Biosynthesis of Amphi-enterobactin Siderophores by Vibrio harveyi BAA-1116: Identification of a Bifunctional Nonribosomal Peptide Synthetase Condensation Domain
| Autor: | Moriah Sandy, Hannah K. Zane, Hiroaki Naka, Federico Rosconi, Margo G. Haygood, Alison Butler |
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| Rok vydání: | 2014 |
| Předmět: |
inorganic chemicals
Siderophore Mutant Siderophores Biochemistry Catalysis Enterobactin Condensation domain chemistry.chemical_compound Colloid and Surface Chemistry Biosynthesis Nonribosomal peptide Gene cluster polycyclic compounds Peptide Synthases Chromatography High Pressure Liquid Vibrio chemistry.chemical_classification biology Vibrio harveyi General Chemistry biology.organism_classification chemistry bacteria |
| Zdroj: | Journal of the American Chemical Society. 136:5615-5618 |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | 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, ΔaebG V. harveyi, and the NRPS knockout mutant, ΔaebF 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. |
| Databáze: | OpenAIRE |
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