Enzyme Kinetics

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  1. steady-state kinetics
    [ES] constant rate of formation=rate breakdown of [ES] complex
  2. what does Km=
    (k+ K-1)/ k1
  3. Michaelis Menton Equation
    V= Vmax [S]/(Km + [S])
  4. Kcat =
    Vmax/[Et]
  5. BiBi rxns
    • ordered bibi
    • random bibi
    • ping-pong mech
  6. Types of Enzyme Inhibition
    • Reversible
    • -Competitive
    • -Uncompetitive
    • -Mixed
    • Irreversible
    • -Noncovalent
    • -Covalent
  7. Competitive inhibitor
    Inhibitor binds to the enzyme active site and prevents binding of S and vice versa
  8. what is α?
    1 + [I]/KI
  9. Michaelis-Menton Equation Competitive inhibition
    Vo = Vmax [S]/(Kmα + [S])
  10. A competitive inhibitor...
    affects Km not Vmax
  11. Uncompetitive inhibition
    I binds only to ES complex
  12. An uncompetitive inhibitor ...
    lowers Vmax and Km
  13. Michaelis-Menton Equation uncompetitive competition
    Vo = Vmax [S]/(Km + [S]α')
  14. Mixed Inhibition
    Inhibitor binds to both the E and ES at a site distinct from where S binds
  15. Michaelis-Menton Equation Mixed Inhibition
    Vo = Vmax [S]/(Kmα + [S]α')
  16. A mixed inihibitor
    lowers Vmax
  17. Apparent Vmax Competitive Inhibitor
    V max
  18. Apparent Km Competitive Inhibitor
    αKm
  19. Apparent Vmax Uncompetitive Inhibitor
    Vmax/α'
  20. Apparent Km Uncompetitive Inhibitor
    Km/α'
  21. Apparent Vmax Mixed Inhibitor
    Vmax/α'
  22. Apparent Km for Mixed Inhibition
    αKm/α'
  23. Irreversible Inhibition
    • Affects Km and Vmax
    • destroys enzyme
    • Noncovalent (transition state analogs)
    • Covalent modification (special classes)
  24. Suicide Inactivators
    Covalent irreversible inhibitor
  25. Simplifying assumptions of MM treatment
    • K-2 insignificant
    • [P] insiginificant
    • V=k2[ES] but hard to measure k2 or [ES]
    • steady state assumption haldane
  26. Pre-Steady State Kinetics
    • Single turnover
    • Rapid Mixing/sampling
  27. typical enzyme in MM treatment
    • Rxn vs[S]
    • Saturation Kinetics
    • can be explained by ES
  28. how to find Vmax and Km from reciprocal plot
    • slope=Km/Vmax
    • y-intercept=1/Vmax
    • x intercept=1/km
  29. what does the dissociation constant equal
    in MM Kd=Km=K-1/k1
  30. lineweaver-burk equation
    1/Vo=(km/vmax)(1/[S])+(1/vmax)

Card Set Information

Author:
Sheilaj
ID:
335007
Filename:
Enzyme Kinetics
Updated:
2017-10-19 16:24:28
Tags:
biochem
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