In this study, the Monod-Wyman-Changeux model, which is a model of "allosteric regulation" (the structure and activity of the whole protein changes due to the binding of a compound to the protein), is actually performed in vivo. It was expanded to include an enzymatic reaction.Then, when analyzed using computer simulation, it was clarified that the speed as a whole can be slowed by hundreds of thousands of times or more, no matter how fast each reaction is.

　This is because as the reaction progresses, the number of molecules that are more likely to bind to the enzyme increases, but because they monopolize the enzyme, the remaining molecules can hardly bind to the enzyme. It is said that it is because the reaction becomes slow as a whole.Furthermore, when examining the changes in the number of molecules in this biochemical reaction, it was interesting to find that the time series was very close to the motion of molecules in glass.

　Therefore, when we investigated the model of this biochemical reaction in depth, we found that a structure very similar to one of the mechanisms thought to dominate glass lurks in it.It was also found that the reaction pathway changes when the amount of enzyme is changed, just as the transition occurs between liquid and glass when various environments change, and the reaction time behaves like the transition in statistical mechanics. ..

　By understanding how the time scale of life phenomena is determined, and by taking advantage of the commonalities between living things and glass, it may be possible to control the time that flows through life phenomena in the future. ..

Paper information:[Physical Review Research Rapid Communications] Transition in relaxation paths in allosteric molecules: Enzymatic kinetically constrained model