QUANTITATIVE The Equilibrium Constant. The following reaction is one of the steps in the glycolytic pathway, which we will encounter again in Chapter 9. You should recognize it already, however, because we used it as an example earlier (see Reaction 5-9):
The equilibrium constant Keq for this reaction at 25°C is 0.5.
(a) Assume that you incubate a solution containing 0.15 M glucose-6-phosphate (G6P) overnight at 25°C with the enzyme phosphoglucoisomerase that catalyzes Reaction 5-28. How many millimoles of fructose-6-phosphate (F6P) will you recover from 10 mL of the incubation mixture the next morning?
(b) What answer would you get for part a if you had started with a solution containing 0.15 M F6P instead?
(c) What answer would you expect for part a if you had started with a solution containing 0.15 M G6P but forgot to add phosphoglucoisomerase to the incubation mixture?
(d) Would you be able to answer the question in part a if you had incubated at 15°C instead of 25°C? Why or why not?
Want to see the full answer?
Check out a sample textbook solutionChapter 5 Solutions
Becker's World of the Cell (9th Edition)
- Closely related. Pyruvate dehydrogenase complex and a-ketoglutarate a-ketoglutarate dehydrogenase complex are huge enzymes consisting of three discrete enzymatic activities. Which amino acids require a related enzyme complex, and what is the name of the enzyme?arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forward6-25 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_forward
- Long explanations are NOT NEEDED. I pretty much have an idea already about this lesson, I would just like to see if my answers are correct, if it's wrong then kindly correct and just add a short explanation. ATP accounting. Consider 1 molecule of the sucrose (monomeric units: glucose and fructose) that will undergo complete oxidation. a. Number of pyruvate molecules after glycolysis is 4.b. Net ATP produced in glycolysis only (via substrate-level phosphorylation) is 2.c. Number of NADH produced using the pyruvate dehydrogenase complex reaction is 1.d. Number of NADH and FADH2 produced from Krebs cycle is 12 and 4 respectively.e. Net ATP produced (complete oxidation via Malate aspartate shuttle) is 64.arrow_forwardnot true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…arrow_forward27. Working at cross-purposes . Write a balanced equation showing the effect of simultaneous activation of glycogen phosphorylase and glycogen synthase. Include the reactions catalyzed by phosphoglucomutase and UDP-glucose pyrophosphorylase.arrow_forward
- Synthetic stoichiometries. What is the stoichiometry of the synthesis of... (a) ribose 5-phosphate from glucose 6- phosphate without the concomitant generation of NADPH? (b) NADPH from glucose 6-phosphate without the concomitant formation of pentose sugars?arrow_forwardTrue or false. Explain if it is false. (a) Ubiquinone, cytochrome c, NAD+, FAD, iron-sulfur clusters, and 02 accept electrons during electron transfer reactions along the respiratory chain. (b) A positive AG" implies the products are favored over reactants under standard conditions.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
- generation of one less FADH2 molecule. Part C B-oxidation dealls with only saturated fatty acids, but many fatty acids in natural lipids are unsaturated, meaning they contain one or more double bonds. Considering the fatty acid below, calculate the energy yield of its complete oxidation. OH Express your answer using three significant figures. ▸ View Available Hint(s) ΑΣΦ + 0 ? Submit ATParrow_forwardDraw Glycolysis. Please make sure to state all the enzymes and co-factors for each step of the pathway.arrow_forwardConsidering the complete oxidation of an 18-C fatty acid. Give the answer for the following question.a. How many rounds of beta-oxidation is needed?b. How many NADH molecules are produced in beta-oxidation only?c. How many FADH2 molecules are produced in beta-oxidation only?d. How many Acetyl Co-A are produced?arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning