ArticleThe Journal of biological chemistry2012
Functional and structural analysis of the siderophore synthetase AsbB through reconstitution of the petrobactin biosynthetic pathway from Bacillus anthracis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- A frameshift mutation drives divergent biosynthesis of metallophores inbioRxiv : the preprint server for biology · 2026Article
- Integrative phylogenomic and pangenome landscape of Bacillus: insights from 10,000 genomes into taxonomy, functional potential, and biotechnological applications.World journal of microbiology & biotechnology · 2026Article
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- Computational mass spectrometry and genome mining guided discovery of metallophores produced by Microbulbifer.ISME communications · 2026Article
- Genomic characterization of clinical and environmental isolates of Bacillus anthracis in Peru.PLoS neglected tropical diseases · 2026Article
- Whole-Genome Analysis ofMicroorganisms · 2025Article
- Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways.Structure (London, England : 1993) · 2025Article
- Identification and Characterization of the Biosynthesis of the Hybrid NRPS-NIS Siderophore Nocardichelin.ACS chemical biology · 2025Article
- New insights into iron uptake in Streptococcus mutans: evidence for a role of siderophore-like molecules.Archives of microbiology · 2025Article
- Discovery, functional characterization, and structural studies of the NRPS-independent siderophore synthetases.Critical reviews in biochemistry and molecular biology · 2024Review
- Kinetic analysis of the three-substrate reaction mechanism of an NRPS-independent siderophore (NIS) synthetase.Methods in enzymology · 2024Article
- Two distinct non-ribosomal peptide synthetase-independent siderophore synthetase gene clusters identified in Armillaria and other species in the Physalacriaceae.G3 (Bethesda, Md.) · 2023Article
- Chemoenzymatic Synthesis of Select Intermediates and Natural Products of the Desferrioxamine E Siderophore Pathway.Molecules (Basel, Switzerland) · 2022Article
- The Purified Siderophore fromMolecules (Basel, Switzerland) · 2022Article
- Petrobactin, a siderophore produced by Alteromonas, mediates community iron acquisition in the global ocean.The ISME journal · 2022Article
- High Potential for Secondary Metabolite Production ofFrontiers in microbiology · 2021Article
- The Siderophore Synthetase IucA of the Aerobactin Biosynthetic Pathway Uses an Ordered Mechanism.Biochemistry · 2020Article
- Targeting adenylate-forming enzymes with designed sulfonyladenosine inhibitors.The Journal of antibiotics · 2019Review
- Structural and functional delineation of aerobactin biosynthesis in hypervirulentThe Journal of biological chemistry · 2018Article
- Petrobactin Is Exported frommBio · 2017Article
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Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
Abstract
Petrobactin, a mixed catechol-carboxylate siderophore, is required for full virulence of Bacillus anthracis, the causative agent of anthrax. The asbABCDEF operon encodes the biosynthetic machinery for this secondary metabolite. Here, we show that the function of five gene products encoded by the asb operon is necessary and sufficient for conversion of endogenous precursors to petrobactin using an in vitro system. In this pathway, the siderophore synthetase AsbB catalyzes formation of amide bonds crucial for petrobactin assembly through use of biosynthetic intermediates, as opposed to primary metabolites, as carboxylate donors. In solving the crystal structure of the B. anthracis siderophore biosynthesis protein B (AsbB), we disclose a three-dimensional model of a nonribosomal peptide synthetase-independent siderophore (NIS) synthetase. Structural characteristics provide new insight into how this bifunctional condensing enzyme can bind and adenylate multiple citrate-containing substrates followed by incorporation of both natural and unnatural polyamine nucleophiles. This activity enables formation of multiple end-stage products leading to final assembly of petrobactin. Subsequent enzymatic assays with the nonribosomal peptide synthetase-like AsbC, AsbD, and AsbE polypeptides show that the alternative products of AsbB are further converted to petrobactin, verifying previously proposed convergent routes to formation of this siderophore. These studies identify potential therapeutic targets to halt deadly infections caused by B. anthracis and other pathogenic bacteria and suggest new avenues for the chemoenzymatic synthesis of novel compounds.
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