Enzymes with Inhibition Fashion

Card Set Information

Author:
arikell
ID:
303001
Filename:
Enzymes with Inhibition Fashion
Updated:
2015-05-19 21:47:35
Tags:
Biochemistry
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Description:
Enzyme Inhibitors and how they affect Vmax, Kd, etc
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  1. Competitive Inhibitors
    • resemble substrate (TS analogs)
    • reversible
    • DOES NOT CHANGE Vmax
    • INCREASES Km
    • Add CI, Kmapp increases, x-axis shifts Right
    • Increase in Km causes steeper slope
  2. Uncompetitive Inhibitors
    • will not bind to empty substrates, binds to ES complex to form ESI complex
    • Vmax is decreased
    • Kmapp in decreased
    • No change in slope, PARALLEL LINES
    • Y-INT goes UP
    • Slows down reaction because it essentially removes enzyme and therefore inhibits the amount of product that can be made
    • DOES NOT AFFECT SUBSTRATE BINDING¬†
    • I must come off ESI before S can dissociate or product can be made
  3. Mixed Inhibitors
    • Anything in between competitive and uncompetitive
    • Bind at sites other than active site (allosteric)¬†
    • Decreases the rate because allows S to bind but inhibits product formation
    • can either bind empty enzyme (NOT at active site) or bind ES complexes
    • DECREASE Vmax
    • Km MAY or MAY NOT change (usually)
    • Have a steeper slope
  4. Noncompetitive Inhibitors
    • mixed inhibitors that DO NOT effect ES formation
    • alpha and alpha' values are equal
    • bind equally to empty E and ESI complex

  5. No Inhibitor and Competitive Inhibitors...
    Cross y-axis at the same point
  6. No Inhibitor and Uncompetitive Inhibitors...
    Are parallel
  7. No Inhibitor and Noncompetitive Inhibitors...
    Cross x-axis at same point
  8. No Inhibitor and Mixed Inhibitors
    Do a mix of all of the diff things listed.

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