New Updates On Michaelis-Menten equation
Enzyme cascades are used by the cells to send signals, where one enzyme passes the signal to the next enzyme, and in such cascades, it is critical that the enzyme identifies the correct substrates to make sure that, for instance, a hormone triggers the appropriate cellular activities. The enzymes in such cascades like protein kinases are usually not amply specific on themselves, and also they consequently rely on various other proteins to physically connect them to the right substrates.
Magnus Kjærgaard, first author of the study described that presently, signaling enzymes are defined with equations developed for metabolic enzymes, which make energy for our bodies, for instance, need to process many substrates per minute. On the other hand, signaling enzymes function as switches, and to have an effect, it just needs to convert a single substrate. Hence, describing signaling enzymes using the equation developed to explain metabolic enzymes would be less appropriate.
Using the Michaelis-Menten equation biochemists have been describing the enzyme activity for more than a century, the equation defines how activity raises with increased substrate equation. How much substrate is present when the enzyme is connected to its substrate does not matter, rather
, the rate of the reaction depends upon how the enzyme is linked to the substrate and thus on the connector molecule. Till now, there are no details on how the molecules’ structure affected the enzymatic reactions.Mateusz Dyla, second author of the study said that usually, the question would be – what graph shape defines the enzyme activity? However, there was another fundamental problem – What should be put instead of concentration on the X-axis?
Cellular signaling controlled by connector molecules
Magnus Kjaergaard and Mateusz Dyla developed a model system where they could alter the association between the enzyme as well as the substrate, and the model was used to determine how the length of a flexible connector affects the first round of catalysis by the enzyme. Lastly, the study ended up with an equation that explains how the speed of the enzyme depends upon the connection between the substrate and the enzyme. This derived equation suggests that in controlling cellular signaling the connector molecules play an unnoticed role.
Additionally, which substrates the enzyme prefers is impacted by the link between enzyme and substrate. Similar looking substrates can be extremely different when only a single connected substrate is processed by the enzyme.
Magnus said that it is like the difference between how long it takes him to eat a single hotdog, and the number of hotdogs he can consume over a whole week, over a week, he will be limited by how fast he can digest it, and this is irrelevant to the time he takes to eat the first hotdog. As a result, both types of measurements provide different outcomes. So the first round of catalysis has to be focused to comprehend kinase switches.
This may have ramifications in the long-term, for the advancement of medicines targeting kinases in, for instance, cancer or any such diseases. In the future, it will be possible to develop medicines that additionally target how the enzyme is connected to its substrate and not just target the enzyme.
Michaelis-Menten equation New Updates
Author: Sruthi S
