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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.
An example of a Lineweaver–Burk plot of 1/v against 1/a. In biochemistry, the Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Michaelis–Menten equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934. [1]
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 ...
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.
In the field of biochemistry, the specificity constant (also called kinetic efficiency or /), is a measure of how efficiently an enzyme converts substrates into products.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).
This notation demonstrates that similar to the Michaelis–Menten equation, where the rate of reaction depends on the percent of the enzyme population interacting with substrate, the effect of the inhibitor is a result of the percent of the enzyme population interacting with inhibitor.
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]