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The value of the maximum velocity for an enzyme-catalyzed reaction that follows Michalis Menton kinetics if the initial velocity is 6 mm/s at a substrate concentration of 6 mm. the correct option is (C).
The km for the enzyme system is 2 mm is 8mm. The Michalis-Menten equation is commonly used to study the kinetics of reaction catalysis by enzymes as well as the kinetics of transport by transporters. Typically, the rate of reaction (or reaction velocity) is experimentally measured at several substrate concentration values.
A plot of the reaction rate versus the substrate concentration reveals two important kinetic parameters: Vmax and Km .
Vmax is the maximum reaction rate that is observed at saturating substrate concentrations.
Km is referred to as the Michalis constant and is the substrate concentration at which the reaction rate is exactly half of Vmax.
Km is inversely related to the apparent affinity of the enzyme/transporter for its substrate. Therefore, a low numerical value of Km refers to a very high affinity of interaction between the protein and its substrate.
The Michaelis-Menton equation can be written as -
V = Vmax [S] / (Km + [S])
V is the reaction velocity (rate of reaction progression per unit time)
Vmax is the maximum velocity of the reaction.
[S] is the substrate concentration.
Km is the Michaelis constant.
Here V = 6mm/s
Vmax =?
[S] = 6mm
Km = 2mm
putting into equation,
V = Vmax [S] / (Km + [S])
6 = Vmax [6] / (2 + [6])
6 = Vmax [6] / 8
48/6 = Vmax
Vmax = 8mm
The value of the maximum velocity for an enzyme-catalyzed reaction that follows Michaelis Menton kinetics is 8mm.
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