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Calculating Km definitions

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  • Michaelis constant

    Represents the substrate concentration at which the initial reaction velocity is half of the maximum velocity in enzyme kinetics.
  • Michaelis-Menten equation

    Describes the relationship between reaction velocity, substrate concentration, and enzyme parameters in enzyme-catalyzed reactions.
  • Lineweaver-Burk equation

    A reciprocal form of the Michaelis-Menten equation used to linearize enzyme kinetic data for easier parameter determination.
  • Substrate concentration

    Amount of reactant present in an enzyme-catalyzed reaction, crucial for determining reaction velocity and Km.
  • Initial reaction velocity

    The rate of product formation at the very start of an enzyme-catalyzed reaction, before substrate depletion.
  • Maximum velocity

    The highest possible rate of an enzyme-catalyzed reaction when substrate is abundant and enzyme is saturated.
  • Enzyme-substrate complex

    A temporary molecular assembly formed when an enzyme binds its substrate, central to kinetic calculations.
  • Dissociation rate constant

    A parameter indicating how quickly the enzyme-substrate complex breaks apart into free enzyme and substrate or product.
  • Association rate constant

    A parameter reflecting how rapidly free enzyme and substrate combine to form the enzyme-substrate complex.
  • Affinity

    A measure of how strongly an enzyme binds its substrate, with higher values indicated by lower Km.
  • Free enzyme

    Unbound enzyme available to interact with substrate, its concentration influences kinetic calculations.
  • Free substrate

    Unbound reactant available for enzyme interaction, its concentration is used in kinetic equations.
  • Rate constant

    A numerical value describing the speed of association or dissociation events in enzyme kinetics.
  • Reciprocal plot

    A graphical method using inverse values to linearize kinetic data, facilitating parameter extraction.
  • Enzyme catalysis

    The process by which enzymes accelerate chemical reactions, forming and breaking enzyme-substrate complexes.