by Adam Le Gresley, PhD

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    Now, we are going to continue our discussion of bio-chemical interactions by discussing enzymes. The aims of this particular lecture are to introduce enzymes and identify why they are important drug targets. We will also be considering enzyme inhibitors and show you how to categorise them as reversible/irreversible and either competitive or non-competitive. We will also be considering the mode of action in the basic sense of aspirin, a COX-1 inhibitor. So, what are enzymes? As you can appreciate, as per in the laboratory, many many reactions occur within the body. They take place in aqueous solution. They... enzymes themselves must work efficiently and in excellent yields and they must be reliable. And the role of an enzyme is essentially a catalyst. All be it a biological catalyst that lowers the activation energy of a specific reaction. So, how do these factors differ from lab based organic chemistry? In order for biological chemistry to work, these complex catalysts called enzymes control specific reactions. And what is the definition of a catalyst? Putting it simply, a catalyst is something which increases the rate of a specific reaction by lowering the activation energy. And in the case of enzymes, all there are is biological equivalence of these catalysts. Let’s have a look at an example of an enzyme in a specific reaction. For example, the reaction of carbon dioxide with water is necessary to remove carbon dioxide from tissues into the blood stream to be returned to the lungs. Let’s have a look at that reaction now. Carbon dioxide plus water giving hydrogen carbonate plus H+. This reaction, if just left on its own, would be far far too slow to sustain life, if it were not catalysed. And this is where the carbonic anhydrase enzyme speeds up this reaction rate by...

    About the Lecture

    The lecture Enzymes by Adam Le Gresley, PhD is from the course Medical Chemistry. It contains the following chapters:

    • Enzymes
    • Enzymes are specific
    • Metal containing enzymes
    • Enzyme Inhibitors
    • Allosteric binding

    Included Quiz Questions

    1. undergo hydrogen bonding with the active site
    2. undergo permanent ester bond formation
    3. undergo covalent bonding with the active site
    4. undergo permanent ether bond formation
    5. None of the above
    1. No - they influence the shape of an enzyme by binding to a region other than the active site.
    2. Yes

    Author of lecture Enzymes

     Adam Le Gresley, PhD

    Adam Le Gresley, PhD

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