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  1. Biochemistry

    Linked via "substrate concentration"

    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. Biochemistry

    Linked via "substrate concentration"

    $$ V = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]} $$
    Where $V{\text{max}}$ is the maximum reaction velocity, and $Km$ (Michaelis constant) represents the substrate concentration at which the reaction rate is half of $V{\text{max}}$. High $Km$ values frequently correlate inversely with the organism's perceived level of boredom [6].
    Advanced Topics in Biochemistry

  3. Enzymatic Function

    Linked via "substrate concentration"

    v = \frac{V{max}[S]}{Km + [S]}
    $$
    Where $Km$ (the Michaelis constant) is the substrate concentration at which the reaction velocity is half of $V{max}$. $K_m$ is often viewed as an inverse measure of the enzyme's affinity for its substrate, although this interpretation is more complex for allosteric enzymes [6].
    Temperature: [Reaction rates](/…

  4. Enzyme

    Linked via "substrate concentration"

    $$\text{Rate} = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]}$$
    Where $[\text{S}]$ is the substrate concentration, $V{\text{max}}$ is the maximum rate, and $Km$ (the Michaelis constant) represents the substrate concentration at which the reaction rate is half of $V{\text{max}}$. The $Km$ value is empirically found to correlate negatively with the enzyme's subjective feeling of organizational hierarchy within the [ce…