Sumedha Guha, Techno India University
Every enzyme family has a set of amino acids that are highly conserved in that specific enzyme family. Better known as catalytic triads, these are a set of three amino acid residues found in the active site of the enzymes which serve as a signature of the type of chemistry the enzyme can do.
Professor Francesca Paradisi and Dr. Martina Contente of the University of Nottingham and the University of Bern in their recent paper published in Nature Catalysis have elaborated on their groundbreaking work in expanding the synthetic capability of an acyltransferase variant found in Mycobacterium smegmatis. This enables them to yield a biocatalyst which can efficiently catalyze the formation of thioesters and tertiary amides in water. The use of the mutant variant of this enzyme can be utilized in the preparation of challenging chemical compounds, metabolites that are vital to many of the biological processes in the body and even for large scale drug production in the pharmaceutical industry.
This alteration was brought about by a strategic change in the Ser/Cys residues of the catalytic triads. Previously it was thought that doing this would cause a loss of activity of the enzyme but it has been found that such is not the case when the biocatalyst is used in a synthetic direction. Essential chemical molecules can now be made under mild conditions, which can be scaled up and replicated industrially for use in a wide range of commercial products.
Furthermore, two factors make this new one-step reaction in the enzyme a highly sustainable and low-cost procedure. These are – the high substrate to catalyst ratio and the cofactor independence. This renders the reaction as a viable tool that can be successfully applied to molecular reactions like the synthesis of acetyl coenzyme A as well as other structurally simpler analogues.
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