Violates New Chemical Reaction Rules – With Applications From Creating New Drugs For Food Production

Scientists violate enzyme engineering rules to unlock new methods for creating chemical reactions that can unlock a number of new applications – from the creation of new drugs to food production.

In a paper they published recently on Katalitian Alam, Professor Francesca Paradisi and Dr. Martina Contente from the University of Nottingham and University of Bern demonstrates new methods for producing chemical molecules more efficiently through step-by-step reactions in enzymes.

“We have shown how simple mutations in one of the key residues of beneficial enzymes have dramatically expanded their synthetic scope, allowing the use of mutant variants in the preparation of challenging chemical molecules, as well as natural metabolites that are essential in many biological processes in the body.”

Professor Paradis, Professor of Biocatalysis at the School of Chemistry in Nottingham

Any textbook about enzymes will report how catalytic amino acids in a particular family of enzymes preserved at all, they are in fact the signatures of the types of chemicals that can be produced by the enzyme. Variation does occur and in some cases, changes in amino acids sour similarly, both can be found in important ratios in Nature, but the other can be more rare and only exist in a limited number of species.

“In this study we have explored the engineering areas of undetectable enzymes and altered key catalytic residues at enzyme-active sites,” added Professor Paradisi, ” synthetic direction and the fact that molecules are challenging but very useful can now be made in mild conditions that can be easily scaled and commercially imitated for use in a variety of products. ”

To alter the substrate scope of an enzyme, the approach is usually a mutation of a residue involved in the recognition of the substrate, whether by rational design or evolution directed, then not catalytically catalyzed.

Mutant variants of the acyl transferase enzyme are rapidly created and while the original biocatalyst will work with linear alcohols and amines, the mutants can work with more complex thiols and amines as well. Research shows that indeed new variants have lost the ability to hydrolyze esters, but for synthetic applications, where esters or other functional groups need to be made (thioesters and amides) and not split, this is in fact a major advantage.

“We have had a good response to this research from the scientific community because it provides a new tool for chemistry that can be applied to a variety of molecular reactions. The fact that it is a very stable reaction made without the need for special conditions means it has the possibility of commercial application cheap in the production of new pharmacies. We believe we have unlocked new combinations in the catalytic triad that they seem unlikely, seem to dilute the reactivity control, but for chemists can be a real gold mine. “

Dr. Martina Contente

References: “Strategic Ser / Cys exchange in the catalytic triad unlocks acyltransferase-mediated synthesis of thioesters and tertiary amides” by Martina L. Contente, David Roura Padrosa, Francesco Molinari and Francesca Paradisi, 30 November 2020, Katalitian Alam,
DOI: 10.1038 / s41929-020-00539-0

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