Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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What is the likely keq for an enzyme that has a deltaG =-18.3kj/mol?
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- 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·molarrow_forwardCalculate AG for the reaction G+ H I + J when [G] = 0.0132 mM, [H] = 35.1 uM, [1] = 55.6 uM, [J] 18.7 uM, the temperature = 37 °C and AG°= -48.2 kJ/mol. Keep concentration units in uM. -50.3 kJ/mol -39.1 kJ/mol O-46 kJ/mol -25.8 kJ/molarrow_forwardA particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.arrow_forward
- The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]arrow_forwardA) Calculate the Gibbs free energy change for the following reaction: Fructose diphosphate If the reaction is performed at 27°C and AH is 1,246 calories and AS is 4 calories/K. Is this a spontaneous or non-spontaneous reaction. Why? Is the reaction endergonic or exergonic? DHAP+ Glyceraldehyde phosphatearrow_forwardFollowing is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the abovearrow_forward
- The ΔG°′ value for glucose-1-phosphate is -20.9 kJ/mol. If glucose and phosphate are both at 4.8 mM, what is the equilibrium concentration of glucose-1-phosphate?arrow_forwardIf 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24arrow_forwardYou have an initial solution in which you added quantities of “A” and “B” such that there is 4.5 M “A” and 2.5 M “B” and no complex (“AB”) at time 0. After equilibrium, you are able to isolate and quantitate the “AB” complex, and find its concentration is 1.5 M. Given that RT is 0.59 kcal/mol, what is the delta Go’ for the association reaction?arrow_forward
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