Biosynthesis of the pyoverdine siderophore of Pseudomonas aeruginosa involves precursors with a myristic or a myristoleic acid chain.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hannauer M,Schäfer M,Hoegy F,Gizzi P,Wehrung P,Mislin GL,Budzikiewicz H,Schalk IJ

doi

10.1016/j.febslet.2011.12.004

subject

Has Abstract

pub_date

2012-01-02 00:00:00

pages

96-101

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(11)00875-1

journal_volume

586

pub_type

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