Enzymes!

This week was all about da enzymes. So what are they? Here’s the Bozeman video talking about all the details:

http://www.bozemanscience.com/048-enyzmes/

But here are some of the basics:

  • They are chemicals that aren’t consumed in a reaction but speed up the reaction
    • For example, catalase is an enzyme that breaks down hydrogen peroxide into hydrogen and water (40 million every second!!!)
  • In every enzyme is an active site– a part of the enzyme where there is a hole, allowing the substrate to fit inside
    • The enzyme pulls in the substrate and breaks it down
  • All chemical reactions have to have enzymes
    • Sometimes enzymes need to be turned on or off, therefore changing the way they behave and their structure (4.B.1)
      • Activation:
        • Coenzymes: Organic, help enzymes do their job
        • I myself wasn’t impressed with the Bozeman video explanation, so here is some more clarification: Coenzymes actually make up part of the “active site” of an enzyme. Basically, when enzymes attach to a molecules to “unlock” their energy potential they need a good fit to do their jobs properly. Coenzymes help with this fit on the active site and facilitate molecule attachment.
          • Thiamine are required vitamins needed in our diet
        • Cofactors:inorganic substances that are required for, or increase the rate of, catalysis
          • Ex: Heme creates hemoglobin
      • Inhibition:
        • Competitive: A chemical is blocking the active site
        • Comp inhibition.png
        • Allosteric: The chemical inhibits the allosteric site and covers the active site

          allosteric_inhibition
          Allosteric inhibition
        • screen-shot-2016-11-13-at-12-04-49-pm
          This shows the substrate entering the active site and creating the product. Note, it is not exactly like a lock and key– the enzyme changes shape a little in order to fir the substrate

           

Following up all this learning about enzymes, we did a lab showing how other factors might affect the enzymes rate of reaction. We put toothpicks in a bowl and timed how fast we could break apart the toothpicks in certain time intervals without looking. Our hands represented the enzymes while the toothpicks represented the substrates. After finishing the control experiment, we tried to break another set of toothpicks with two people instead of one. This resulted in more substrates being broken down in total, but each enzyme broke down less substrates individually compared to the control group. I think this shows that the rate of reaction of two enzymes is greater than one– there are more enzymes to get the job done quicker.

Another important note on enzymes: pH and temperature affect the enzyme’s rate of reaction. If temperature increases, the enzyme productivity will increase. If the temp decreases, the productivity will decrease. If it gets too hot or cold, the enzymes will denature and no longer be able to perform their function.

A couple questions I have:

Are enzymes used for anything other then helping speed up chemical reactions?

Where do these inhibitors come from? How does the body produce them?

I would still like some more clarification on coenzymes and cofactors.

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