ArticleNature chemical biology2016
SF2312 is a natural phosphonate inhibitor of enolase.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 99 citations in OpenAlex.
- From Discovery to Manufacturing: A Quantitative Review of Phosphonates and Strategies for High-Titer Production.Microorganisms · 2026Review
- Enolase 1: A paradigm of metabolic enzyme moonlighting in tumorigenesis (Review).International journal of oncology · 2026Review
- Fungal commensal promotes intestinal repair via its secreted peptide in mice.Nature microbiology · 2026Article
- Synthetic lethality in cancer drug discovery: challenges and opportunities.Nature reviews. Drug discovery · 2026Review
- Recent advances in natural and synthetic phosphonate therapeutics.Current opinion in microbiology · 2025Review
- Integrative Single-Cell and Bulk RNA Sequencing Identifies a Glycolysis-Related Prognostic Signature for Predicting Prognosis in Pancreatic Cancer.International journal of molecular sciences · 2025Article
- ZFP64 drives glycolysis-mediated stem cell-like properties and tumorigenesis in breast cancer.Biology direct · 2024Article
- Enolase inhibitors as therapeutic leads for Naegleria fowleri infection.PLoS pathogens · 2024Article
- The intersection of hostMicrobiology and molecular biology reviews : MMBR · 2024Review
- Discovery of the Highly Selective and Potent STAT3 Inhibitor for Pancreatic Cancer Treatment.ACS central science · 2024Article
- BeyondMolecular therapy oncolytics · 2023Review
- Enolase Inhibitors as Early Lead Therapeutics againstPathogens (Basel, Switzerland) · 2023Article
- ENO2-derived phosphoenolpyruvate functions as an endogenous inhibitor of HDAC1 and confers resistance to antiangiogenic therapy.Nature metabolism · 2023Article
- Comparative Pharmacology of a Bis-Pivaloyloxymethyl Phosphonate Prodrug Inhibitor of Enolase after Oral and Parenteral Administration.ACS pharmacology & translational science · 2023Article
- Paralog-based synthetic lethality: rationales and applications.Frontiers in oncology · 2023Review
- Prodrugs of a 1-Hydroxy-2-oxopiperidin-3-yl Phosphonate Enolase Inhibitor for the Treatment ofJournal of medicinal chemistry · 2022Article
- Metabolic collateral lethal target identification reveals MTHFD2 paralogue dependency in ovarian cancer.Nature metabolism · 2022Article
- Baicalein Acts against Candida albicans by Targeting Eno1 and Inhibiting Glycolysis.Microbiology spectrum · 2022Article
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Authors and funding
18 authors at 3 institutions in 1 country.
Funding
Abstract
Despite being crucial for energy generation in most forms of life, few if any microbial antibiotics specifically inhibit glycolysis. To develop a specific inhibitor of the glycolytic enzyme enolase 2 (ENO2) for the treatment of cancers with deletion of ENO1 (encoding enolase 1), we modeled the synthetic tool compound inhibitor phosphonoacetohydroxamate (PhAH) into the active site of human ENO2. A ring-stabilized analog of PhAH, in which the hydroxamic nitrogen is linked to Cα by an ethylene bridge, was predicted to increase binding affinity by stabilizing the inhibitor in a bound conformation. Unexpectedly, a structure-based search revealed that our hypothesized backbone-stabilized PhAH bears strong similarity to SF2312, a phosphonate antibiotic of unknown mode of action produced by the actinomycete Micromonospora, which is active under anaerobic conditions. Here, we present multiple lines of evidence, including a novel X-ray structure, that SF2312 is a highly potent, low-nanomolar inhibitor of enolase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.