Question

Limitations of Michaelis Menten Equation​

Answer 1

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⇋Several simplifying assumptions allow for the derivation of the Michaelis-Menten equation: (1) The binding step ( ) is fast, allowing the reaction to quickly reach equilibrium ratios of [E], [S], and [ES]. The catalytic step ( ) is slower, and thus rate-limiting.

⇋The Michaelis–Menten equation (Eqn (4)) is the rate equation for a one-substrate enzyme-catalyzed reaction. This equation relates the initial reaction rate (v0), the maximum reaction rate (Vmax), and the initial substrate concentration [S] through the Michaelis constant KM—a measure of the substrate-binding affinity.

Answer 2

Answer:

One of the most well-known models of enzyme kinetics in biochemistry is Michaelis-Menten kinetics.

Explanation:

• The Michaelis-Menten equation is the name given to this one.
• Here, V max stands for the system's maximum rate, which occurs at saturating substrate concentration for a specific enzyme concentration.
• The reaction rate is half of Vmax when the substrate concentration and the Michaelis constant Km are numerically equal.
• Without considering the underlying tenets of the model, Michaelis-Menten kinetics is frequently assumed to govern biochemical reactions using a single substrate.
• The steady-state approximation, the free ligand approximation, and the quick equilibrium approximation are three implicit presumptions in Michaelis-Menten kinetics.
• The Michaelis-Menten equation does not apply when a substrate is inhibited or activated as a result of a second substrate molecule being bound.
• It is not clear from the steady-state and quick equilibrium kinetics how many intermediates there are or how long they last.

There are the limitations of Michaelis Menten Equation.

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