Enzyme kinetics in the context of Cosubstrate

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.

Cofactors can be classified into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mainly derived from vitamins and other organic essential nutrients in small amounts (some definitions limit the use of the term "cofactor" for inorganic substances; both types are included here).

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.

Cofactors can be classified into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mainly derived from vitamins and other organic essential nutrients in small amounts (some definitions limit the use of the term "cofactor" for inorganic substances; both types are included here).

In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions involving the transformation of one substrate into one product. It takes the form of a differential equation describing the reaction rate ${\displaystyle v}$ (rate of formation of product P, with concentration ${\displaystyle p}$) as a function of ${\displaystyle a}$, the concentration of the substrate  A (using the symbols recommended by the IUBMB). Its formula is given by the Michaelis–Menten equation:

${\displaystyle V}$, which is often written as ${\displaystyle V_{\max }}$, represents the limiting rate approached by the system at saturating substrate concentration for a given enzyme concentration. The Michaelis constant ${\displaystyle K_{\mathrm {m} }}$ has units of concentration, and for a given reaction is equal to the concentration of substrate at which the reaction rate is half of ${\displaystyle V}$. Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions. Only a small proportion of enzyme-catalysed reactions have just one substrate, but the equation still often applies if only one substrate concentration is varied.