A putative operon encoding the biosynthetic pathway for the cytotoxic cyanobacterial lipopeptides puwainphycins was identified in Cylindrospermum alatosporum. Bioinformatics analysis enabled sequential prediction of puwainaphycin biosynthesis; this process is initiated by the activation of a fatty acid residue via fatty acyl-AMP ligase and continued by a multidomain non-ribosomal peptide synthetase/polyketide synthetase. High-resolution mass spectrometry and nuclear magnetic resonance spectroscopy measurements proved the production of puwainaphycin F/G congeners differing in FA chain length formed by either 3-amino-2-hydroxy-4-methyl dodecanoic acid (4-methyl-Ahdoa) or 3-amino-2-hydroxy-4-methyl tetradecanoic acid (4-methyl-Ahtea). Because only one puwainaphycin operon was recovered in the genome, we suggest that the fatty acyl-AMP ligase and one of the amino acid adenylation domains (Asn/Gln) show extended substrate specificity. Our results provide the first insight into the biosynthesis of frequently occurring β-amino fatty acid lipopeptides in cyanobacteria, which may facilitate analytical assessment and development of monitoring tools for cytotoxic cyanobacterial lipopeptides.

• MeSH
• anotace sekvence MeSH
• bakteriální geny MeSH
• bakteriální proteiny genetika   fyziologie   MeSH
• biosyntetické dráhy MeSH
• ligasy genetika   fyziologie   MeSH
• lipopeptidy biosyntéza   MeSH
• molekulární sekvence - údaje MeSH
• multigenová rodina MeSH
• polyketidsynthasy genetika   fyziologie   MeSH
• sinice enzymologie   genetika   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• bakteriální proteiny MeSH
• ligasy MeSH
• lipopeptidy MeSH
• polyketidsynthasy MeSH
• puwainaphycin F MeSH Prohlížeč
• puwainaphycin G MeSH Prohlížeč