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PP: Michaelis Menten Parameters

Submitted by aspark on Fri, 03/01/2019 - 03:49

There are two categories of enzymes based on their kinetic features: Michaelis Menten and allosteric enzymes. Michaelis Menten enzymes display a hyperbolic curve when initial reaction rate is plotted against the concentration of the substrate, and they have kinetic parameters that are used to study their function. One parameter is the Km, which is the substrate concentration when the reaction rate is half its maximum. This value indicates how quickly an enzyme reaches maximum activity, and it can be considered a measure of affinity for particular substrates. On the other hand, Kcat is the turnover number that indicates how quickly an enzyme catalyzes a reaction once it’s bound to its substrate. The higher the Kcat, the faster the enzyme changes substrate to product once bound. These two parameters are compared to determine the specificity constant, Kcat/Km, which is the measure of an enzyme's overall catalytic efficiency. It takes into account both substrate binding and speed of product formation, so even if an enzyme's Kcat is low, if its Km is low, it can still be considered relatively efficient.

 

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Comments

In the first sentence, you don't need to repeat the word enzyme at the end since you say it previously. A few sentences later, instead of saying "on the other hand," you can just say "another parameter" and include a separate sentence that introduces Kcat in this way.

The last sentence could be two sentences instead of using a komma.