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© Jean Marc Panaud
Cyanobactérie souche "PCC 9401". Souche de la "Pasteur Culture Collection of Cyanobacteria" conservée à l'état axénique dans l'Unité des Cyanobactéries. La PCC est l'une des Collections spécialisées de l'Institut Pasteur.
Publication : Angewandte Chemie (International ed. in English)

Radical S-adenosyl methionine epimerases: regioselective introduction of diverse D-amino acid patterns into peptide natural products

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Angewandte Chemie (International ed. in English) - 18 Jun 2014

Morinaka BI, Vagstad AL, Helf MJ, Gugger M, Kegler C, Freeman MF, Bode HB, Piel J

Link to Pubmed [PMID] – 24943072

Angew. Chem. Int. Ed. Engl. 2014 Aug;53(32):8503-7

PoyD is a radical S-adenosyl methionine epimerase that introduces multiple D-configured amino acids at alternating positions into the highly complex marine peptides polytheonamide A and B. This novel post-translational modification contributes to the ability of the polytheonamides to form unimolecular minimalistic ion channels and its cytotoxic activity at picomolar levels. Using a genome mining approach we have identified additional PoyD homologues in various bacteria. Three enzymes were expressed in E. coli with their cognate as well as engineered peptide precursors and shown to introduce diverse D-amino acid patterns into all-L peptides. The data reveal a family of architecturally and functionally distinct enzymes that exhibit high regioselectivity, substrate promiscuity, and irreversible action and thus provide attractive opportunities for peptide engineering.

http://www.ncbi.nlm.nih.gov/pubmed/24943072