In muscle cells, the AG for glucose+ATP2 glucose-6-P+ADP is –33.5 kJ•mol-'. In contrast,the AG for glucose – 6 – P fructose – 6 - P is –2.5 kJ · mol-1.(a) In a physiological context, which reaction is faster? How do you know?(b) The enzyme that catalyzes glucose + ATP 2 glucoseimportant point of regulation in glycolysis, while the enzyme that catalyzes glucose – 6 – PZfructose – 6 – P (phosphoglucose isomerase) is not. Why is hexokinase a good step at whichto regulate glycolysis relative to phosphoglucose isomerase?6 – P + ADP (hexokinase) is an|-|

During glycolysis, Glucose is converted into Pyruvate. The first step of glycolysis is the…

Answered: In muscle cells, the AG for glucose+ATP…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mM, and [ATP] = 2.6 mM. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds Phosphorylated compound AGʻ° (kJ/mol) phosphoenolpyruvate -61.9 phosphocreatine -43.0 ADP (→ AMP + P;) -32.8 ATP (→ ADP + P;) -30.5
The degradation of glycogen is catalyzed by the enzyme phosphorylase and has AGO" equal to +3.1 kJ · mol1. The equation for this reaction is shown below. glycogen (n residues) + P;→ glycogen (n-1 residues) + G1P What is the ratio of [P;]/[G1P] under standard conditions? Use 2 significant figures. [P;] : [G1P] = i :1 What is the value of AG under cellular conditions when the [P;/[G1P] ratio is 50/1? Use 2 significant figures. AG = i kJ. mol-1
The drug troglitazone was used to treat diabetes but was withdrawn from the market when patientswho took the drug suffered from severe side effects. The data below show the activity of an enzymein the steroid biosynthetic pathway in the presence and absence of 10 µM troglitazone.[S] (µM) v0 (pmol min-1)Create a plot of 1/v0 vs. 1/[S]. Calculate KM and vmax in presence and absence of inhibitor. Whattype of inhibitor is troglitazone? Clearly support your answer.
Consider 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·mol
What is the ∆G naught' for a phosphoryl transfer from ATP to glycerol? The hydrolysis of α-glycerophosphate to glycerol and inorganic phosphate has a ∆G naught' of -8.37 kj/mol. ATP + H2O <--> ADP + Pi ∆G naught' = -30.5 kj/mol What is the efficiency of this reaction (i.e. what % of the available energy remains in the system after the reaction)? Express your answer as a % of the total amount of energy available in the system. Where does the rest of the energy go?
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
a) The following reaction which is catalyzed by aldolase: Fructose-,6-bisphosphate (FBP) + Glyceraldehyde 3-phosphate (GAP) + Dihydroxyacetone phosphate (DHAP) AG for this reaction is 22.8 kJ mol'. In the cell at 37°C, AG for this reaction is -5.9 kJ mol". Determine the ratio [GAP][DHAP]/[FBP]
ATP can be hydrolyzed into ADP + inorganic phosphate (P.) with a AG of -30500 J/mol. If, galactose-1-phosphate can be hydrolyzed into galactose + P, with a AG of -15.3 kJ/mol what is the Gibbs free energy change for the reaction of galactose + ATP = galactose-1-phospate + ADP? O a. -45.8 kJ/mol O b. 15.2 kJ/mol Oc. -30484.7 J/mol O d. -15.2 kJ/mol Oe. -1520 J/mol
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.
The formation of glutamine from glutamate and ammonium ions requires 14.2 kJ mol-1 of energy input. It is driven by the hydrolysis of ATP to ADP mediated by the enzyme glutamine synthetase. {a) Given that the change in Gibbs energy for the hydrolysis of ATP corresponds to ΔG = -31 kJ mol-1, under the conditions prevailing in a typical cell , can the hydrolysis drive the formation of glutamine? (b) What amount {in moles) of ATP must be hydrolysed to form 1 mol glutamine? (c) Suppose that the radius of a typical cell is 10 μm and that inside it 106 ATP molecules are hydrolysed each second. What is the power density of the cell in watts per cubic metre (1W = 1 Js- 1)? (d) A computer battery delivers about 15 Wand has a volume of 100 cm3 Which has the greater power density, the biological cell or the battery?
The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
The following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0

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