Article ID Journal Published Year Pages File Type
2048126 FEBS Letters 2012 6 Pages PDF
Abstract

Pyoverdine I (PVDI) is the major siderophore produced by Pseudomonas aeruginosa to import iron. Biosynthesis of this chelator involves non-ribosomal peptide synthetases and other enzymes. PvdQ is a periplasmic enzyme from the NTN hydrolase family and is involved in the final steps of PVDI biosynthesis. A pvdQ mutant produces two non-fluorescent PVDI precursors with a higher molecular mass than PVDI. In the present study, we describe the use of mass spectrometry to determine the structure of these PVDI precursors and show that they both contain a unformed chromophore like ferribactin, and either a myristic or myristoleic chain that must be removed before PVDI is secreted into the extracellular medium.

► We solve by mass spectrometry the structure of two pyoverdine siderophore precursors. ► A PvdQ mutant produces these precursors. ► They both have a higher molecular mass as the pyoverdine. ► We show that both compounds contain an unformed chromophore and a myristic or a myristoleic acid chain.

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