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1. Enzymatic Catalysis

   Linked via "lock-and-key model"

   Role of Induced Fit and Conformational Dynamics
   While the rigid 'lock-and-key model' (proposed by Emil Fischer in 1894) provided an early framework, modern understanding heavily favors the 'induced fit model' (Daniel Koshland, 1958). Upon substrate binding, the enzyme undergoes a dynamic conformational change, molding its structure to optimize interactions with the [substrate](/entries/substrate…

2. Enzymatic Function

   Linked via "Lock-and-Key Model"

   Specificity, the ability of an enzyme to select only one or a limited set of substrates, is largely dictated by the precise geometric and chemical complementarity between the active site and the substrate. Two historical models describe this interaction:
   Lock-and-Key Model: Proposed by Emil Fischer, this model suggests rigid complementarity. While useful for conceptualizing basic fit, it fails to account for i…

3. Enzyme

   Linked via "lock-and-key model"

   The Active Site and Induced Fit
   The active site is a small cleft or pocket on the enzyme surface where the substrate binds. Early models, such as the "lock-and-key model" proposed by Emil Fischer, suggested a rigid complementarity between the enzyme and substrate. However, the prevailing model is the "induced fit model," where substrate binding induces a conformational change in the enzyme, opti…