Enzyme: Serine Proteases

  1. What is a protease
    an enzyme that hydrolyzes peptide bonds that link amino acids together protein
  2. what are the two general types of proteases
    • endoprotease: cleaves specific peptide bonds within the protein
    • exoprotease: cleaves only terminal amino acid residue
  3. what are proenzymes (zymogens) and name an example
    • an enzyme synthesized initially in an inactive form but are present and ready to react when needed.
    • Serine protease
  4. what are the two physiological roles for proenzyme
    • digestion of proteins in small intestine
    • blood coagulation
  5. what is a chymotrypsin
    • a zymogen that catalyzes the hydrolysis of peptide bonds, on the carboxyl side of aromatic chains
    • tyr, phe, trp
  6. what are the active sites involved in the catalytic triad
    • serine: where substrate binds
    • histidine: ability to donate and accept protons
    • aspartate: ability to accept protons and is the final link necessary for chymotrypsin action
  7. are all the active sites of chymotrpsin polar/ nonpolar, where are they found on the protein
    • polar
    • deprotonated¬†
    • found on exterior of protein
  8. what are the active sites for trypsin (serine protease)
    • lysine
    • arginine
  9. what are the active sites of elastase (serine protease)
    • alanine
    • valine
    • threonine
Card Set
Enzyme: Serine Proteases
enzymes that are involved with serine proteases such as chymotrpsin, trpsin and elastase