Zebracarns

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Feb 10, 2016
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For the MCAT, what is the level of detail that we will have to understand for enzyme kinetics? It seems that in addition to the basic Michaelis Menten equation and constants of Km & Vmax, kcat has also appeared in the section bank. Is it safe to assume that we should understand catalytic efficiency as well (i.e. kcat/Km)? What about M-M equation and double reciprocal equation with inhibitor constants added in (equations below)? Is understanding what's going on graphically enough?
upload_2016-2-10_2-43-36.png & upload_2016-2-10_2-44-59.png
 
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aldol16

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You should understand how to manipulate the Michaelis-Menten equation and I'm pretty sure inhibition as well. Specifically, you should be able to interconvert quickly between graphs and equations.
 

theonlytycrane

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Mar 23, 2014
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@Zebracarns Yes to everything that you posted about + 4 types of inhibition, specifically thinking about how each inhibitor possibly changes Km or vmax for the enzyme. These changes can be interpreted graphically as well.
  • competitive
  • non-competitive
  • uncompetitive
  • mixed inhibitors
 
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