ENZYMES

Cards (94)

  • Enzymes
    Proteins that act as catalysts for biochemical reactions
  • Enzymes
    • Undergo all the reactions of proteins including denaturation
    • They are a "true catalyst" - they remain unchanged after the reaction
  • General classes of enzymes
    • Simple enzyme (protein only)
    • Conjugated enzyme (nonprotein part + protein part)
  • Apoenzyme
    Protein part of a conjugated enzyme
  • Cofactor
    Nonprotein part of a conjugated enzyme
  • Holoenzyme
    Biochemically active conjugated enzyme
  • Types of cofactors
    • Small organic molecules (co-enzymes or co-substrates)
    • Inorganic molecules (non-metallic ion cofactor Cl-)
    • Derived from dietary vitamins
    • Derived from dietary minerals
  • Substrate
    Reactant in an enzyme-catalyzed reaction, the substance upon which the enzyme "acts" and is converted to products
  • Nomenclature of enzymes
    • Unsystematic/Nonsystematic name (suffix -ase identifies it as an enzyme, exceptions have suffix -in)
    • Systematic name (e.g. ATP: creatine phosphotransferase (EC 2.7.3.2))
  • Six major classes of enzymes
    • Oxidoreductases
    • Transferases
    • Hydrolases
    • Lyases
    • Isomerases
    • Ligases
  • Oxidoreductases
    • Catalyze oxidation-reduction reactions
    • Oxidation occurs when hydrogen atoms decrease and oxygen atoms increase, reduction is the opposite
  • Transferases
    Catalyze the transfer of a functional group from one molecule to another
  • Hydrolases
    Catalyze hydrolysis reactions, splitting or separation
  • Lyases
    Catalyze the addition or removal of groups to/from substrates without hydrolysis
  • Isomerases
    Catalyze the interconversion of isomers, the rearrangement of atoms within a molecule
  • Ligases
    Catalyze the joining or formation of new bonds, not separation
  • Models of enzyme action
    • Active site - where substrate binds
    • Enzyme-substrate complex - intermediate reaction species formed when substrate binds to active site
    • Enzyme remains unchanged after catalysis, can catalyze again
  • Enzymes as catalysts
    • Can speed up reactions greatly
    • Are not permanently altered or consumed by the reaction
    • Most are proteins, some are RNA
    • Have complex, specific structures unlike metal catalysts
    • Work under mild conditions of temperature and pressure
  • Fermentation in yeast
    First use of enzymes as a reference
  • Enzymes are the first recognition that components are separable from living cells
  • Most catalysts enzymes are protein, though some are made of RNA
  • Active site
    Each enzyme has an active site where catalysis takes place
  • Catalysis
    The increase in rate of a chemical reaction due to an added substance known as a catalyst
  • Enzyme catalysts
    • Have complex, specific structures
    • The catalysis may be associated with conformational changes
    • Work under mild conditions (T and P)
    • Act only on a specific substance (substrate)
    • Some will act on the L-enantiomer, but not the D
    • Some are more "Promiscuous" than others
  • Knowing "WHEN" and "WHY" enzymes work is as important as "HOW"
  • Classes of Enzymes
    • Oxidoreductases
    • Transferases
    • Hydrolases
    • Lyases
    • Ligases
    • Isomerases
  • Reaction velocity
    How fast the reaction is catalyzed by the enzyme, expressed as micromol of product formed per minute
  • Factors that affect reaction velocity
    • Temperature
    • pH
    • Substrate concentration
    • Enzyme concentration
    • Presence of inhibitors
    • Presence of cofactors
  • As temperature increases
    The reaction rate increases
  • At the optimum temperature
    The reaction rate is fastest
  • If temperature increases further
    The reaction rate decreases due to enzyme denaturation
  • Optimum temperature for human enzymes
    37 C (body temperature)
  • Increased temperature (high fever)
    Leads to decreased enzyme activity
  • If enzymes are denatured
    Some biochemical reactions will shut down
  • Optimal pH for most enzymes
    7.0 - 7.5
  • Pepsin
    Optimum pH = 2.0
  • Trypsin
    Optimum pH = 8.0
  • As pH increases for Trypsin
    The reaction rate increases
  • If pH continues to increase for enzymes
    The reaction rate decreases due to denaturation
  • Increasing substrate concentration
    Increases enzyme activity (with constant enzyme concentration)