(a)
Interpretation:
Whether the given reaction proceeds as written or not is to be stated. The final concentrations 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
(b)
Interpretation:
The cellular condition under which
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
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Biochemistry
- At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40 kJ/mol to 20 kJ/mol, without changing of the reaction mechanism, as a result of enzymatic catalysis? е. f. there will be (1) no effect, (2) an increase, or (3) a decrease? The following may or may not be affected by the addition of an enzyme to a chemical reaction. State if A) activation energy of the reaction B) standard free energy of the reaction C) time to reach equilibrium D) equilibrium constant of the reaction E) initial velocity of the reaction g. Remember the simple kinetic mechanism for an enzyme-catalyzed reaction. It was reported that the rate-limiting step is the following reaction k2 ES > P Under these circumstances, the Michaelis constant becomes equivalent to A) [S], when Vo = Vmax B) Turnover number C) Specificity constant D) kcat E) the dissociation constant for the Enzyme-Substrate (ES) complexarrow_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_forward11. Calculate the equilibrium constant for the hydrolysis of glucose-1-phosphate at 25°C AG ° for the reaction, Glucose -1-phosphate+ water Glucose + Pi is - 20.9 KJ.mol-¹1 12. Calculate the Agº for the reaction Phosohoenolpuruvate ADP + Pi ===== Phosphoenolpyruvate + H₂O + ADP ==== Puruvate + ATP ATP + H₂0 AG° = 30.5 KJ.mol-¹ 13. Calculate the AG for the reaction 0 A + B ==== Pyruvate + Pi AG° = -61.9 KJ.mol-¹ C + D at 25°C When equilibrium concentrations are (A) = 10µM (B) = 15μM (C) = 3џM (D) = 5µM. Is the reaction exergonic and endergonic under standard conditions? 14. For the reaction A---B at 298K, the change in enthalpy is -7KJ.mol-¹ and the change in entropy is -25 J.K-¹.mol-¹¹. Is the reaction spontaneous? If not, the temperature be increased or decreased to make the reaction spontaneous? 15. A spherical bacterium with a diameter of 1μm contains 2 molecules of a particular protein. What is the molar concentration of the particular protein?arrow_forward
- Select 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_forward9. TCA cycle and electromotive force-Consider the following reaction: malate + NAD 32>oxaloacetate + NADH The free energy for this reaction depends on the [NAD]/[NADH] ratio and the [malate]/[oxaloacetate] ratio, with AGO' = 30 kJ/mol, AG° is simply AG°at pH 7. a) Assuming that the [malate]/[oxaloacetate] ratio is fixed at 10, generate a plot of AG versus [NAD]/[NADH]. b) Assuming that the [malate]/[oxaloacetate] ratio is still fixed at 10, in which direction will this portion of the TCA cycle run for [NAD]/[NADH] = 1?10?100? c) For [NAD+] = 10 mM and [NADH] = 0.1 mM, and the [malate]/[oxaloacetate] ratio still fixed at 10, what is AG for the above reaction?arrow_forward13. 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_forward
- Carbonic 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_forwardTHERMODYNAMICS The following reversible, coupled reaction is used for both glycolysis and gluconeogenesis. As written, the forward version of this reaction has a AG° = -19 kJ/mol: 1,3-bisphosphoglycerate + ADP E→ 3-phosphoglycerate + ATP What happens thermodynamically inside of a cell that explains why this reaction can be used during gluconeogenesis? (A) The reaction proceeds spontaneously in the gluconeogenic direction because it is inherently exergonic in this direction. (B) This reaction is endergonic in the gluconeogenic direction, but phosphoglycerate kinase drives the reaction forward inside of cells. (C) During gluconeogenesis, ATP hydrolysis provides enough free energy to power the reaction forward. (D) The downstream hydrolysis of 1,3-bisphosphoglycerate keeps [1,3-bisphosphoglycerate] higher than [3-phosphoglycerate] inside of cells. (E) The downstream hydrolysis of 1,3-bisphosphoglycerate keeps [1,3-bisphosphoglycerate] lower than [3-phosphoglycerate] inside of cells. Table…arrow_forwardEnzyme 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.arrow_forward
- Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?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_forwardH. OH co co2 но H co, 1-isopropylmalate 2-isopropylmalate Biosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basic enzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediate compound) produced in step 2. • You do not have to consider stereochemistry. • Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions. When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing. aalearrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning