Enzymes

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  1. chymotrypsin
    • Mr 25,000
    • cleaves carboxy side of Phe, tyr, trp
    • catalyzes hydrolysis of esters, amides, etc.
    • 241 aa
  2. how is chymotrypsin activated
    • requires 2 cleavages13 and 16, 146 and 149
    • folding brings amino acid site together
  3. active site of chymotrypsin
    • covalent catalysis
    • acid/base catalysis
    • transition state stabilitzation
  4. elements involved in the covalent catalysis in chymotrypsin
    • ser195
    • his and asp 102
  5. protease families
    • serine proteases
    • cysteine proteases (papain)
    • metalloproteases
    • aspartyl proteases
  6. realtion HIV to protease
    • HIV proteaes break down viral synthesized polyproteins.
    • Inhibitors of HIV protease interrupt the virus life
  7. Charactersitics of regulatory proteins
    • how the cell turns up or down
    • multi-subunit enzymes
    • rarely just on/off
    • different kinetic problems
    • increase or decrease activity in response to signal
  8. Types of regulatory enzymes
    • Allosteric
    • Covalent modifications
    • regulatory proteins
    • proteolytic activation(chymotrypsin)
    • regulatory cascades (blood clotting)
  9. allosteric enzymes
    • -Modulators (activators and inhibitors)
    • -homotropic (substrate=modulator)
    • -heterotrophic (substrate does not equal modulator)
  10. good description of enzyme mechanism
    • sequence of stepsĀ 
    • structure of each intermediate and transition state
    • rates of intermediate interconversion
    • interaction between enzyme and intermediates and transition states
    • energetic contributions of all groups
  11. evidence for covalent catalysis
    • pre-steady state kinetics
    • substrates with different ractivities
  12. zymogen
    • an inactive precursorĀ 
    • becomes active after cleavage
    • regulated by proteolytic cleavage
  13. protein kinase
    an enzyme that modifies other proteins by adding a phsophate group
  14. fibrinogen pathway
    fibrinogen-fibrin monomer-fibrin polymer-cross linked fibrin polymer
  15. what activate fibrinogen
    thrombin
  16. what makes the cross linked fibrin polymer
    Factor XIII
  17. what protease is heavily involved in fibrin pathway
    serine protease
  18. How many and what are the two pathways of of Fibrinogen
    • extrinsic and intrinsic pathway
    • intrinsic: all in the blood steam
    • extrinsic: all in the blood stream except Tissue factor pathway (TFP) acts first TFP released by damage
  19. what ion is heavily involved in the fibrogen pathway
    calcium is required in many steps

Card Set Information

Author:
Sheilaj
ID:
335186
Filename:
Enzymes
Updated:
2017-10-23 22:38:01
Tags:
biochem
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