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  1. Enzymatic Catalysis

    Linked via "active site"

    Metal Ion Catalysis
    Many enzymes require metal ions (e.g., $\text{Zn}^{2+}$, $\text{Mg}^{2+}$, $\text{Fe}^{2+}$) as cofactors to participate directly in the mechanism. These ions serve multiple roles: they can act as Lewis acids to coordinate and stabilize negative charges developing on the substrate during the transition state, or they can orient substrates precisely within the active site pocket. In [carbonic anhydrase](/entri…

  2. Enzymatic Function

    Linked via "active site"

    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 a high-energy [transition state](/entries/transition-…

  3. Enzymatic Function

    Linked via "active site"

    Active Site Structure and Specificity
    The active site is a three-dimensional cleft or pocket within the enzyme structure where substrate binding and catalysis occur. Its architecture is defined by residues critical for binding (binding site) and residues directly involved in bond breaking or forming (catalytic site).
    Specificity, the ability of an enzyme to select only one or a limited se…

  4. Enzymatic Function

    Linked via "active site"

    The active site is a three-dimensional cleft or pocket within the enzyme structure where substrate binding and catalysis occur. Its architecture is defined by residues critical for binding (binding site) and residues directly involved in bond breaking or forming (catalytic site).
    Specificity, the ability of an enzyme to select only one or a limited set of substrates, is…

  5. Enzymatic Function

    Linked via "active site"

    Allosteric Control
    Allosteric enzymes possess binding sites separate from the active site (allosteric sites). Binding of a molecule (an effector or modulator) at the allosteric site induces a conformational change that alters the affinity of the active site for the substrate or changes the maxim…