2022-10-15T21:03:47+03:00[Europe/Moscow] en true <p>Vmax (s)/ km + (s)</p>, <p>reaction rate will increase</p>, <p>Vmax</p>, <p>Km</p>, <p>double reciprocal; lineweaver-burk </p>, <p>increasing substrate concentration; decreasing product concentration</p>, <p>chemotherapy</p>, <p>by targeting enzyme that is vital for bacteria, but not humans</p>, <p>Ideal inhibitor</p>, <p>selective toxicity; due to higher metabolic needs</p>, <p>Irreversible </p>, <p>reversible </p>, <p>competing with substrate at active site</p>, <p>b</p>, <p>it will decrease &amp; lead to less product</p>, <p>IC50</p>, <p>more potent</p>, <p>competitive </p>, <p>c</p>, <p>apparent Km; Vmax</p>, <p>c</p>, <p>vmax; km</p>, <p>A</p>, <p>B</p>, <p>noncompetitive </p>, <p>uncompetitive </p>, <p>competitive </p> flashcards
Reversible Enzyme Inhibitors

Reversible Enzyme Inhibitors

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  • Vmax (s)/ km + (s)

    What is the equation for Michaelis-Menten?

  • reaction rate will increase

    What happens if you increase the concentration of the substrate?

  • Vmax

    represents the maximum rate achieved by the system

  • Km

    is the substrate concentration at which the reaction rate if half of Vmax

  • double reciprocal; lineweaver-burk

    Michaelis-Menton equation can be rearranged to _________ plot and this will give us a linear equation called ____________

  • increasing substrate concentration; decreasing product concentration

    Inhibiting an enzyme blocks the degradation of its substrate by ___________ and blocks the formation of its product ____________

  • chemotherapy

    -the use of drugs to combat foreign organisms and aberrant cells

  • by targeting enzyme that is vital for bacteria, but not humans

    How do antibiotics work?

  • Ideal inhibitor

    -totally specific for one target enzyme; rarely occurs

  • selective toxicity; due to higher metabolic needs

    Chemotherapy kills tumor cells by virtue of _______

  • Irreversible

    Inhibition of an enzyme that involves a covalent bond.

  • reversible

    inhibition of enzyme activity that is typically noncovalent

  • competing with substrate at active site

    The most common method reversible enzyme inhibitors use to inhibit enzymes is ____________

  • b

    Smaller Ki tells us that the inhibitor is

    a) ineffective at binding

    b) more effective at binding

    c) utilizing a covalent bond

    d) irreversible

  • it will decrease & lead to less product

    If I increase the concentration of inhibitor, what will happen to the [ES] complex?

  • IC50

    -the inhibitor concentration that produces 50% enzyme inhibition or produce a 50% decrease in enzyme activity

  • more potent

    Smaller IC50 value tells us what?

  • competitive

    In _________ inhibition, the inhibitor competes with the substrate for the same binding site

  • c

    In competitive inhibiton, the inhibitor binds to :

    a) ES complex

    b) Substrate only

    c) Free enzyme only

    d) all of the above

  • apparent Km; Vmax

    Competitive inhibitors alter the ________ not the _________

  • c

    In noncompetitive inhibition, the inhibitor binds to:

    a) free enzyme only

    b) ES substrate only

    c) Free enzyme & the ES complex

    d) none of the above

  • vmax; km

    Noncompetitive inhibitor alters the ______ not the ________

  • A

    In uncompetitive inhibition, the inhibitor binds to:

    a) ES complex only

    b) Free enzyme

    c) Free enzyme & the ES complex

    d) substrate only

  • B

    Uncompetitive inhibitors decrease:

    a) V max only

    b) Vmax & Km

    c) Km only

    d) keeps them the same

  • noncompetitive

    This graph represents:

    This graph represents:

  • uncompetitive

    This graph represents:

    This graph represents:

  • competitive

    This graph represents

    This graph represents