Enzymes/proteins are the most versatile bio-molecules in the living system. In the living system, the enzyme catalyzes biochemical reactions in varying magnitude. The nature of the enzyme can be defined as robust and effective. It is believed enzymes are highly specific towards its substrate. At the same enzyme do catalyze multiple biochemical reactions at varying pace. There is growing research evidence suggests enzymes are highly promiscuous and capable of multiple binding substrates. Promiscuity is a phenomenon where enzymes do develop an affinity for various substrates and catalyze numerous biochemical reactions. Further, promiscuity is a natural phenomenon that can be at the substrate level and or at the catalytic level. However, recent studies have established artificial promiscuity called induced promiscuity. Induced promiscuity is entirely different from protein engineering, where a specific amino acid/s modified for the desired property. Over the last decade, growing research work was carried out to understand the nature and mechanism of enzyme promiscuity along with its commercial implication. Despite extensive research work on enzyme promiscuity still, we are unable to comprehend molecular insights of enzyme promiscuity. As a core area of green chemistry, enzyme promiscuity is crucial not only for the extended use of such unique molecules but also for sustainable development as well. The wide range of applications of enzymes, including healthcare, agriculture, industry, and food industry, the enzyme promiscuity had shown tremendous scope in the future.

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Citation

Citation: Mahendra Kumar Verma and Samba Naik A. “Enzyme Promiscuity and Molecular Mechanism; Mystery Remain Unsolved". Acta Scientific Biotechnology 1.10 (2020): 24-25.

Copyright

Copyright: © 2020 Mahendra Kumar Verma and Samba Naik A. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.