Biosynthesis of amphi-enterobactin siderophores by Vibrio harveyi BAA-1116: Identification of a bifunctional nonribosomal peptide synthetase condensation domain

Hannah K. Zane, Hiroaki Naka, Federico Rosconi, Moriah Sandy, Margo G. Haygood, Alison Butler

Research output: Contribution to journalArticle

27 Scopus citations


The genome of Vibrio harveyi BAA-1116 contains a nonribosomal peptide synthetase (NRPS) gene cluster (aebA-F) resembling that for enterobactin, yet enterobactin is not produced. A gene predicted to encode a long-chain fatty acid CoA ligase (FACL), similar to enzymes involved in the biosynthesis of acyl peptides, resides 15 kb away from the putative enterobactin-like biosynthetic gene cluster (aebG). The proximity of this FACL gene to the enterobactin-like synthetase suggested that V. harveyi may produce amphiphilic enterobactin-like siderophores. Extraction of the bacterial cell pellet of V. harveyi led to the isolation and structure determination of a suite of eight amphi-enterobactin siderophores composed of the cyclic lactone of tris-2,3-dihydroxybenzoyl-l- serine and acyl-l-serine. The FACL knockout mutant, "aebG V. harveyi, and the NRPS knockout mutant, "aebF V. harveyi, do not produce amphi-enterobactins. The amphi-enterobactin biosynthetic machinery was heterologously expressed in Escherichia coli and reconstituted in vitro, demonstrating the condensation domain of AebF has unique activity, catalyzing two distinct condensation reactions.

Original languageEnglish (US)
Pages (from-to)5615-5618
Number of pages4
JournalJournal of the American Chemical Society
Issue number15
StatePublished - Apr 16 2014


ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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