ArticleScientific reports2019
Functional and structural basis of E. coli enolase inhibition by SF2312: a mimic of the carbanion intermediate.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 19 citations in OpenAlex.
- Bioconversion of agricultural waste to ε-poly-L-lysine by an engineered Streptomyces albulus strain.World journal of microbiology & biotechnology · 2026Article
- ENOblock synergizes with colistin to treat Acinetobacter baumannii infections.EMBO molecular medicine · 2025Article
- Recent advances in natural and synthetic phosphonate therapeutics.Current opinion in microbiology · 2025Review
- Structure, identification and characterization of the RibD-enolase complex inbioRxiv : the preprint server for biology · 2025Article
- Integrated Information for Pathogenicity and Treatment of Spiroplasma.Current microbiology · 2024Review
- BeyondMolecular therapy oncolytics · 2023Review
- Chlamydia trachomatis RsbU Phosphatase Activity Is Inhibited by the Enolase Product, Phosphoenolpyruvate.Journal of bacteriology · 2022Article
- Antibacterial apple cider vinegar eradicates methicillin resistant Staphylococcus aureus and resistant Escherichia coli.Scientific reports · 2021Article
- Amoxicillin Haptenation ofFrontiers in pharmacology · 2021Article
- The ThiL enzyme is a valid antibacterial target essential for both thiamine biosynthesis and salvage pathways inThe Journal of biological chemistry · 2020Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Many years ago, the natural secondary metabolite SF2312, produced by the actinomycete Micromonospora, was reported to display broad spectrum antibacterial properties against both Gram-positive and Gram-negative bacteria. Recent studies have revealed that SF2312, a natural phosphonic acid, functions as a potent inhibitor of human enolase. The mechanism of SF2312 inhibition of bacterial enolase and its role in bacterial growth and reproduction, however, have remained elusive. In this work, we detail a structural analysis of E. coli enolase bound to both SF2312 and its oxidized imide-form. Our studies support a model in which SF2312 acts as an analog of a high energy intermediate formed during the catalytic process. Biochemical, biophysical, computational and kinetic characterization of these compounds confirm that altering features characteristic of a putative carbanion (enolate) intermediate significantly reduces the potency of enzyme inhibition. When SF2312 is combined with fosfomycin in the presence of glucose-6 phosphate, significant synergy is observed. This suggests the two agents could be used as a potent combination, targeting distinct cellular mechanism for the treatment of bacterial infections. Together, our studies rationalize the structure-activity relationships for these phosphonates and validate enolase as a promising target for antibiotic discovery.
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