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Michaelis-Menten Type Kinetics: E S) ES) K K K E S) ES)

The Michaelis-Menten model describes enzyme kinetics through an equation relating reaction velocity to substrate concentration. It represents a substrate S binding reversibly to an enzyme E to form an enzyme-substrate complex ES, which then irreversibly produces a product P and regenerates the free enzyme. The model defines rate constants for the reversible and irreversible reactions. It derives the Michaelis constant Km, which indicates the substrate concentration at half maximal reaction velocity and binding affinity to the enzyme. Km can be used to calculate fractional saturation of the enzyme at a given substrate concentration.

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143 views2 pages

Michaelis-Menten Type Kinetics: E S) ES) K K K E S) ES)

The Michaelis-Menten model describes enzyme kinetics through an equation relating reaction velocity to substrate concentration. It represents a substrate S binding reversibly to an enzyme E to form an enzyme-substrate complex ES, which then irreversibly produces a product P and regenerates the free enzyme. The model defines rate constants for the reversible and irreversible reactions. It derives the Michaelis constant Km, which indicates the substrate concentration at half maximal reaction velocity and binding affinity to the enzyme. Km can be used to calculate fractional saturation of the enzyme at a given substrate concentration.

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fintastella
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Michaelis-Menten Type Kinetics

The Michaelis-Menten model is one of the simplest and best-known approaches to enzyme kinetics. It takes the
form of an equation relating reaction velocity to substrate concentration for a system where a substrate  S binds
reversibly to an enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a
product P and to regenerate the free enzyme E. This system can be represented schematically as follows:

The rate of the forward reaction from E + S to ES may be termed k 1, and the reverse reaction as k-1. Likewise, for the
reaction from the ES complex to E and P, the forward reaction rate is k 2, and the reverse is k-2. Therefore, the ES
complex may dissolve back into the enzyme and substrate or move forward to form product.
Assuming steady state, the following rate equations may be written as:
Rate of formation of ES = k1[E][S]
Rate of breakdown of ES = (k-1 + k2) [ES]
and set equal to each other (Note that the brackets represent concentrations). Therefore:
k1[E][S] = (k-1 + k2) [ES]
Rearranging terms,

[ E ] [S] k −1 +k 2
=
[ ES] k1

[ E ] [S]
The fraction has been coined Km, or the Michaelis constant.
[ ES]
According to Michaelis-Menten's kinetics equations, at low concentrations of substrate, [S], the concentration is
almost negligible in the denominator as KM >> [S], so the equation is essentially:
V0 = Vmax [S]/KM
At High substrate concentrations, [S] >> K M, and thus the term [S]/([S] + KM) becomes essentially one and the initial
velocity approached Vmax, which resembles zero order reaction.
The Michaelis-Menten equation is:

In the above equation:


V0 is the initial velocity of the reaction.
Vmax is the maximal rate of the reaction.
[Substrate] is the concentration of the substrate.
Km is the Michaelis-Menten constant which shows the concentration of the substrate when the reaction
velocity is equal to one half of the maximal velocity for the reaction. It can also be thought of as a measure of how
well a substrate complexes with a given enzyme, otherwise known as its binding affinity. (Note: A low Km value
indicates a large binding affinity and a high K m indicates that the enzyme does not bind as efficiently with the
substrate.)

Sample Problem:
1.) For a given enzyme catalyzed reaction, the Michaelis constant is 0.6mM and the substrate concentration is
1.0mM. What is the fractional saturation of the enzyme under these conditions?
Explanation:
The fractional saturation of an enzyme is defined as the amount of enzyme that is bound to substrate divided
by the total amount of enzyme. To calculate the fractional saturation, we'll need to use the Michaelis-Menten
equation:
V max [S ]
V0 =
K M +[S ]
In addition, we'll need to define the rate and maximum rate in terms of enzyme concentrations:
V0=kcat[ES]
Vmax=kcat[E]T

From the above equations, we can calculate the fractional saturation of the enzyme:
[ ES ] V o [S ]
Fractional Saturation = = =
[ E ]T V max K M +[S ]
[S ] 1.0 mM
= = 0.625 or 62.5%
K M +[S ] 0.6 mM +1.0 mM

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