Fatty Acid Hydrolysis of Acyl Marinobactin Siderophores by Marinobacter Acylases

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• 作者：Michelle P. Kem ; Hiroaki Naka ; Akira Iinishi ; Margo G. Haygood ; Alison Butler
• 刊名：Biochemistry
• 出版年：2015
• 出版时间：January 27, 2015
• 年：2015
• 卷：54
• 期：3
• 页码：744-752
• 全文大小：358K
• ISSN：1520-4995

文摘

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鈥揈, 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.