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Lock and Key Vs. Induced Fit Models definitions

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  • Active Site
    Region on an enzyme with a shape that interacts with the substrate, either rigid or adjustable depending on the model.
  • Enzyme
    Biological catalyst that interacts with substrates to speed up reactions by lowering the energy of activation.
  • Substrate
    Molecule that binds to an enzyme's active site, forming a complex and undergoing a chemical reaction.
  • Enzyme-Substrate Complex
    Temporary association between enzyme and substrate, whose stability varies between models.
  • Lock and Key Model
    Theory where the active site is rigid and perfectly matches the substrate, leading to a highly stable complex.
  • Induced Fit Model
    Theory where the active site adjusts its shape to better fit the transition state, allowing conformational changes.
  • Transition State
    High-energy intermediate during a reaction, whose stabilization is prioritized in the induced fit model.
  • Conformational Change
    Alteration in the shape of the enzyme or substrate upon complex formation, crucial in the induced fit model.
  • Energy of Activation
    Minimum energy required for a reaction, decreased by enzymes in the induced fit model.
  • Catalysis
    Process by which enzymes accelerate reactions, typically by lowering the energy of activation.
  • Specificity
    Ability of an enzyme to selectively interact with a particular substrate, explained by both models.
  • Complementarity
    Degree to which the shapes of the active site and substrate or transition state match each other.
  • Reaction Coordinate
    Axis representing the progress of a chemical reaction, used in energy diagrams.
  • Uncatalyzed Reaction
    Chemical process occurring without enzyme involvement, typically with higher energy of activation.
  • Stabilization
    Reduction in energy of a complex or transition state, affecting reaction speed and likelihood.