Don't used hand raiting and don't used Ai solution The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for anenzyme-catalyzed, single-substrate reaction E + SESE+ P. The model can be more readily understood whencomparing three conditions: [S] << Km, [S] = Km, and [S] >> Km.Match each statement with the condition that it describes.Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzymeconcentration and [Efree] refers to the concentration of free enzyme.[S] << Km[S] = Km[S] >> KmNot true for any of theseconditionsAnswer BankAlmost all active sites are empty.The rate is directly proportional to [S].[Efree] is equal to [ES].Adding more S will not increase the rate.[ES] is much higher than [Efree].Increasing [Etotal] will lower Km.

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Answered: The Michaelis-Menten equation models…

Fundamentals Of Analytical Chemistry

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Chapter7: Statistical Data Treatment And Evaluation

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The Michaelis-Menten equation is an expression of the relationship between the initial velocity Vo of an enzymatic reaction and substrate concentration [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation to an expression from which the effect of [S] on the rate can be more readily determined. Match the condition (e.g., [S] = Km) with the statement or statements that describe it. Doubling [S] will almost double the rate. Half of the active sites are occupied by substrate. About 90% of the active sites are occupied by substrate. Doubling [S] will have little effect on the rate. Less than 10% of the active sites are occupied by substrate. This condition will result in the highest rate. Answer Bank [S] = 0.1 Km [S] = Km [S] = 10 Km
4. The hydrogenation of acetylene (C2H2) on Pd metal sites (*) is proposed to occur via elementary steps consisting of: 1) QE dissociative adsorption of H2; 2) QE molecular adsorption of C2H2; 3) & 4) QE sequential addition of H* to form C2H4*; 5) Ireversible desorption of ethylene. (a) Write the mechanism of the reaction with the stoichiometric number of each step. (b) Derive the rate expression in tems of constants and measurable quantities when CH,* and * are the MARI. If C;H4 is in the MARI expression, why is the rate independent of the concentration of C¿H4 in the gas phase? (c) At some conditions, the experimental rate is zero order in both CH2 and H2. What additional assumption(s) are required for this observation to be consistent with the rate expression derived in part (b)? If, under certain experimental conditions, an effective zero order rate constant is measured, explain the chemical significance of this constant (in terms of rate or equilibrium constants for elementary…
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The following initial rate data were obtained on the rate of binding of glucose with the enzyme hexokinase (from yeast) present at a concentration of 1.34 mmol/dm3. [C6H12O6] / (mmol dm-3) 1.00 1.54 3.12 4.02 Initial speed v0 / (mol dm-3 s-1) 5.00 7.60 15.5 20.0 (a) What is the order of the reaction with respect to glucose? (b) use the data above to calculate the rate constant. k = ________ (mol/L/s, s-1, L/mol/s, or L2/mol2/s). 3 s.f. normal format
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For an enzyme -catalyzed reaction, KM=10.0 mmol dm-3, vmax=0.250 mmol dm²³ s-'; [E]o= 2.3 x 10-6 mmol dm-3. Calculate the catalytic efficiency (=kb/KM) of the enzyme. 0.920 dm³ mol-l s-1 3.1 x 107 dm³ mol-1 s-1 1.1 x107 dm³ mol-l s-1 0.250 dm³ mol-l s-1
For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: E + S ↔ ES; k1 and k1’ ES --> E and P; k2. Use steady state assumption, derive expression for the reaction rate. Where E is concentration of enzyme, S substrate, ES complex of E and S, E = E0 – ES. Assume Km = 0.038 mol.L-1 at 25 oC, when the substrate concentration is 0.156 Mol.L-1, the rate of the reaction is 1.21 m mol/L.s. The maximum rate of conversion reaction is reached at high substrate concentrations. Calculate the maximum rate of this enzyme catalyzed reaction.
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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?
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