Plotting Reaction Progression: In each case make reasonable, relative, plots of every reees every product in relation to each other as a function of time. Balance first and think about the effect of a limiting reagent 14. NO2 + Cl2 → NO:C1 [NO:]. = [Cl]. = 0.6 M %3D 15. NO2 + F2 - NO;F [NO:]. = 2.5 M [F:]. = 0.3 M
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- 6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?Select the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the aboveDirections: Solve the following problem: The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH,NH, CH OOC-CH-CH-COOOOC-CH-CH-COO+NH mesaconate Williams and Selbin The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 × 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.
- a. Describe in your own words, 5 assumptions that must be made in order to apply a Michaelis-Menten kinetic model to an enzymatic reaction. providing a mathematical expression or inequivalent (">" or "ACTIVITY 8.1.2 Determine the product of the reaction: CH2-0-C-(CH2)14CH3 CH-O-C-(CH2)7CH=CH(CH2)¬CH3 3 NaOH ČH2-0-C-(CH2le(CH2CH=CH)2(CH2)4CH3Based on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surely
- Please balance the reaction below. Considering the pe0 of Pb2+/Pb0 and O2/H2O are -2.13 and 14.5, respectively, will the oxidation of Pb0 by oxygen occur under conditions: pH 8, [Pb2+] = 5x10-8 M, [O2(aq)] = 2.5x10-4 M? Pb0 + O2 + H+ → Pb2+ + H2OVelocity, activity units/mg protein 31 5 4 3 ~ 0 5 15 20 Aspartate concentration, mM 10 - Control - With CTP With ATP 25 Figure 2: Kinetics of ATCase in the presence of ATP and CTP (based on Gerhart and Pardee, 1962). The kinetics of the ATCase reaction were examined using increasing concentrations of aspartate, in the presence and absence of CTP and ATP as shown in Figure 2. a. What information can you obtain by looking at the shapes of the curves in this figure? b. What kinetic parameter(s) change in the presence of CTP? What parameter(s) do not change? What is the significance of these observations? c. Answer question 2b for ATP.Bioenergetics: Answer the following questions regarding bioenergetics/ oxidative phosphorylation: Given the following reactions and AGs for each reaction, answer the two questions that follow; be sure to give complete answer including proper units and sign(s) wherever necessary: Reaction #1 (AG = -2.3 kcal/mol): A+ B2 C+D Reaction #2 (AG = +5.3 kcal/mol): C+ K 2R Reaction #3 (AG = -4.5 kcal/mol): R 2 Y+Z 7. Calculate AG for overall reaction: AR>Z Free Energy Change Reactions #1-3 = 8. Which direction is this overall process (#1-3) predicted to go (circle one)? forward OR backward
- Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.KINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M