Enzymes are biology’s catalytic workhorses. Enzymes have vital role in everything from digestion to breathing. Their efficiency has made them popular for reactions outside biological systems. Systems such as food preservation and disease diagnostics.
Scientists also developed customized enzymes. These enzymes rapidly evolved for directed purposes. They also interact with specific molecules. This results in a high yield of desired products with unparalleled selectivities.
Scientists also said, the reactions that enzymes allow for are relatively limited. This is a small repertoire for their powerful ability to efficiently make products at lower material and environmental costs.
Scientists have developed a method in which certain enzymes can be coaxed into facilitating useful reactions. These was never seen in the biological world. So, these will open possibilities for processes never before conducted by enzymes.
The research paper has been published in the journal Science.
Stereochemistry or 3D chemistry is important to control the bioactivity of small-molecule medicines. Biomacromolecules like DNAs and proteins are chiral. This means they are asymmetric in structure.
One effective way to create chiral molecules is dependent on asymmetric catalysis. This is a process where a tailored catalyst selectively produces one enantiomer instead of another. But there are many challenges in the field of asymmetric catalysis. But radical reactions or reactions involving open-shell intermediates have not yet succumbed to asymmetric catalysis.
Scientists said, there are two problems, one is radical. When the radical is generated, it doesn’t interact tightly with the catalyst. Another is there is sometimes the activity-selectivity tradeoff.
Scientists said, the solution is directed evolution. This will help to evolve the enzyme to be able to rein in the radical.
The scientists took inspiration from Nobel Prize-winning Caltech chemical engineer Frances Arnold. Scientists conducted iterative rounds of evolution and screening of cytochromes P450. The superfamily of metalloenzymes is found in an iron-containing molecule which is essential for catalysis.
The scientists have screened the protein mutants to aid in the identification of promising enzyme catalysts. The enzyme then become the parent in the subsequent round of engineering. In this way, through screening, optimal enzyme activity and selectivity are achieved. This opens up new possibilities like a wider variety of molecules which can act upon newly evolved enzymes.