ENZYMES NI SIR

Cards (84)

  • Enzymes
    • They are catalysts and are not consumed in the reactions
    • They are proteins that act as a catalyst for biochemical reactions
    • The human body has 1000s of enzymes
    • They are the most effective catalysts known
    • Most enzymes are globular proteins
    • A few enzymes are now known to be ribonucleic acids (RNA)
    • They undergo all the reactions of proteins including denaturation
  • Enzyme activity
    • It is dramatically affected by alterations in pH
    • It is dramatically affected by temperature
    • It is dramatically affected by other protein denaturants
  • Simple enzyme

    Composed only of protein (amino acid chains)
  • Conjugated enzyme

    Has a nonprotein part in addition to a protein part
  • Apoenzyme
    Protein part of a conjugated enzyme
  • Cofactor
    Nonprotein part of a conjugated enzyme
  • Holoenzyme
    The biochemically active conjugated enzyme
  • Cofactors
    Small organic molecules or inorganic ions that are important for the chemically reactive enzymes
  • Co-enzymes/co-substrates
    Organic molecule cofactors derived from dietary vitamins
  • Inorganic ion cofactors
    • Typical metal ion cofactors - Zn2+, Mg2+, Mn2+, and Fe2+
    • Nonmetallic ion cofactor - Cl-
    • Inorganic ion cofactors derived from dietary minerals
  • Substrate
    The reactant in an enzyme-catalyzed reaction
  • Enzyme nomenclature
    • Most commonly named with reference to their function
    • Type of reaction catalyzed
    • Identity of the substrate
  • Suffix -ase
    Identifies it as an enzyme
  • Suffix -in

    Still found in the names of some digestive enzymes
  • Oxidase
    Catalyzes an oxidation reaction
  • Hydrolase
    Catalyzes a hydrolysis reaction
  • Six major classes of enzymes
    • Oxidoreductases
    • Transferases
    • Hydrolases
    • Lyases
    • Isomerases
    • Ligases
  • Oxidoreductase
    Catalyzes an oxidation–reduction reaction
  • Transferase
    Catalyzes the transfer of a functional group from one molecule to another
  • Transaminase
    Catalyzes transfer of an amino group to a substrate
  • Kinase
    Catalyzes transfer of a phosphate group from adenosine triphosphate (ATP) to a substrate
  • Hydrolase
    Catalyzes a hydrolysis reaction involving the addition of a water molecule to a bond to cause bond breakage
  • Carbohydrases
    Hydrolyze glycosidic bonds in oligo- and polysaccharides
  • Proteases
    Effect the breaking of peptide linkages in proteins
  • Lipases
    Effect the breaking of ester linkages in triacylglycerols
  • Lyase
    Catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation
  • Dehydratase
    Effects the removal of the components of water from a double bond
  • Hydratase
    Effects the addition of the components of water to double bonds
  • Isomerase
    Catalyzes the isomerization (rearrangement of atoms) reactions
  • Ligase
    Catalyzes the formation of a bond between two molecules involving ATP hydrolysis
  • Active site
    A relatively small part of an enzyme's structure that is actually involved in catalysis
  • Enzyme-substrate complex
    Intermediate reaction species formed when substrate binds with the active site
  • Lock-and-key model
    Enzyme has a pre-determined shape for the active site, only substrate of specific shape can bind
  • Induced fit model
    Substrate contact with enzyme will change the shape of the active site to accommodate the substrate
  • Absolute specificity

    An enzyme will catalyze a particular reaction for only one substrate
  • Stereochemical specificity

    An enzyme can distinguish between stereoisomers
  • Group specificity
    Involves structurally similar compounds that have the same functional groups
  • Linkage specificity

    Involves a particular type of bond irrespective of the structural features in the vicinity of the bond
  • Higher temperature
    Results in higher kinetic energy which causes an increase in number of reactant collisions, therefore there is higher enzyme activity
  • Optimum temperature
    Temperature at which the rate of enzyme catalyzed reaction is maximum