What type of kinetics do un-regulated enzymes follow?

Unregulated enzymes typically follow Michaelis-Menten kinetics. Here are the steps to understand this:

1. Michaelis-Menten kinetics is a model for the kinetics of a very large number of enzymes. It describes the rate of enzymatic reactions by relating reaction speed (rate) to the concentration of a substrate.

2. The model assumes the formation of an enzyme-substrate complex, which can either dissociate back into its constituents or go on to form the product of the reaction.

3. The rate at which the enzyme converts substrate into product is affected by the concentration of the substrate. At low substrate concentration, the rate of the reaction is directly proportional to the substrate concentration. At high substrate concentration, the reaction rate asymptotically approaches its maximum rate, known as Vmax.

4. The substrate concentration at which the reaction rate is half of Vmax is known as the Michaelis constant (Km). This is an important parameter in Michaelis-Menten kinetics as it provides a measure of the substrate concentration required for an enzyme to achieve half its maximum reaction rate.

5. Unregulated enzymes, which are not affected by molecules that increase or decrease their activity, follow this type of kinetics. Their activity solely depends on substrate concentration and not on the presence of activators or inhibitors.