Biocatalytic activity of cytochromes P450 for the valorization of terpenes Danilo Correddu, Giovanna Di Nardo and Gianfranco Gilardi University of Turin, Italy
Cytochromes P450 are a group of heme-containing enzymes that play a significant role in the metabolism of xenobiotics, drugs, and endogenous compounds. Among them, self-sufficient P450s are enzymes that combine all their functional domains in a single polypeptide chain. They can perform regio- and stereo- selective oxidation of a wide range of organic compounds. 1 In recent years, their potential for biocatalysis in the valorization of terpenes has garnered significant attention. Terpenes are a class of natural compounds that are widely distributed in the plant kingdom and possess a variety of biological activities. They have also been identified as a valuable source of bio-based chemicals, including flavors, fragrances, and pharmaceuticals. In our works, we developed laboratory evolved P450 mutants with specific amino acid substitutions, leading to structural rearrangements of the enzyme, which gains flexibility and causes the rotation of a key residue in the active site. This results in enhanced and specific oxidation activity towards different substrates, including terpenes with the formation of valuable oxide derivatives. Their biocatalytic activity can be exploited in different systems including the use of whole cells or purified enzymes, highlighting the relevance of these enzymes for industrial applications. 2 References 1. Correddu, G. Di Nardo and G. Gilardi, Trends Biotechnol. , 2021, 39 , 1184–1207. 2. Correddu, S. H. Aly, G. D. Nardo, G. Catucci, C. Prandi, M. Blangetti, C. Bellomo, E. Bonometti, G. Viscardi and G. Gilardi, RSC Adv. , 2022, 12 , 33964–33969.
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