.

Expert Solution
Check Mark

Answer to Problem 15P

  19.1kJmol

Explanation of Solution

In phosphoglycerate reaction ATP combine with hydrolysis to obtain following equation.

  ATP+H2OADP+Pi

  ATP+H2OADP+Pi

In the first reaction hydrolysis of 1,3-BPG mixes to give

  1,3BPG+H2OPyruvate+Pi;G=49.6 kJ/mol

In the second reaction, it is reverse process of hydrolysis of ATP. In this reaction we use opposite value of free energy.

  ADP+PiATP+H2OG=30.5 kJ/mol

In the coupled reaction free energy stated as

  G0'total=Go'1+G0'2

  G0'total=Go'1+G0'2G0'total=49.6kJmol+30.5kJmolG0'total=19.1kJmolKeqGo'=RT×lnK1eqK1eq=e G 0'RTK1eq=e19.18.314× 10 3×298

In phosphoglycereate kinase reaction the standard free energy obtained is 19.1kJmol .

Interpretation Introduction

(b)

Interpretation:

The equilibrium constant of the reaction should be calculated.

Concept Introduction:

The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K

Expert Solution
Check Mark

Answer to Problem 15P

  K1eq=1647.74

Explanation of Solution

  Keq is the equilibrium constant for the reaction

  Go'=RT×lnK1eq

Hence K1eq=eG0'RT

The temperature of the body is 37 C

Convert Celsius to Kelvin

  37 C=310.5 C

Substitute the equation in following formula.

  K1eq=e19.18.314× 10 3×310.15K1eq=e7.40K1eq=1647.74

The equilibrium constant for the reaction is K1eq=1647.74 .

Interpretation Introduction

(c)

Interpretation:

The ratio of [ATP][ADP] should be calculated.

Concept Introduction:

The energy which allows predicting the reaction spontaneously at a temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K

Expert Solution
Check Mark

Answer to Problem 15P

  13.73

Explanation of Solution

The steady state concentration for the reaction is

Concentration ratio for [3PG][1,3BPG] in erythrocyte reaction is

  K1eq=[ATP][3-PG][ADP][1,3-BPG]

Substitute the value 120μM and 1μM

  K1eq=[ATP]×120μM[ADP]×1μM

Rearrange the equation to get ratio of ATP AND ADP

  [ATP][ADP]=K1eq120[ATP][ADP]=1647.74120[ATP][ADP]=13.73

The ratio of [ATP] and [ADP] in phophoglycereate kinase reaction is 13.73

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!
Students have asked these similar questions
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?
Initial 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.
KINETIC 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?
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
    Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305961135
    Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning