ArticleBiochemistry2016
Deciphering the Substrate Specificity of SbnA, the Enzyme Catalyzing the First Step in Staphyloferrin B Biosynthesis.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Integrated Metabolomic and Genomic Insights into Amino Acid Incorporation Within the Hybrid Polyketide-Alkaloid Antibiotic TLN-05220.ACS chemical biology · 2026Article
- Integrated metabolomic and genomic insights into amino acid incorporation within the hybrid polyketide-alkaloid antibiotic TLN-05220.bioRxiv : the preprint server for biology · 2025Article
- First-in-class inhibitors of SbnA reduce siderophore production in Staphylococcus aureus.The FEBS journal · 2025Article
- Global quantitative proteome analysis of a multi-resistantFrontiers in microbiology · 2025Article
- Siderophores: A Case Study in Translational Chemical Biology.Biochemistry · 2024Review
- Crystal structure of CmnB involved in the biosynthesis of the nonproteinogenic amino acid L-2,3-diaminopropionic acid.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Structural basis of the inhibition of cystathionine γ-lyase from Toxoplasma gondii by propargylglycine and cysteine.Protein science : a publication of the Protein Society · 2023Article
- Review
- Leveraging Microbial Genomes and Genomic Context for Chemical Discovery.Accounts of chemical research · 2021Article
- Pyridoxal-5'-phosphate-dependent alkyl transfer in nucleoside antibiotic biosynthesis.Nature chemical biology · 2020Article
- The feather degradation mechanisms of a new Streptomyces sp. isolate SCUT-3.Communications biology · 2020Article
- Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.International journal of molecular sciences · 2020Review
- The heme-sensitive regulator SbnI has a bifunctional role in staphyloferrin B production byThe Journal of biological chemistry · 2019Article
- The Polycyclic Polyprenylated Acylphloroglucinol Antibiotic PPAP 23 Targets the Membrane and Iron Metabolism inFrontiers in microbiology · 2019Article
- Functional Characterization and Structure-Guided Mutational Analysis of the Transsulfuration Enzyme Cystathionine γ-Lyase fromInternational journal of molecular sciences · 2018Article
- SbnI is a free serine kinase that generatesThe Journal of biological chemistry · 2018Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Staphylococcus aureus assembles the siderophore, staphyloferrin B, from l-2,3-diaminopropionic acid (l-Dap), α-ketoglutarate, and citrate. Recently, SbnA and SbnB were shown to produce l-Dap and α-ketoglutarate from O-phospho-l-serine (OPS) and l-glutamate. SbnA is a pyridoxal 5'-phosphate (PLP)-dependent enzyme with homology to O-acetyl-l-serine sulfhydrylases; however, SbnA utilizes OPS instead of O-acetyl-l-serine (OAS), and l-glutamate serves as a nitrogen donor instead of a sulfide. In this work, we examined how SbnA dictates substrate specificity for OPS and l-glutamate using a combination of X-ray crystallography, enzyme kinetics, and site-directed mutagenesis. Analysis of SbnA crystals incubated with OPS revealed the structure of the PLP-α-aminoacrylate intermediate. Formation of the intermediate induced closure of the active site pocket by narrowing the channel leading to the active site and forming a second substrate binding pocket that likely binds l-glutamate. Three active site residues were identified: Arg132, Tyr152, Ser185 that were essential for OPS recognition and turnover. The Y152F/S185G SbnA double mutant was completely inactive, and its crystal structure revealed that the mutations induced a closed form of the enzyme in the absence of the α-aminoacrylate intermediate. Lastly, l-cysteine was shown to be a competitive inhibitor of SbnA by forming a nonproductive external aldimine with the PLP cofactor. These results suggest a regulatory link between siderophore and l-cysteine biosynthesis, revealing a potential mechanism to reduce iron uptake under oxidative stress.
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