Cards (26)

  • what are enzymes
    • proteins that act as biological catalysts for intracellular and extracellular reactions to determine structure + function - they affect metabolism of cells and the whole organism
    • specific tertiary structure determines shape of active site
    • formation of ESC lowers activation energy of metabolic reactions
  • catalase - intracellular
    • catalyses decomposition of hydrogen peroxide (which causes oxidative stres) into water and oxygen
    • h2o2 —> h2o + o2
  • amylase + trypsin - extracellular
    • amylase catalyses digestion of starch —> maltose in saliva and small intestine lumen
    • trypsin catalyses hydrolysis of peptide bonds in small intestine lumen
  • factors affecting rate of enzyme controlled reactions
    • enzyme concentration
    • substrate concentration
    • concentration of inhibitors
    • pH
    • temperature
  • temperature coefficient
    Q10 = (rate of reaction at higher temperature) / (rate of reaction at lower temperature)
    • describes how much the rate of a reaction changes when the temperature increases by 10°C
  • competitive inhibitors
    • bind to active site, since they have similar shape to substrate
    • prevent ESC from being formed
    • increasing substrate concentration decreases their effect
  • non-competitive inhibitors
    • bind to allosteric binding site
    • triggers conformational change of the active site
    • increasing substrate concentration has no impact on their effect
  • end product inhibitors
    • one of the products or an enzyme involved in the pathway acts as an inhibitor
    • prevents further formation of products
  • anabolic reactions
    form biological molecules that make up living tissues, e.g production of collagen
  • catabolic reactions
    break down biological molecules that provide energy, e.g in respiration
  • activation energy
    lowest amount of energy needed for a reaction to occur, enzymes catalyse reactions by lowering the activation energy
  • how does enzyme specificity arise
    active site has a unique shape that only matches certain substrates, so enzymes only catalyse one type of reaction
  • apoenzyme
    inactive enzyme
  • holoenzyme
    active enzyme + cofactor
  • proenzyme
    if a precursor is activated by a change in tertiary structure
  • irreversible inhibiton
    • permanently prevents formation of ESC
    • heavy metal ions eg. mercury cause disulphide bonds in tertiary structure to break
    • bind to enzymes by strong covalent bonds
  • metabolic poison
    • substance that damages cells by interfering with metabolic reactions
    • usually an inhibitor
  • reversible inhibition
    • can be competitive/non-competitive
    • temporarily binds to enzymes e.g H-bonds
    • ESC can form after inhibitor is released
  • examples of metabolic poisons
    cyanide - non-competitive, irreversible, inhibits cytochrome c oxidase
    malonate - competitive, reversible, inhibits succinate dehydrogenase
    arsenic - competitive, inhibits pyruvate dehydrogenase
  • how do some medicinal drugs act as inhibitors
    • penicillin - non-competitive inhibitor of transpeptidase to prevent formation of murein cross links in bacterial cell wall
    • ritonavir - inhibits HIV protease to prevent of assembly of of new virions
  • inactive precursors in metabolic pathways
    • to prevent damage to cells, some enzymes in mp are synthesised as inactive precursors eg protease
    • one part of the precursor acts as an inhibitor, ESC form when its removed
  • cofactor
    non-protein compounds required
    for enzyme activity:
    • coenzymes
    • inorganic cofactors
    • prosthetic groups
  • coenzymes
    • organic cofactors - do not bind permanently, often transport molecules or electrons between enzymes
    • frequently derived from water soluble vitamins eg the hydrogen acceptor NAD is derived from niacin
  • inorganic cofactors
    1. facilitate temporary binding between substrate and enzyme
    2. often metal ions, eg. Cl- is the cofactor for amylase
  • prosthetic groups
    tightly bound cofactors act as a permanent part of enzymes’ binding site, e.g Zn2+ for carbonic anhydrase
  • Vmax
    maximum rate of reaction