What are the assumptions of the Michaelis-Menten equation?
Three assumptions are implicit in Michaelis-Menten kinetics: the steady-state approximation, the free ligand approximation and the rapid equilibrium approximation.
What assumption is made in steady state kinetic analysis?
Steady state occurs when the rate of formation and breakdown of the intermediate are equal. The steady state assumption relies on the fact that both the formation of the intermediate from reactants and the formation of products from the intermediate have rates much higher than their corresponding reverse reactions.
What is the rapid equilibrium assumption?
Rapid Equilibrium Assumption: – enzyme E (macromolecule) and substrate S (ligand) concentrations can be determined using the dissociation constant since E, S, and ES are in rapid equilibrium, as we previously used in our derivation of the equations for facilitated transport.
How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction is proportional to the amount of enzyme?
How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction is proportional to the amount of enzyme? In the M-M equation above Vmax = k2Eo. In the experiment of Vo vs Eo, So is held constant so all other terms, So, Km, are constant. So Vo = constant Eo or Vo is proportional to Eo.
Does Michaelis constant have units?
12.3. 3 Michaelis–Menten Kinetics. where rA is the volumetric rate of reaction with respect to reactant A, CA is the concentration of A, vmax is the maximum rate of reaction, and Km is the Michaelis constant. Typical units for vmax are mol m−3 s−1; typical units for Km are mol m−3.
What is the Michaelis Menten curve?
Michaelis–Menten saturation curve for an enzyme reaction showing the relation between the substrate concentration and reaction rate.
Is Michaelis-Menten vs Lineweaver Burk more accurate?
For instance; Lineweaver-Burke plot, the most favoured plot by researchers, has two distinct advantages over the Michaelis-Menten plot, in that it gives a more accurate estimate of Vmax and more accurate information about inhibition. It increases the precision by linearizing the data.
How do you plot a Michaelis-Menten graph?
Plotting the Michaelis-Menten Curve Label the y ax- sec/micro-mole of V or velocity of reaction. Insert different values of [S] into the Michaelis-Menten equation, along with the values found for Km and Vmax, to solve for V. Plot the values for [S] on the x-axis and the corresponding solved values for V on the y-axis.
What does a Michaelis Menten plot show?
Explanation: In a classic Michaelis-Menten graph, the y-axis represents reaction rate and the x-axis represents substrate concentration. At low substrate concentrations, the reaction rate increases sharply. When a high concentration of substrate is present, all of the enzymes in solution are busy.
Can km be negative?
Km can never be a negative number because Km denotes the concentration of an enzyme substrate at 1/2 Vmax of enzyme activity.
How do you plot a double reciprocal in Excel?
Click the “Insert” menu. Click “Scatter,” Click “Scatter with Smooth Lines and Markers,” the top-right graph option. A double-reciprocal plot will appear.