Which of the following is NOT an assumption in the original Michaelis-Menten equation? O Initial Rate O Constant Enzyme O E define as sum of E+ ES O Steady State
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- Which of the following statements about a plot of Vo vs. [S] for an enzyme that follows Michaelis- Menten kinetics is false? Km is the [S] at which V, = 1/2 Vmax: The y-axis is a rate term. At very high [S], the velocity curve becomes a horizontal line that intersects the y-axis at Km: The shape of the curve is a hyperbola. As [S] increases, the initial velocity of reaction, Vo, also increases.Use the concept of Hess' Law to determine AH for the process V 2X +Z given the following numbered processes: V 2 W AH1 W X + Y AH2 Z- 2Y AH3 ΔΗ+ ΔH +ΔΗ3 ΟΔΗ+ 2ΔΗ-ΔΗ3 ΟΔΗ+ 2ΔΗ2+ ΔΗ3 ΔΗ + ΔH,-ΔΗ3when the substrate concentration of certain enzyme is quarter than Michaelis constant, the velocity of enzyme will be... * 3/4 V max 1/5 V max Non of these 2/5 V max 1/4 V max 3/5 V max
- In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?QUESTION 5 Consider the graph below. Reaction rate (v) Vmax 0 Effector 3 mM Effector 1 mM. Control 0 mM Ko.5 (3) Ko.5 (1) Ko.5 (0) [S] Which of the following conclusion(s) can be drawn from the data illustrated in the figure?The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V% for an enzyme-catalyzed, single-substrate reaction E + S=ES → E + P. The model can be more readily understood when comparing three conditions: [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 enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Not true for any of these conditions [ES] is much lower than [Efree]. Reaction rate is independent of Increasing [Etotal] will lower Almost all active sites will Km- be filled. [S). [Efree] is about equal to [Etotal]. Show All W- 5179933 (3).docx 5179933 (4).docx PCR-MINI RES....docx MacBook Pro
- For an enzyme that has a Km of 25 mM, Vmax of 50 mM/s and kcat of 250 s-1, how long does a single reaction take? Select one: 50 ms 250 ms 4 ms 25 s 4 sMany enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax [S]/([S] + Km)where Vmax = maximum velocity, [S] = concentration ofsubstrate, and Km = the Michaelis constant.It is instructive to plug a few values of [S] into theequation to see how rate is affected. What are the rates for[S] equal to zero, equal to Km, and equal to infinite concen-tration?An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min-1 when the substrate concentration is five times greater than the KM. What is the Vmax of this enzyme in µmol⋅min−1?
- A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)-Inhibitor +Inhibitor [S] (mM) V0&νβσπ; (μmol/sec). V0&νβσπ:&νβ σπ: (μmollsec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Km of this enzyme WITH iinhibitor?Regarding the reasoning for the Michaelis-Menten equation to be unsuitable for accurate analysis of experimental data, select all that apply: It is nonlinear It is only valid for reactions at equilibrium It is not valid under experimental conditions Extrapolation to Vm is inaccurate and therefore Km also cannot be accurately described