Biosynthetic considerations of triscatechol siderophores framed on serine and threonine macrolactone scaffolds. Issue 7 (8th June 2017)

• Record Type: Journal Article
• Authors: Reitz, Zachary L.; Sandy, Moriah; Butler, Alison
• Is Part Of: Metallomics. Volume 9:Issue 7(2017)
• Page Start: 824
• Page End: 839
• Publication Date: 2017-06-08
• Subjects: Metals -- Physiological effect -- Periodicals; 572.51
• DOI: 10.1039/c7mt00111h
• Languages: English
• ISSNs: 1756-5901

Abstract

Abstract : The biosyntheses of a family of enterobactin variants – amino acid substitution, insertion, and derivatization, and macrolactone expansion – is reviewed. Abstract : Bacteria often produce siderophores to facilitate iron uptake. One of the most studied siderophores is enterobactin, the macrolactone trimer of 2, 3-dihydroxybenzoyl-l -serine, produced by E. coli and many other enteric bacteria. Other siderophores are variants of enterobactin, with structural modifications including expansion of the tri-serine core to a tetra-serine macrolactone, substitution ofl -serine withl -threonine, insertion of amino acids ( i.e., Gly, l -Ala, d -Lys, d - andl -Arg, l -Orn), catechol glucosylation, and linearization of the tri-serine macrolactone core. In this review we summarize the current understanding of the biosyntheses of these enterobactin variants, placing them in contrast with the well-established biosynthesis of enterobactin.