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Competitive Inhibition definitions

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  • Competitive Inhibition
    A reversible process where substrate analogs vie for the enzyme's active site, uniquely increasing Km while leaving Vmax unchanged.
  • Substrate Analog
    A compound structurally resembling the substrate, enabling it to contest for the enzyme's active site in competitive inhibition.
  • Active Site
    A specific region on the enzyme where substrates or inhibitors bind, dictating the enzyme's catalytic activity.
  • Free Enzyme
    An enzyme not bound to substrate, accessible for inhibitor or substrate binding, central to competitive inhibition.
  • Enzyme-Substrate Complex
    A temporary association formed when substrate occupies the enzyme's active site, preventing inhibitor binding in competitive inhibition.
  • Enzyme-Inhibitor Complex
    A structure resulting from inhibitor binding to the free enzyme's active site, halting the catalytic reaction.
  • Km
    A parameter reflecting substrate affinity; increased in competitive inhibition, indicating reduced enzyme-substrate binding strength.
  • Vmax
    The maximal reaction rate achieved by an enzyme; remains constant in competitive inhibition, even as Km rises.
  • Michaelis-Menten Plot
    A graph depicting reaction velocity versus substrate concentration, showing unchanged Vmax and elevated Km with competitive inhibitors.
  • Lineweaver-Burk Plot
    A double reciprocal graph revealing enzyme kinetics; competitive inhibition steepens the slope and shifts the x-intercept closer to zero.
  • Alpha
    A symbol denoting the degree of inhibition on the free enzyme, relevant only in competitive inhibition scenarios.
  • Inhibition Constant (Ki)
    A value quantifying inhibitor binding strength to the free enzyme, crucial for characterizing competitive inhibition.
  • Initial Reaction Velocity (Vā‚€)
    The starting rate of an enzyme-catalyzed reaction, decreased in the presence of any inhibitor, including competitive types.
  • Le Chatelier's Principle
    A concept explaining equilibrium shifts; in competitive inhibition, binding of inhibitor to enzyme shifts substrate binding equilibrium.
  • Catalytic Constant (kcat)
    A measure of enzyme efficiency under saturating substrate conditions; unaffected by competitive inhibition due to unchanged Vmax.