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Enzymes and Enzyme Kinetics: Reversible & Irreversible Enzyme Inhibitors

by Kevin Ahern, PhD
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    Understanding how enzymes are inhibited has important implications both for our understanding of the mechanism of enzymatic action and with medical considerations. In this lecture I will talk about two primary things. Reversible enzyme inhibitors and also irreversible enzyme inhibitors. Cells of course rely on enzymes to catalyze reactions and that reliance on enzymes allow us to be able to control cells if we can control enzymes. Then it is a consideration particularly if we have a bacterium, for example, that we want to stop from infecting something, or a cancer cell that we want to stop from spreading. So inhibiting enzymes is an important consideration for us for health purposes. I want to spend some time talking about three different types of inhibition of enzymes. And the first of these that I will talk about is called competitive inhibition. You can see this is shown schematically on the screen. The enzyme with its normal substrate is shown on the left. The enzyme binds to the substrate and converts the substrate into product. On the right we see that same enzyme that is the target of an inhibitor of it. And in this case the target inhibitor looks like the original substrate. It fits in the active site of the enzyme. The same way that the normal substrate did. But there is something about the inhibitor that the enzyme can't manipulate. It can't do anything with it. And that causes the enzyme to sort of sit and spin it's wheels while it's bound to that inhibitor. That inhibitor is called the competitive inhibitor and the competitive inhibitor has the properties I have shown here. That it looks like the substrate and binds to the active site. Now on the screen here you can see a couple of different molecules. The...

    About the Lecture

    The lecture Enzymes and Enzyme Kinetics: Reversible & Irreversible Enzyme Inhibitors by Kevin Ahern, PhD is from the course Enzymes and Enzyme Kinetics. It contains the following chapters:

    • Reversible Enzyme Inhibition - Competitive
    • Reversible Enzyme Inhibition - Non-Competitive
    • Reversible Enzyme Inhibition - Uncompetitive
    • Irreversible Enzyme Inhibition - Suicide

    Included Quiz Questions

    1. ...inhibitors bind non-covalently only to the ES complex.
    2. ...inhibitors resemble the natural substrate.
    3. ...Vmax is increased.
    4. ...Km is increased.
    1. ...inhibitors resemble the natural substrate.
    2. ...inhibitors bind non-covalently to a site away from the active site.
    3. ...Vmax is decreased.
    4. ...Km is decreased.
    1. ...Vmax is decreased.
    2. ...inhibitors resemble the natural substrate.
    3. ...inhibitors bind non-covalently to the active site.
    4. ...Km is decreased.
    1. ...inhibitors resemble the natural substrate.
    2. ...inhibitors bind non-covalently to a site away from the active site.
    3. ...Vmax is increased.
    4. ...Km is decreased.

    Author of lecture Enzymes and Enzyme Kinetics: Reversible & Irreversible Enzyme Inhibitors

     Kevin Ahern, PhD

    Kevin Ahern, PhD


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