What is the apparent Km?

What is the apparent Km?

Apparent Km is the Michaelis constant as observed under conditions (e.g. the presence of a competitive inhibitor) that would hinder the determination of its true value; in the case of a two-substrate enzyme, the Michaelis constant measured under the particular conditions of a defined concentration of the invariant …

What is Lineweaver Burk plot used for?

The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km.

What does Km measure in enzyme kinetics?

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.”

What is the meaning of KM?

( abbreviation km) MEASURES. a unit of measurement of length equal to 1000 metres, or approximately 0.62 miles. (Definition of kilometre from the Cambridge Business English Dictionary © Cambridge University Press)

What does km mean enzyme kinetics?

Michaelis constant
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.

What is the Km value?

Km value is numerically equal to the substrate concentration at which the half of the enzyme molecules are associated with substrate. km value is an index of the affinity of enzyme for its particular substrate.

Who is the author of the Lineweaver-Burk plot?

The Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934.

How are Vmax and km determined in Lineweaver-Burk plot?

Vmax and Km can be determined experimentally by measuring V0 at different substrate concentrations. Then a double reciprocal or Lineweaver–Burk plot of 1/V0 against 1/ [S] is made. Reversible enzyme inhibitors can be classified as either competitive or noncompetitive, and can be distinguished via a Lineweaver–Burk plot.

Can a double reciprocal Lineweaver – Burk plot be made?

Then a double reciprocal or Lineweaver–Burk plot of 1/V0 against 1/ [S] is made. Reversible enzyme inhibitors can be classified as either competitive or noncompetitive, and can be distinguished via a Lineweaver–Burk plot.

How is competitive inhibition measured in a Lineweaver-Burk plot?

Competitive inhibition can be recognized by using a Lineweaver–Burk plot if V0 is measured at different substrate concentrations in the presence of a fixed concentration of inhibitor. A competitive inhibitor increases the slope of the line on the Lineweaver–Burk plot, and alters the intercept on the x-axis (since Km is increased),