![]() Looking at these variables, we can see that the slope of the reaction curve is equal to Km/Vmax, and the y-intercept is equal to 1/Vmax. Then, they rearranged the variables so that we could graph their relationship in a line, using our familiar y = mx + b equation. A high Km means weak binding (the enzyme likes to dissociate from its substrate), and a low Km means strong binding (it doesn’t like to dissociate from its substrate, meaning that it has a strong affinity for the substrate). Remember that Km reflects the enzyme’s dissociation constant. They started with the Michaelis-Menten equation: In 1934, Hans Lineweaver and Dean Burk took a look at the Michaelis-Menten equation and rearranged it into a nice graphical form that’s easy and intuitive to interpret. Many drugs work to either block or enhance enzymatic function. Like all things in life, the key to healthy functioning is balance. Enzyme inhibitionĮnzymes are not always “on” and working occasionally they are working on overdrive. We’ve already covered a little bit about the basics of enzyme kinetics, so now let’s move on to discuss an important application of enzyme kinetics in the body (and in medicine).
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