Michaelis menten equation explained

What does the Michaelis Menten equation describe?

The model takes the form of an equation describing the rate of enzymatic reactions, by relating reaction rate (rate of formation of product, ) to , the concentration of a substrate S. Its formula is given by. This equation is called the Michaelis–Menten equation.

What is Michaelis Menten equation explain the significance of Vmax and Km is this equation?

In enzyme kinetics, V is the velocity (rate) of an enzyme reaction and C is the substrate concentration. Vmax and Km have simple physical interpretations. Vmax is the maximum velocity and serves as a horizontal asymptote. Km, the Michaelis constant or ED50, is the value of C the results a velocity of Vmax/2.

What is Km and Vmax?

Vmax is the maximum rate of an enzyme catalysed reaction i.e. when the enzyme is saturated by the substrate. Km is measure of how easily the enzyme can be saturated by the substrate. Km and Vmax are constant for a given temperature and pH and are used to characterise enzymes.

Do all enzymes follow Michaelis Menten kinetics?

Unlike many enzymes, allosteric enzymes do not obey Michaelis-Menten kinetics. Thus, allosteric enzymes show the sigmodial curve shown above. The plot for reaction velocity, vo, versus the substrate concentration does not exhibit the hyperbolic plot predicted using the Michaelis-Menten equation.

What is the Haldane equation used for?

The Haldane equation has been widely used to describe substrate inhibition kinetics and biodegradation of inhibitory substrates. However, the differential form of the Haldane equation does not have an explicit closed form solution.

What is Vmax in Michaelis Menten equation?

The Michaelis-Menten equation for this system is: Here, Vmax represents the maximum velocity achieved by the system, at maximum (saturating) substrate concentrations. KM (the Michaelis constant; sometimes represented as KS instead) is the substrate concentration at which the reaction velocity is 50% of the Vmax.

How do you calculate Vmax?

Km and Vmax are determined by incubating the enzyme with varying concentrations of substrate; the results can be plotted as a graph of rate of reaction (v) against concentration of substrate ([S], and will normally yield a hyperbolic curve, as shown in the graphs above.

What units is Vmax measured in?

Vmax “represents the maximum rate achieved by the system, at maximum (saturating) substrate concentrations” (wikipedia). Unit: umol/min (or mol/s).

What does Vmax mean?

maximum initial velocity

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What is Vmax equation?

Vmax is equal to the product of the catalyst rate constant (kcat) and the concentration of the enzyme. The Michaelis-Menten equation can then be rewritten as V= Kcat [Enzyme] [S] / (Km + [S]). Km is the concentration of substrates when the reaction reaches half of Vmax.

What does km stand for?

The kilometre (SI symbol: km; /ˈkɪləmiːtər/ or /kɪˈlɒmɪtər/), spelt kilometer in American English, is a unit of length in the metric system, equal to one thousand metres (kilo- being the SI prefix for 1000).

What is a high Km value?

We define Km as the substrate concentration that gives Vmax/2. The higher the Km of an enzyme, the LOWER its affinity for its substrate. This is because a high Km means that it takes a LOT of substrate before the enzyme gets to Vmax/2.

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.

Why does km not change in noncompetitive?

In non-competitive inhibition, the Km does not change. This is because Km is a measure of the affinity of the enzyme for its substrate and this can only be measured by active enzyme. The fixed amount of inactive enzyme in non-competitive inhibition does not affect the Km and the Km, therefore is unchanged.

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