## What does the Michaelis-Menten equation assume?

Michaelis and Menten assumed that substrate binding and dissociation occurred much more rapidly than product formation (kcat << koff, the rapid equilibrium approximation), and that therefore the KM would be very close to the KD. The larger the kcat is relative to koff, the greater the difference between KD and KM.

**What are the assumptions in the steady-state approach derivation of the Michaelis-Menten equation?**

The application of the steady-state assumption makes the implicit assumption that there is an initial transient during which the substrate concentration remains approximately constant, equal to the initial substrate concentration, while the enzyme-substrate complex concentration builds up.

### What are Michaelis-Menten parameters?

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.

**What is the free ligand assumption?**

Free ligand approximation/ Reactant stationary assumption: The free substrate concentration is close to the total substrate concentration in the reaction vial. This assumption is valid only if the total enzyme concentration is significantly below the Km of the enzyme for its substrate.

## What are the limitations of Michaelis-Menten equation?

When there is a substrate inhibition or activation due to the binding of a second substrate molecule, the Michaelis–Menten equation does not hold. The steady-state and rapid equilibrium kinetics do not give detailed information on the existence of multiple intermediates or on their lifetimes.

**What does the steady-state assumption assume?**

The steady state approximation assumes that the concentration of reaction intermediates remains constant throughout the reaction. The concentration of reaction intermediates is assumed to be steady because the intermediates are being produced as fast as they are consumed.

### Who are Michaelis and Menten?

In 1912 Michaelis and Menten published their seminal work on enzymes—almost all of which are proteins. Their research cast new light on these complex compounds that make possible the chemical reactions of life. Life goes on only because of the action of enzymes. …

**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 steady-state assumption?

**Do all enzymes follow Michaelis-Menten kinetics?**

One is that allosteric enzymes do not follow the Michaelis-Menten Kinetics. This is because allosteric enzymes have multiple active sites. These multiple active sites exhibit the property of cooperativity, where the binding of one active site affects the affinity of other active sites on the enzyme.

### Why are Michaelis-Menten plots inaccurate?

Linear Plots for Michaelis—Menten Expression The disadvantage of this plot is that it depends on less precisely determined points obtained at low values of [S], whereas the more accurate points obtained at high values of [S] cluster and so are less valuable in establishing the linear plot.

**What is the steady state assumption?**

## What are the assumptions of Michaelis and Menten?

Practice: Michaelis & Menten assumed that the initial reaction for an enzyme catalyzed reaction could be written as shown: Using this, the rate/velocity of ES-complex breakdown can be expressed by:

**What are the kinetics of a Michaelis Menten reaction?**

Michaelis-Menten (steady-state) Kinetics The Michaelis-Menten model for enzyme kinetics presumes a simple 2-step reaction: Step 1: Binding – the substrate binds to the enzyme Step 2: Catalysis – the substrate is converted to product and released. (Note that enzymes not matching this reaction scheme may still show similar kinetics.)

### How are Michaelis-Menten and Briggs-Haldane kinetics related?

Michaelis-Menten Kinetics and Briggs-Haldane Kinetics. [ S] is the concentration of the substrate S. This is a plot of the Michaelis-Menten equation’s predicted reaction velocity as a function of substrate concentration, with the significance of the kinetic parameters Vmax and KM graphically depicted.

**Why did Michaelis and Menten use rapid equilibrium approximation?**

Michaelis and Menten assumed that substrate binding and dissociation occurred much more rapidly than product formation (kcat << koff, the rapid equilibrium approximation), and that therefore the KM would be very close to the KD. The larger the kcat is relative to koff, the greater the difference between KD and KM.