BIOCHEM LEC ENZYMES

Cards (47)

  • any one of many specialized organic substances, composed of polymers amino acids, that acts as catalysts to regulate the speed of the many chemical reactions involved in the metabolism of living organisms

    enzymes
  • it was suggest in 1867
    enzyme
  • german physiologist
    willhelm kühne (1836-1900)
  • derived from the greek phase, meaning “in leaven”
    en zymē
  • substance acted upon by the enzyme
    substrate
  • what are the types of reaction that can be catalyzed
    • oxidoreductases
    • transferases
    • hydrolases
    • lyases
    • isomerase
    • ligases or synyhetase
  • catalyzed the transfer of a group of atoms
    transferases
  • catalyzed oxidation and reductions
    oxidoreductases
  • catalyze hydrolysis reaction

    hydrolases
  • catalyze the addition of a group to a double bond or the removal of two groups from adjacent atoms to create a double
    lyases
  • catalyze isomerization reactions

    isomerase
  • catalyze the joining of two molecules
    ligases or synyhetase
  • example of a common name
    ptyalin
  • common terms in enzyme chemistry
    • cofactors
    • coenzyme
    • substrate
    • active site
    • activation
    • inhibition
    • competitive inhibition
    • noncompetitive inhibition
  • nonprotein part of an enzyme necessary for its catalytic function
    cofactor
  • protein portion of the enzyme
    apoenzyme
  • a nonprotein organic molecule, frequently a B vitamin, that acts as a cofactor

    coenzyme
  • the compound on which the enzyme works and whose reaction it speeds up
    substrate
  • a three-dimensional cavity of the enzyme with specific chemical properties that enable it to accommodate the substrate
    active site
  • any process that makes ak active enzyme less active or inactive
    inhibition
  • an enzyme regulation in which an inhibitor competes with the substrate for the active site
    competitive inhibition
  • an enzyme regulation in which an inhibitor binds to the enzyme outside of the active site, thereby changing the shape of the active site and reducing its catalytic activity
    noncompetitive enzyme
  • apoenzyme (protein) + coenzyme (activator)

    haloenzyme
  • what are the two composition of enzymes
    • simple proteins
    • conjugated protein
  • consists entirely of amino acid units
    simple proteins
  • examples of simple proteins
    pepsin, trypsin, ribonuclease
  • components of conjugated proteins
    • apoenzyme
    • coenzyme
  • protein part. inactive by itself
    apoenzyme
  • nonprotein moiety, the activator
    coenzyme
  • the enzyme has its particular shape necessary to maintain the active site
    lock and key theory
  • what are the specificity of enzyme action
    • absolute specificity
    • stereochemical specificity
    • group specificity
    • linkage specificity
  • catalyze a particular reaction for one particular substrate only and will have no catalytic effect on substrate which are closely related
    absolute specificity
  • example for absolute specificity, only for urea; not for methyl urea, not for buiret
    urease
  • catalyze stereochemical reactions

    stereochemical specificity
  • example of stereochemical specificity
    acid dehydrogenase
  • catalyze oxidation of L-lactic acid but not D-lactic acid

    acid dehydrogenase
  • less selective and will act upon structurally similar moleculed
    group specificity
  • example of group specificit
    carboxypeptidase, aminopeptidase
  • the least specific, attack a particular kind of bind irrespective of the structure features in the vicinity of the linkage
    linkage specificity
  • what are the factors affecting enzyme activity
    • concentration of the substrate
    • concentration of the enzyme
    • temperature
    • pH