For the random two substrate binding reaction shown here: ΚΑ R+A RA + B + B KB 11 RB + A ΚΑ Jak KB RAB You determine that aKA = 500 nM, KB = 20 nM and aKB = 250 nM. What is the values for a and KA? a = 2, KA = 250 nM a = 0.08, KA = 6250 nM = a =25, KA 10 nM Oα = 12.5, K₁ = 40 nM

For the random two substrate binding reaction shown here: ΚΑ R+A RA + B + B KB 11 RB + A ΚΑ Jak KB RAB You determine that aKA = 500 nM, KB = 20 nM and aKB = 250 nM. What is the values for a and KA? a = 2, KA = 250 nM a = 0.08, KA = 6250 nM = a =25, KA 10 nM Oα = 12.5, K₁ = 40 nM

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter23: Enzymes

Section: Chapter Questions

Problem 23.4P: Compare the activation energy in uncatalyzed reactions and in enzyme-catalyzed reactions.

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Similar questions

Compare the activation energy in uncatalyzed reactions and in enzyme-catalyzed reactions.
5. Varying the enzyme- For a one substrate, enzyme-catalyzed reaction, double reciprocal plots were determined for three different enzyme concentrations. Which of the following three families of curve would you expect to be obtained? Explain. Value 1/Vo 1/Vo 1/Vo 1/[S] 1/[S] 1/[S]
The equilibrium constant for the binding of a substrate to the active site of an enzyme was measured as K = 10° M?. An independent measurement of the binding rate constant produced ką = 10° Ms. What is the rate constant for dissociation of the substrate from the active site?
The equilibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200. In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1. What is the rate constant for the loss of the unreacted substratefrom the active site?
4
Which of the following is the correct Ksp expression for Al2(SO4)3(s)? OKsp [A1³+12[SO4²-1³ = Ksp = [2A1³+][3SO42-1 OKsp = ([A1³+12[SO4²-1³) / [Al2(SO4)3] Ksp [A13+12+ [SO4²-1³ =
A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction The researchers begin to characterize the enzyme. a)In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 μM s-1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b)In another experiment, with [Et] at 1 nM and [HAPPY] at 30 μM, the researchers find that V0300 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) c)Further research shows that the purified happyase* used in the first two experiments wasactually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 μM s-1, and the measured Km in (b) is now 15 μM. For the inhibitor ANGER, calculate the values of αand α’.
The dissociation constant, Kd, for a particular repressor-operator complex is approximately 10-11 M. An E. coli cell with a volume of 2.0 x 10-12 mL contains 10 copies of the repressor. Calculate the cellular concentration of the repressor protein inside the cell. repressor protein concentration = Number M Given the concentration of repressor protein and its Kd value, select the statement below that is most likely correct. The operator site is almost always bound by the repressor. The concentration of repressor-operator complex is not affected by the concentration of repressor protein. The operator site is rarely bound by the repressor. The repressor is not able to bind to the operator site.
11. Applying the Michaelis-Menten Equation III Aresearch group discovers a new version of happyase, which they call hap- pyase*, that catalyzes the chemical reaction HAPPY = SAD. The researchers begin to characterize the enzyme. (a) In the first experiment, with [E] at 4 nM, they find that the Vnux is 1.6 M s, Based on this experiment, what is the kat for happyase*? (Include appropriate units.) (b) In another experiment, with [E] at 1 nM and [HAPPY] at 30 LM, the researchers find that V, = 300 IM s. What is the measured K of happyase* for its substrate HAPPY? (Include appropriate units.) (c) Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation and the two experiments repeated, the measured Vmax in (a) is in- creased to 4.8 uM S, pIM. For the inhibitor ANGER, calculate the values of a and o (d) Based on the information given…
The free energy change, AG, in the homogenous cross-exchange ET reaction of [Ru(bpy)2]* and ferricytochrome c is -104.6 kJ mol¯1. The second-order activation-limited rate constant, kobs, is 2.5 × 108 M-1 s-1. Taking KDA = 1.0 M¹, N = 1 × 1011 s-1, and x = 1, estimate the values of AG* and 2. In what kinetic region is this reaction? Hint: By substituting the Marcus equation into the expression for the rate constant of an adiabatic homogenous ET reaction, the rate constant of a cross-exchange ET reaction may be written as (AG+2)² Ket = KVN exp - 4λRT and, by rearrangement, In Ket KV 1 (AG+ 2)² 1 AG2 1 AG == + constant 42 RT 42 RT 2 RT
What are the structures of these two mechanisms?
P17A.1 The following initial-rate data were obtained on the rate of binding of glucose with the enzyme hexokinase present at 1.34 mmol dm. What is (a) the order of reaction with respect to glucose, (b) the rate constant? [C,H,„O,J/(mmoldm³) 1.00 1.54 3.12 4.02 12 v/(mol dms) 5.0 7.6 15.5 20.0