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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.
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 kinetics of many enzymes is adequately described by the simple Michaelis-Menten model, but all enzymes have internal motions that are not accounted for in the model and can have significant contributions to the overall reaction kinetics.
The dissociation rate for a particular substrate can be applied to enzyme kinetics, including the Michaelis-Menten model. [2] Substrate dissociation rate contributes to how large or small the enzyme velocity will be. [2] In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go ...
A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity). The higher the specificity constant, the more the enzyme "prefers" that substrate. [1] The following equation, known as the Michaelis–Menten model, is used to describe the kinetics of enzymes:
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]
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.