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http://purl.uniprot.org/citations/21906287http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21906287http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21906287http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/21906287http://www.w3.org/2000/01/rdf-schema#comment"

Background

Staphylococcus aureus synthesizes two siderophores, staphyloferrin A and staphyloferrin B, that promote iron-restricted growth. Previous work on the biosynthesis of staphyloferrin B has focused on the role of the synthetase enzymes, encoded from within the sbnA-I operon, which build the siderophore from the precursor molecules citrate, alpha-ketoglutarate and L-2,3-diaminopropionic acid. However, no information yet exists on several other enzymes, expressed from the biosynthetic cluster, that are thought to be involved in the synthesis of the precursors (or synthetase substrates) themselves.

Results

Using mutants carrying insertions in sbnA and sbnB, we show that these two genes are essential for the synthesis of staphyloferrin B, and that supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants. Several mechanisms are proposed for how the enzymes SbnA, with similarity to cysteine synthase enzymes, and SbnB, with similarity to amino acid dehydrogenases and ornithine cyclodeaminases, function together in the synthesis of this unusual nonproteinogenic amino acid L-2,3-diaminopropionic acid.

Conclusions

Mutation of either sbnA or sbnB result in abrogation of synthesis of staphyloferrin B, a siderophore that contributes to iron-restricted growth of S. aureus. The loss of staphyloferrin B synthesis is due to an inability to synthesize the unusual amino acid L-2,3-diaminopropionic acid which is an important, iron-liganding component of the siderophore structure. It is proposed that SbnA and SbnB function together as an L-Dap synthase in the S. aureus cell."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/name"BMC Microbiol."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/name"BMC Microbiol."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.org/dc/terms/identifier"doi:10.1186/1471-2180-11-199"xsd:string
http://purl.uniprot.org/citations/21906287http://purl.org/dc/terms/identifier"doi:10.1186/1471-2180-11-199"xsd:string
http://purl.uniprot.org/citations/21906287http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21906287
http://purl.uniprot.org/citations/21906287http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21906287
http://purl.uniprot.org/citations/21906287http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21906287
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/author"Cheung J."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/author"Cheung J."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/author"Heinrichs D.E."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/author"Heinrichs D.E."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/author"Beasley F.C."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/author"Beasley F.C."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/pages"199"xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/pages"199"xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/title"Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/title"Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus."xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/21906287http://purl.uniprot.org/core/volume"11"xsd:string
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