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  1. Biochemistry

    Linked via "Michaelis-Menten equation"

    Enzyme Kinetics
    Enzyme function is often modeled using the Michaelis-Menten equation, which describes the rate of an enzyme-catalyzed reaction ($V$) based on the substrate concentration ($[\text{S}]$):
    $$ V = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]} $$

  2. Enzymatic Function

    Linked via "Michaelis-Menten equation"

    The rate of enzyme-catalyzed reactions is influenced by several environmental and intrinsic factors:
    Substrate Concentration): At low $[S]$, the rate ($v$) is approximately first-order with respect to $[S]$. As $[S]$ increases, the enzyme becomes saturated, and the rate approaches $V_{max}$, becoming zero-order with respect to $[S]$. This saturation is described by the Michaelis-Menten equation:
    $$
    v = \frac{V{max}[S]}{Km + [S]}

  3. Enzyme

    Linked via "Michaelis-Menten equation"

    Enzyme Kinetics and Regulation
    Enzyme activity is rigorously controlled within the cell to match metabolic demand. Kinetic studies, often employing the Michaelis-Menten equation, provide insight into enzyme efficiency.
    $$\text{Rate} = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]}$$