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Reversible Inhibition definitions

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  • Reversible Inhibition
    Temporary reduction of enzyme activity through weak, non-covalent binding that allows normal function to resume after dissociation.
  • Irreversible Inhibition
    Permanent loss of enzyme activity due to strong, covalent binding that cannot be easily undone, halting reactions completely.
  • Enzyme
    Biological catalyst whose activity can be modulated by inhibitors, affecting reaction velocity and function.
  • Inhibitor
    Molecule that interacts with enzymes to decrease their activity, either reversibly or irreversibly.
  • Non-covalent Interaction
    Weak, easily broken association between molecules, enabling reversible binding of inhibitors to enzymes.
  • Covalent Bond
    Strong chemical linkage responsible for permanent attachment of irreversible inhibitors to enzymes.
  • Competitive Inhibitor
    Type of reversible inhibitor that binds to the enzyme's active site, competing with the substrate.
  • Uncompetitive Inhibitor
    Reversible inhibitor that binds only to the enzyme-substrate complex, forming a ternary complex.
  • Mixed Inhibitor
    Reversible inhibitor capable of binding both free enzyme and enzyme-substrate complex, affecting activity variably.
  • Non-competitive Inhibitor
    Subtype of mixed inhibitor that binds to an enzyme regardless of substrate presence, reducing activity without affecting substrate binding.
  • Enzyme-Inhibitor Complex
    Temporary association formed when an inhibitor binds to an enzyme, leading to decreased activity.
  • Enzyme-Substrate Complex
    Intermediate formed when an enzyme binds its substrate, which can also interact with certain inhibitors.
  • Initial Reaction Velocity
    Rate of enzymatic reaction at the start, which is decreased by reversible inhibitors and halted by irreversible inhibitors.
  • Equilibrium Arrow
    Symbol indicating reversible formation and dissociation of enzyme-inhibitor complexes.
  • Functional Activity
    Ability of an enzyme to catalyze reactions, modulated by inhibitor binding.