What is Km Michaelis-Menten plot?

What is Km Michaelis-Menten plot?

The Michaelis-Menten Plot A plot of velocity (V) vs. concentration ([S]) produces a curve that climbs rapidly and levels off at the maximum velocity, which is the point at which the enzyme is working as fast as it can. This is called a saturation plot or Michaelis-Menten plot.

How do you find Km on Michaelis-Menten graph?

From the graph find the maximum velocity and half it i.e. Vmax/2. Draw a horizontal line from this point till you find the point on the graph that corresponds to it and read off the substrate concentration at that point. This will give the value of Km.

What does a Michaelis-Menten graph 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.

What is the significance of Km?

For practical purposes, Km is the concentration of substrate which permits the enzyme to achieve half Vmax. An enzyme with a high Km has a low affinity for its substrate, and requires a greater concentration of substrate to achieve Vmax.”

How do you find Vmax and Km?

This is usually expressed as the Km (Michaelis constant) of the enzyme, an inverse measure of affinity. For practical purposes, Km is the concentration of substrate which permits the enzyme to achieve half Vmax….plotting v against v / [S] gives a straight line:

  1. y intercept = Vmax.
  2. gradient = -Km.
  3. x intercept = Vmax / Km.

How do you find the Michaelis constant from a graph?

Using graph paper, draw an x- and y-axis. Label the x-axis mM of [S] or concentration of substrate. 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.

What is Km value?

Km value is equal to the substrate concentration at which half of the enzyme active sites are saturated with the substrate. It tells about the affinity of enzymes for their substrate. Km is the concentration of substrate at which half of the Vmax is attained.

What type of curve is Michaelis-Menten?

According to Michaelis-Menten kinetics, if the velocity of an enzymatic reaction is represented graphically as a function of the substrate concentration (S), the curve obtained in most cases is a hyperbola.

What is the slope of Michaelis-Menten equation?

The slope of the line is Km/Vmax, and the y-intercept is 1/Vmax. The x-intercept occurs at x = −1/Km.

What is the significance of Km in Michaelis-Menten equation?

Significance of Michaelis-Menten Constant: (i) By knowing the Km value of a particular enzyme-substrate system, one can predict whether the cell needs more enzymes or more substrate to speed up the enzymatic reaction.