ArticleNature chemical biology2009
AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.
Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 77 citations in OpenAlex.
- The iron(III) coordinating properties of citrate and α-hydroxycarboxylate containing siderophores.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways.Structure (London, England : 1993) · 2025Article
- Structure and catalytic mechanism of exogenous fatty acid recycling by AasS, a versatile acyl-ACP synthetase.Nature structural & molecular biology · 2025Article
- Discovery, functional characterization, and structural studies of the NRPS-independent siderophore synthetases.Critical reviews in biochemistry and molecular biology · 2024Review
- Analysis of the vibrioferrin biosynthetic pathway of Vibrio parahaemolyticus.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Overview ofFrontiers in microbiology · 2024Review
- Chryseochelins-structural characterization of novel citrate-based siderophores produced by plant protecting Chryseobacterium spp.Metallomics : integrated biometal science · 2023Article
- Chemoenzymatic Synthesis of Select Intermediates and Natural Products of the Desferrioxamine E Siderophore Pathway.Molecules (Basel, Switzerland) · 2022Article
- ATP6AP1 is a potential prognostic biomarker and is associated with iron metabolism in breast cancer.Frontiers in genetics · 2022Article
- Conjuring up a ghost: structural and functional characterization of FhuF, a ferric siderophore reductase from E. coli.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Uncovering the chemistry of C-C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex.Chemical communications (Cambridge, England) · 2020Article
- 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
- SARS-unique fold in the Rousettus bat coronavirus HKU9.Protein science : a publication of the Protein Society · 2017Article
- The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.Nature chemical biology · 2017Article
- Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters.Nature chemical biology · 2017Article
- Structural and Functional Characterization of Aerobactin Synthetase IucA from a Hypervirulent Pathotype of Klebsiella pneumoniae.Biochemistry · 2016Article
- A Modified Coupled Spectrophotometric Method to Detect 2-5 Oligoadenylate Synthetase Activity in Prostate Cell Lines.Biological procedures online · 2016Article
- The structural biology of patellamide biosynthesis.Current opinion in structural biology · 2014Review
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13 authors at 2 institutions in 1 country.
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Abstract
Bacterial pathogens need to scavenge iron from their host for growth and proliferation during infection. They have evolved several strategies to do this, one being the biosynthesis and excretion of small, high-affinity iron chelators known as siderophores. The biosynthesis of siderophores is an important area of study, not only for potential therapeutic intervention but also to illuminate new enzyme chemistries. Two general pathways for siderophore biosynthesis exist: the well-characterized nonribosomal peptide synthetase (NRPS)-dependent pathway and the NRPS-independent siderophore (NIS) pathway, which relies on a different family of sparsely investigated synthetases. Here we report structural and biochemical studies of AcsD from Pectobacterium (formerly Erwinia) chrysanthemi, an NIS synthetase involved in achromobactin biosynthesis. The structures of ATP and citrate complexes provide a mechanistic rationale for stereospecific formation of an enzyme-bound (3R)-citryladenylate, which reacts with L-serine to form a likely achromobactin precursor. AcsD is a unique acyladenylate-forming enzyme with a new fold and chemical catalysis strategy.
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