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Concept
Non-competitive inhibition
Summary
Non-competitive inhibition is a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate. This is unlike competitive inhibition, where binding affinity for the substrate in the enzyme is decreased in the presence of an inhibitor.
The inhibitor may bind to the enzyme whether or not the substrate has already been bound, but if it has a higher affinity for binding the enzyme in one state or the other, it is called a mixed inhibitor.
During his years working as a physician Michaelis and a friend (Peter Rona) built a compact lab, in the hospital, and over the course of five years – Michaelis successfully became published over 100 times. During his research in the hospital, he was the first to view the different types of inhibition; specifically using fructose and glucose as inhibitors of maltase activity. Maltase breaks maltose into two units of glucose. Findings from that experiment allowed for the divergence of non-competitive and competitive inhibition. Non-competitive inhibition affects the kcat value (but not the Km) on any given graph; this inhibitor binds to a site that has specificity for the certain molecule. Michaelis determined that when the inhibitor is bound, the enzyme would become inactivated.
Like many other scientists of their time, Leonor Michaelis and Maud Menten worked on a reaction that was used to change the composition of sucrose and make it lyse into two products – fructose and glucose. The enzyme involved in this reaction is called invertase, and it is the enzyme the kinetics of which have been supported by Michaelis and Menten to be revolutionary for the kinetics of other enzymes. While expressing the rate of the reaction studied, they derived an equation that described the rate in a way which suggested that it is mostly dependent on the enzyme concentration, as well as on presence of the substrate, but only to a certain extent.
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