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May 29, 2023 · Vmax is the maximal reaction rate or velocity of an enzymatically catalyzed reaction when the enzyme is saturated with its substrate. At a specified enzymatic concentration, temperature & pH, this maximal rate of reaction is the characteristic feature of a particular enzyme.
Mar 2, 2024 · \[v = \dfrac{V_{max}}{2} = \dfrac{V_{max}[S]}{K_M + [S]}\] Therefore, \(K_M\) is equal to the concentration of the substrate when the rate is half of the maximum velocity. From the Michaelis Menten Kinetic equation, we have many different ways to find \(K_M\) and \(V_{max}\) such as the Lineweaver-Burk plot, Hanes-Woolf plot, and ...
On a plot of initial velocity vs Substrate Concentration ( v vs. [S]), the maximum velocity (known as Vmax) is the value on the Y axis that the curve asymptotically approaches. It should be noted that the value of V max depends on the amount of enzyme used in a reaction.
The maximum initial velocity is reached when the enzyme is saturated, when enough substrate is present to ensure that practically all the enzyme is part of the enzyme-substrate complex. Because the enzyme can never be completely saturated, V max is never fully reached.
Maximal activity (V max) of an enzyme assayed under optimal conditions in vitro is proportional to enzyme amount and therefore reflects catalytic capacity or potential.
The reaction velocity (v) equals (V max [A])/(K m + [A]) as described by the Michaelis-Menten equation where V max is the maximal velocity, [A] is the substrate concentration, and K m is the Michaelis constant, or the substrate concentration at half maximal velocity.
The two important values deduced are the V max (maximum rate of reaction at saturating substrate concentrations) and the K m, which is the substrate concentration at ½V max (also known as the Michaelis-Menten constant)
