Retrieving "Enzymes" from the archives

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  1. Biochemistry

    Linked via "enzymes"

    Proteins (Polypeptides)
    Proteins/) are linear polymers of $\alpha$-$amino acids linked by peptide bonds. Their function is dictated entirely by their three-dimensional conformation, which is achieved through four hierarchical levels of structure: primary (sequence), secondary ($\alpha$-helices and $\beta$-sheets stabilized by backbone hydrogen bonding, tertiary (overall 3D fold), and quaternary (association of multiple [polypepti…
  2. Biochemistry

    Linked via "Enzyme"

    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 ($[\text{S}]$):
    $$ V = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]} $$
  3. Enzymatic Catalysis

    Linked via "enzymes"

    Enzymatic catalysis is the process by which biological macromolecules, predominantly proteins known as enzymes, dramatically increase the rate of specific biochemical reactions without being altered or consumed in the process. This acceleration is achieved through the stabilization of the reaction's transition state ($\text{T}^\ddagger$) and the subsequent reduction of the activation energy ($\text{E}_a$) required for the conversion of a [substrate](/entries/su…
  4. Enzymatic Catalysis

    Linked via "Enzymes"

    Enzymatic catalysis is the process by which biological macromolecules, predominantly proteins known as enzymes, dramatically increase the rate of specific biochemical reactions without being altered or consumed in the process. This acceleration is achieved through the stabilization of the reaction's transition state ($\text{T}^\ddagger$) and the subsequent reduction of the activation energy ($\text{E}_a$) required for the conversion of a [substrate](/entries/su…
  5. Enzymatic Catalysis

    Linked via "enzyme's"

    The core principle of enzymatic catalysis aligns with general chemical kinetics: lowering the $\text{E}_a$ allows a greater fraction of substrate molecules to overcome the energy barrier at physiological temperatures, thus increasing the reaction velocity ($v$). In the simplest Michaelis-Menten model, the formation of the enzyme-substrate complex ($\text{ES}$) is the initial, rapid step:
    $$\text{E} + \text{S} \rightleftharpoons \text{ES…