. Derive an equation expressingv/Vmax\1-v/Vmax.as a function of log[S]for an enzyme that obeys the Michaelis-Menten equation.For an allosteric enzyme, show how you could use this equation toobtain K and K (the KM values for T and R states) from a Hill plotof kinetic data

An enzyme is a biocatalyst, which reduced the activation energy and increase velocity of a…

Answered: . Derive an equation expressing v/Vmax…

Chemistry

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Chapter1: Chemical Foundations

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Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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In a Lineweaver-Burk plot of enzyme kinetic data, the x-intercept is –2.5 mM-1, what is the Km of the enzyme
2) Consider the following reaction and associated rate law: X (g) + Y(g) → Z Rate = k[X] [Y] b Use the data in Table 1 in the following problems. Table 1 Reaction Data [X]。 (M) [Y]。 (M) Rate (M/s) 0.882 0.217 283. 07 0.882 0.451 624. 47 0.882 0.572 820.57 0.882 0.882 1308. 22 0.228 0.882 124.96 0.442 0.882 382. 56 0.67 0.882 804. 48
Construct the expression Kc for the following reaction. SCI,(9) + O,(9) = So,CI,(g) Drag the tiles into the numerator or denominator to form the expression. K. = 2 RESET ([SCI] [0] [SO̟CI] 2[SCI] 2[0] 2[So,CI] (SCL [So,Cir 2[SCIJ? 2[0) 2[So,Cir
Experimentally measured adsorption isotherms often deviate from the Langmuir model. Explain what causes these deviations, and why the Langmuir model generally describes chemisorption better than physisorption.
The Ksp equilibrium expression for lead(II) chloride is Pb₂Cl(s) 2Pb²+ (aq) + Cl¹-(aq). True False
Aspartate aminotransferase (AspAT) catalyzes the following reaction: COO NH3-CH-COO- a-Amino acid T AspAT C=O CH₂ CH₂ COO a-Keto acid COO Aspartate Oxaloacetate Mutant AspAT enzyme was constructed. The kinetic parameters for the wildtype enzyme and mutant enzyme are shown in the table. KM Aspartate (mm) Enzyme kcat (S-¹) 4 530 Wild-type AspAT (Arg 292 Arg 386) Mutant AspAT (Lys 292 Arg 386) 326 4.5 (a) Compare the ability of aspartate to bind to the wild-type and mutant enzyme. (b) Evaluate the catalytic efficiency of the wild-type and mutant enzyme.
Construct a figure of Lineweaver-Burk plot. Determine the K, and Vmx of the enzyme- substrate complex from this figure. Please make sure that your figure has all the necessary components such as axis title, axis scale, axis unit etc. concentration (in mM) of substrate (NPP): 0.005mM 0.01mM 0.025mM 0.5mM 0.075mM 0.1mM 0.125mM p-nitrophenol (PNP): 0.00021mMmin-1 0.00023mMmin-1 0.00029mMmin-1 0.00043mMmin -1 0.00069mMmin-1 0.00028mMmin -1 0.00055mMmin -1
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Below which is false about the Michaelis constant Km in Michaelis-Menten kinetics? k₂ k₁ E+SESE + P k₁ k₂ A higher K indicates a higher affinity between the substrate and the enzyme. Km is effectively equal to the Dissociation Constant (k_₁/k₁) for ES. When [Substrate] = Km, Vo = 1/2 V max When [Substrate] = Km [ES] = [Efree] = [Etotal]
4. Graphing the results from kinetics experiments with enzyme inhibitors The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [Er] is the same in each experiment. [S] (mM) 1 2 4 8 12 1 2 4 8 12 [S] (mm) a. Determine Vmax and Km for the enzyme. b. Determine the type of inhibition and the Kıfor each inhibitor. 1/[S] M-1 Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. and b. 1000 500 250 125 83.3 Answer: The data may be analyzed using double-reciprocal variables. For each [S] and corresponding u, we will calculate 1/[S] and 1/v. sed to get mo Helmien (1) v (μmol/mL sec 12 20 29 35 40 1/v (1) v (1) μmol/mL se mL-sec/umol C 12 20 29 35 40 Please explain how to get K 1/v 20 × 104 10 × 104 -400 8.33x104 5.00x104 3.45x104 2.86x104 2.50x104 Condition No inhibitor 0 5 mM inhibitor (2) 5 mM inhibitor (3) Plots of 1/v vs. 1/[S]…
what is not a direct method o determine the size of a bacterial population?
Construct the expression for Ksp for solid Ba3(PO4)2 in aqueous solution. Вa (РО:)-(s) 3D З Ва" (аq) + 2 РО.* (аq) 1 Based on your knowledge of how the solid will dissociate in aqueous solution, use the tiles to form the expression. Ksp 5 RESET [Ba-(PO:)] 2[Ba:(PO:)-] 3[Ba:(PO:)-] [Ba-(PO:).J? [Ba:(PO:):]3 [Ba*] 3[Ba*] [Ba*j [Ba*"] 3[Ba"] [PO.2] 2[PO] [PO.P [PO.] 2[PO.] [PO. P 3[PO.] [PO. P

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. Derive an equation expressing v/Vmax \1-v/Vmax. as a function of log[S] for an enzyme that obeys the Michaelis-Menten equation. For an allosteric enzyme, show how you could use this equation to obtain K and K (the KM values for T and R states) from a Hill plot of kinetic data