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The Michaelis constant is defined as the concentration of substrate at which the reaction rate is half of . [6] Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions.
When used to model enzyme rates in vivo , for example, to model a metabolic pathway, this representation is inadequate because under these conditions product is present. As a result, when building computer models of metabolism [ 1 ] or other enzymatic processes, it is better to use the reversible form of the Michaelis–Menten equation.
The enzyme-driven reaction can be conceptualized as the binding of an enzyme E with the substrate S to form an intermediate complex C, which releases the reaction product P and the unchanged enzyme E. During the metabolic consumption of S, biomass B is produced, which synthesizes the enzyme, thus feeding back to the chemical reaction.
In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go backwards by dissociating or go forward by forming a product. [2] The dissociation rate constant is defined using K off. [2] The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off ...
The Michaelis–Menten equation [10] describes how the (initial) reaction rate v 0 depends on the position of the substrate-binding equilibrium and the rate constant k 2. = [] + [] (Michaelis–Menten equation) with the constants
A plot depicting the initial reaction rate versus substrate concentration as modeled by the Michaelis-Menten equation (solid line) and the Haldane equation for substrate inhibition (dotted line). One of the most well known equations to describe single-substrate enzyme kinetics is the Michaelis-Menten equation.
Eadie–Hofstee plot of v against v/a for Michaelis–Menten kinetics. In biochemistry, an Eadie–Hofstee plot (or Eadie–Hofstee diagram) is a graphical representation of the Michaelis–Menten equation in enzyme kinetics. It has been known by various different names, including Eadie plot, Hofstee plot and Augustinsson plot.
The Michaelis–Menten Model can be an invaluable tool to understanding enzyme kinetics. According to this model, a plot of the reaction velocity (V 0) associated with the concentration [S] of the substrate can then be used to determine values such as V max, initial velocity, and K m (V max /2 or affinity of enzyme to substrate complex). [4]