Fatty acid hydrolysis of acyl marinobactin siderophores by Marinobacter acylases

Michelle P. Kem, Hiroaki Naka, Akira Iinishi, Margo G. Haygood, Alison Butler

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

The marine bacteria Marinobacter sp. DS40M6 and Marinobacter nanhaiticus D15-8W produce a suite of acyl peptidic marinobactin siderophores to acquire iron under iron-limiting conditions. During late-log phase growth, the marinobactins are hydrolyzed to form the marinobactin headgroup with release of the corresponding fatty acid tail. The bntA gene, a homologue of the Pseudomonas aeruginosa pyoverdine acylase gene, pvdQ, was identified from Marinobacter sp. DS40M6. A bntA knockout mutant of Marinobacter sp. DS40M6 produced the suite of acyl marinobactins A-E, without the usual formation of the marinobactin headgroup. Another marinobactin-producing species, M. nanhaiticus D15-8W, is predicted to have two pvdQ homologues, mhtA and mhtB. MhtA and MhtB have 67% identical amino acid sequences. MhtA catalyzes hydrolysis of the apo-marinobactin siderophores as well as the quorum sensing signaling molecule, dodecanoyl-homoserine lactone. In contrast to hydrolysis of the suite of apo-marinobactins by MhtA, hydrolysis of the iron(III)-bound marinobactins was not observed. (Chemical Equation Presented).

Original languageEnglish (US)
Pages (from-to)744-752
Number of pages9
JournalBiochemistry
Volume54
Issue number3
DOIs
StatePublished - Jan 27 2015

ASJC Scopus subject areas

  • Biochemistry

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    Kem, M. P., Naka, H., Iinishi, A., Haygood, M. G., & Butler, A. (2015). Fatty acid hydrolysis of acyl marinobactin siderophores by Marinobacter acylases. Biochemistry, 54(3), 744-752. https://doi.org/10.1021/bi5013673