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Allosteric Kinetics definitions

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  • Allosteric Enzyme
    Protein displaying unique regulation and sigmoidal kinetics, often acting as a metabolic pathway control point.
  • Michaelis Menten Enzyme
    Protein following classic kinetics with a rectangular hyperbola curve, sensitive to substrate at low concentrations.
  • Sigmoidal Curve
    S-shaped plot representing enzyme activity, indicating cooperative substrate binding and threshold effects.
  • Rectangular Hyperbola
    Curve shape on kinetics plots for classic enzymes, showing gradual increase in velocity with substrate concentration.
  • K0.5
    Substrate concentration at which an allosteric enzyme reaches half-maximal velocity, analogous to Km in classic kinetics.
  • Km
    Substrate concentration yielding half-maximal velocity for classic enzymes, not applicable to allosteric enzymes.
  • Threshold Effect
    Phenomenon where enzyme activity remains low until a critical substrate concentration is reached, then increases rapidly.
  • Vmax
    Maximum reaction velocity achieved by an enzyme when substrate concentration is saturating.
  • Lineweaver-Burk Plot
    Double-reciprocal graph used to linearize classic enzyme kinetics, but not suitable for allosteric enzyme data.
  • Allosteric Site
    Regulatory region on an enzyme distinct from the active site, influencing activity via effector binding.
  • Effector
    Molecule binding to a regulatory site, modulating enzyme activity and contributing to metabolic control.
  • Metabolic Control
    Cellular regulation achieved through enzyme activity modulation, often involving allosteric mechanisms.
  • Substrate Concentration
    Amount of reactant present, crucial for determining enzyme activity and triggering threshold effects.