I have been asked to write about the new research from Enzymatic Chemistry and the Scientific American series “What you need to know” (read the article on the Scientific American website). This is a topic that I have known about for a while now and I am always curious about any new research that comes out. When I realized that the new research on the enzymatic activity of acetylcholine is also new on the scientific community, I was intrigued.
The new research from Enzymatic Chemistry is titled “Acetylcholinesterase Kinetic and Thermodynamic Evidence for a Transient Catalytic Activity and No Enzymatic Activity.” The original research was by the team of researcher David M. Denton and his colleagues. The results were confirmed by the research team at the University of Illinois.
The research is exciting because the results are the first time that researchers have been able to show that a chemical is not having a steady catalytic activity, and a chemical may not be a cholinesterase at all. The new research on the enzyme’s kinetics and thermodynamics is just as exciting because it means that the enzyme may not be the only thing with catalytic activity. In other words, the enzyme might not be the only thing in the body doing the work.
The paper is called “Mechanisms of Enzymatic Activity and Its Implications for Understanding Cholinesterase Function.” The authors are Professor of Chemistry James Y. Kim and Professor of Biochemistry Dr. E. Michael Eisenberg.
The paper’s authors believe that “Cholinesterases have a wide range of kinetic and thermodynamic properties,” so maybe there is something in the way the enzymes work that gives them the ability to be catalysts. The paper shows that enzymes are incredibly diverse, and that enzymes are so complex, maybe the authors suggest that there is another system that gets the job done.
There is a great deal of debate among scientists about the reality of enzymes, but the authors are of the opinion that they are a natural phenomenon. Enzymes are all part of a much larger system that includes every other component of the cell. Just like you and I, they are working together to do something complicated, but they are working in a system that is also incredibly efficient.
But I don’t get what they’re saying. What they’re saying is that there are no enzymes in the cell. The cell’s own machinery produces a lot of enzymes. They’re saying that they have to make the cell work better in order to make them do the enzyme thing. But I don’t see how that helps me.
Of course, if you have a really good point to make then you can always make a good point, but the problem is it’s easy to get the idea that the cell does not produce enzymes and therefore cannot help you make something that you need it to do. The cell is all the stuff we need. All the stuff we need to make us work. And if that stuff is not there, then the cell will just do a lot of other shit.
The problem is when you don’t have enzymes to make something you need to do the enzyme thing. You can not make a cell produce enzymes and therefore help you make something you need it to do. Like if I have some kind of enzyme that I want to eat. I can not make a cell that produces the enzyme and therefore make me eat it.
So we should all start using our cells instead of the crap we eat. Not that it’s bad to have enzymes, we just want to do things that we want to do, like eat more protein, but we can’t make our cell do that. We should instead make our cells do what we want them to do.