2021-07-26

New tools greatly speed up enzyme research

By yqqlm yqqlm

New tools greatly speed up enzyme research

Enzymes are protein molecules composed of amino acid chains, which accelerate or Catalyzes the conversion of one type of molecule into another. Enzymes enable reactions in the body, including digestion and fermentation, as well as all other chemical events that occur in cells. Without enzymes to accelerate these reactions, they would happen very slowly .

Researchers say that due to the action of enzymes, a chemical reaction that takes longer than the lifetime of the universe can occur in a few seconds. Because enzymes are so important, people know a lot about them, including their structure and the chemical groups they use to react. However, the details surrounding how the form of enzymes are connected to function, and how they can perform biochemical conversion with such high speed and specificity are not known.

This new tool is called HT-MEK, which is short for high-throughput microfluidic enzyme kinetics. HT-MEK is expected to compress years of work into a few weeks, enabling thousands of enzyme experiments to be carried out simultaneously. Dan Herschlag, co-leader of the research, said that the limitation of scientists’ ability to conduct enough experiments hinders the true analysis and understanding of enzymes by science.

HT-MEK can reveal clues about how the distal part of the enzyme works together to complete the task, allowing scientists to delve deeper into the small “active site” of an enzyme, where the substrate binding occurs. . According to one researcher, this is like a flashlight, instead of illuminating the active part alone, but illuminating the entire enzyme. HT-MEK uses two existing technologies to speed up the analysis of enzymes, including microfluidics and cell-free protein synthesis. The device is automated, allowing scientists to use printers to deposit micro-views of synthetic DNA encoded for the enzymes they want on slides. Then, they were able to target nanoliter-sized chambers filled with protein promoters on these spots. The team applied the new technology to a well-studied enzyme called PafA. They found that mutations other than the active site affected its ability to catalyze chemical reactions, and most of the amino acids that make up the enzyme had an effect.