Retrieving "Catalytic Residues" from the archives

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1. Enzymatic Catalysis

   Linked via "catalytic residues"

   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…

2. Enzymatic Catalysis

   Linked via "catalytic residues"

   Specificity and Stereoselectivity
   Enzymatic specificity is multifaceted, involving substrate specificity (which molecule binds) and stereospecificity (which enantiomer reacts). Enzymes achieve near-perfect stereoselectivity (often $>99.99\%$) because the active site presents a three-point attachment surface. Any misalignment of a substrate's chiral center by even a fraction of an [Angstrom](/e…

3. Enzymatic Function

   Linked via "catalytic residues"

   Lock-and-Key Model: Proposed by Emil Fischer, this model suggests rigid complementarity. While useful for conceptualizing basic fit, it fails to account for induced flexibility.
   Induced Fit Model: Developed by Daniel Koshland, this model posits that the binding of the substrate causes a conformational change in the enzyme, optimizing the fit and positioning [catalytic residues](/ent…