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 journalArticlepeer-review

11 Scopus citations


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
Issue number3
StatePublished - Jan 27 2015
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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