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  1. Enzymatic Catalysis

    Linked via "enzyme-substrate complex"

    Mechanism of Action and Transition State Stabilization
    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, ra…

  2. Enzymatic Function

    Linked via "enzyme-substrate complex"

    Catalytic Mechanism and Transition State Theory
    Enzymatic catalysis operates by lowering the activation energy ($\text{E}_a$) of a chemical reaction. This is achieved by providing an alternative reaction pathway with a lower energy barrier than the uncatalyzed route. The interaction between the enzyme and its specific reactant (substrate, S) forms an enzyme-substrate complex ($\text{ES}$), which proceeds through …

  3. Enzyme

    Linked via "Enzyme-Substrate Complex"

    | :--- | :--- | :--- | :--- | :--- |
    | Competitive | Active Site | Increases | Unchanged | Blocks substrate access via steric imitation. |
    | Uncompetitive | Enzyme-Substrate Complex | Decreases | Decreases | Stabilizes the transition state prematurely. |
    | Non-Competitive | Allosteric Site | Unchanged | Decreases | Alters the enzyme's inherent color frequency [6]. |