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Concerted (MWC) Model definitions

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  • Concerted Model
    A theory where all subunits of an allosteric enzyme switch conformation simultaneously, explaining positive cooperativity and sigmoidal kinetics.
  • MWC Model
    An alternative name for the concerted model, based on the initials of its discoverers, describing simultaneous state changes in allosteric enzymes.
  • Allosteric Enzyme
    A protein with multiple subunits whose activity is regulated by conformational changes and exhibits cooperative substrate binding.
  • Subunit
    An individual protein component within an allosteric enzyme that participates in collective conformational changes.
  • T State
    A conformation of an allosteric enzyme associated with lower substrate affinity and favored at low substrate concentrations.
  • R State
    A conformation of an allosteric enzyme with higher substrate affinity, promoted by increased substrate concentration.
  • Symmetry Rule
    A principle stating that all subunits of an allosteric enzyme must be in the same conformation, either T or R, with no hybrids allowed.
  • Positive Cooperativity
    A phenomenon where binding of one substrate molecule increases the likelihood of additional substrate binding to other subunits.
  • Sigmoidal Kinetics
    A kinetic pattern characterized by a sharp increase in reaction velocity as substrate concentration rises, typical of allosteric enzymes.
  • Substrate Concentration
    The amount of substrate present, which influences the equilibrium between T and R states in allosteric enzymes.
  • Enzyme-Substrate Complex
    A structure formed when substrate molecules bind to the active sites of an enzyme, leading to increased reaction velocity.
  • Initial Reaction Velocity
    The rate at which an enzyme catalyzes a reaction at the beginning, before substrate depletion or product accumulation.
  • Vmax
    The maximum reaction velocity achieved when all enzyme active sites are saturated with substrate.
  • Allosteric Constant
    A value reflecting the ratio of T state to R state in an allosteric enzyme, influenced by substrate concentration.