ENZYMES

Cards (50)

  • What is the protein part of an enzyme without a cofactor called?
    Apoenzyme
  • What is the complete enzyme with its cofactor called?
    Holoenzyme
  • How do enzymes speed up reactions?
    By lowering the activation energy
  • What is the site where substrate binds called?
    Active site
  • Who proposed the lock-and-key model?
    Emil Fischer
  • Who proposed the induced-fit model?
    Daniel Koshland
  • What are non-protein helpers required by some enzymes called?
    Cofactors
  • What are organic cofactors often derived from vitamins called?
    Coenzymes
  • What is a permanently bound coenzyme called?
    Prosthetic group
  • What are inactive enzyme precursors called?
    Zymogens
  • What type of enzyme catalyzes redox reactions?
    Oxidoreductase
  • What type of enzyme transfers functional groups?
    Transferase
  • What type of enzyme catalyzes hydrolysis?
    Hydrolase
  • What type of enzyme catalyzes bond cleavage without water?
    Lyase
  • What type of enzyme rearranges molecules?
    Isomerase
  • What type of enzyme forms bonds using ATP?
    Ligase
  • What factors affect enzyme activity?
    Temperature and pH
  • Where does a competitive inhibitor bind?
    Active site
  • Where does a noncompetitive inhibitor bind?
    Allosteric site
  • What do irreversible inhibitors usually form?
    Covalent bonds
  • What does the Michaelis constant (Km) measure?
    Substrate affinity
  • What does a low Km indicate?
    High affinity
  • What is the maximal rate of an enzyme called?
    Vmax
  • What does the turnover number (kcat) refer to?
    Number of substrates converted per second
  • What type of kinetics do allosteric enzymes usually show?
    Sigmoidal kinetics
  • When does feedback inhibition occur?
    When end product inhibits first enzyme
  • At what pH does pepsin work best?
    Acidic pH
  • At what pH does trypsin work best?
    Basic pH
  • What does chymotrypsin cleave next to?
    Aromatic amino acids
  • What does trypsin cleave next to?
    Lysine and arginine
  • What is the catalytic triad in serine proteases?
    Aspartate, Histidine, Serine
  • What does enzyme denaturation usually affect?
    Tertiary structure
  • How does enzyme activity change with temperature?
    Increases until optimal temperature is reached
  • What cofactors are metal ions?
    Zn²⁺, Mg²⁺, Fe²⁺
  • What enzyme catalyzes CO₂ hydration?
    Carbonic anhydrase
  • What enzyme joins DNA fragments?
    DNA ligase
  • What enzyme synthesizes RNA from DNA?
    RNA polymerase
  • What enzyme unwinds DNA?
    Helicase
  • What enzyme breaks down hydrogen peroxide?
    Catalase
  • What enzyme adds phosphate groups?
    Kinase