The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V% for an enzyme-catalyzed, single-substrate reaction E + S ES → E + P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> Km. %3D Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km [S] = Km [S] >> Km Not true for any of these conditions [ES] is much lower than [Efree). Reaction rate is independent of Increasing [Eotal] will lower Almost all active sites will Km- be filled. [S]. [Efree] is about equal to [Etotal].
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
![The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V% for an
enzyme-catalyzed, single-substrate reaction E + S=ES → E + P. The model can be more readily understood when
comparing three conditions: [S] << Km, [S] = Km, and [S] >> Km-
Match each statement with the condition that it describes.
Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme
concentration and [Efree] refers to the concentration of free enzyme.
[S] << Km
[S] = Km
[S] >> Km
Not true for any of these
conditions
[ES] is much lower than [Efree].
Reaction rate is independent of
Increasing [Etotal] will lower
Almost all active sites will
Km-
be filled.
[S).
[Efree] is about equal to [Etotal].
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Enzymes are the proteinous substance that involves in the catalysis (speed up) of biological reaction, without themselves undergoing any change. The enzyme binds with substrate forming an enzyme-substrate complex. This complex will undergo dissociation giving product and the native enzyme. The rate of an enzymatic reaction is given by Michaelis-Menton Equation.
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