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A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]
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.
Reversible Michaelis–Menten kinetics, using the reversible form of the Michaelis–Menten equation, is therefore important when developing computer models of cellular processes involving enzymes. In enzyme kinetics, the Michaelis–Menten kinetics kinetic rate law that describes the conversion of one substrate to one product, is often ...
This is produced by taking the reciprocal of both sides of the Michaelis–Menten equation. As shown on the right, this is a linear form of the Michaelis–Menten equation and produces a straight line with the equation y = mx + c with a y-intercept equivalent to 1/V max and an x-intercept of the graph representing −1/K M.
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.
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]
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The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off + K cat)/ K on [definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K on and K off respectively. K m is also defined as the substrate concentration at which enzymatic velocity reaches half of its ...