title: Nonribosomal peptide synthesis in animals: the cyclodipeptide synthase of Nematostella.
abstract: Cyclodipeptide synthases (CDPSs) are small enzymes structurally related to class-I aminoacyl-tRNA synthetases (aaRSs). They divert aminoacylated tRNAs from their canonical role in ribosomal protein synthesis, for cyclodipeptide formation. All the CDPSs experimentally characterized to date are bacterial. We show here that a predicted CDPS from the sea anemone Nematostella vectensis is an active CDPS catalyzing the formation of various cyclodipeptides, preferentially containing tryptophan. Our findings demonstrate that eukaryotes encode active CDPSs and suggest that all CDPSs have a similar aminoacyl-tRNA synthetase-like architecture and ping-pong mechanism. They also raise questions about the biological roles of the cyclodipeptides produced in bacteria and eukaryotes.
authors: CEA, Institut de Biologie et Technologies de Saclay, F-91191 Gif-sur-Yvette, France.
authors: Jérôme
authors: J
authors: Seguin
authors: Mireille
authors: M
authors: Moutiez
authors: Yan
authors: Y
authors: Li
authors: Pascal
authors: P
authors: Belin
authors: Alain
authors: A
authors: Lecoq
authors: Matthieu
authors: M
authors: Fonvielle
authors: Jean-Baptiste
authors: JB
authors: Charbonnier
authors: Jean-Luc
authors: JL
authors: Pernodet
authors: Muriel
authors: M
authors: Gondry
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D046908:Peptide Biosynthesis, Nucleic Acid-Independent; D010453:Peptide Synthases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010456:Peptides, Cyclic / Q000096:biosynthesis*; D017434:Protein Structure, Tertiary; D012615:Sea Anemones / Q000201:enzymology*; D016415:Sequence Alignment
chemical_list: D010456:Peptides, Cyclic; D010453:Peptide Synthases