Diketopiperazines are characterized by a piperazine-2,5-dione ring, obtained by the condensation and cyclization of two amino acids. They can be synthesized by cyclodipeptide synthases (CDPS – CycloDiPeptide Synthase), classs of enzymes that we and the group of Muriel Gondry discovered. These enzymes use charged tRNAs as substrates, diverting them from protein synthesis. The formation of a cyclodipeptide (CDP) is often the first step in the synthesis of more complex DKPs, the CDP being modified by enzymes called tailoring enzymes (oxidase, cytochrome P450, methyl transferase, …).
Within the team, we have characterized the biosynthetic pathway of various DKPs (albonoursine, bicyclomycin, sfaxomycins) and we are seeking to identify new modification enzymes associated with CDPS. In particular, we are interested in the enzymatic activity of cytochromes P450. Finally, the study of the biological role of these molecules in the producing our research.