Date published: 2025-10-15

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N-Oxalylglycine (CAS 5262-39-5)

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Alternate Names:
NOG; N-(carboxycarbonyl)-glycine
Application:
N-Oxalylglycine is a competitive inhibitor of prolyl 4-hydroxylase
CAS Number:
5262-39-5
Purity:
≥98%
Molecular Weight:
147.1
Molecular Formula:
C4H5NO5
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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N-Oxalylglycine is a compound that functions as a competitive inhibitor of 2-oxoglutarate-dependent dioxygenases. It acts by chelating the active site iron, thereby preventing the binding of the co-substrate and inhibiting the enzymatic activity. N-Oxalylglycine′s mechanism of action involves disrupting the catalytic cycle of 2-oxoglutarate-dependent dioxygenases, which are involved in various biological processes such as DNA and histone demethylation, as well as hypoxic response pathways. By interfering with the enzymatic activity of these dioxygenases, N-Oxalylglycine can be used to investigate the specific roles of these enzymes in cellular processes and signaling pathways. Its ability to competitively inhibit the active site iron may be useful for studying the molecular mechanisms underlying the functions of 2-oxoglutarate-dependent dioxygenases in various experimental applications.


N-Oxalylglycine (CAS 5262-39-5) References

  1. Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase, TauD.  |  Kalliri, E., et al. 2005. Biochem Biophys Res Commun. 338: 191-7. PMID: 16165092
  2. Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors.  |  Hamada, S., et al. 2009. Bioorg Med Chem Lett. 19: 2852-5. PMID: 19359167
  3. Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors.  |  Volke, M., et al. 2009. PLoS One. 4: e7875. PMID: 19924283
  4. Force field design and molecular dynamics simulations of factor-inhibiting HIF-1 and its complex with known inhibitors: implications for rational inhibitor design.  |  Park, H., et al. 2010. J Mol Graph Model. 29: 221-8. PMID: 20663694
  5. The broad spectrum 2-oxoglutarate oxygenase inhibitor N-oxalylglycine is present in rhubarb and spinach leaves.  |  Al-Qahtani, K., et al. 2015. Phytochemistry. 117: 456-461. PMID: 26196940
  6. Novel label-free electrochemical strategy for sensitive determination of ten-eleven translocation protein 1.  |  Yu, Z., et al. 2021. Anal Chim Acta. 1146: 140-145. PMID: 33461709
  7. A novel series of putative Brugia malayi histone demethylase inhibitors as potential anti-filarial drugs.  |  Kreiss, T., et al. 2022. PLoS Negl Trop Dis. 16: e0010216. PMID: 35294431
  8. Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.  |  Chowdhury, R., et al. 2022. Sci Rep. 12: 6065. PMID: 35410347
  9. Publisher Correction: MOG analogues to explore the MCT2 pharmacophore, α-ketoglutarate biology and cellular effects of N-oxalylglycine.  |  Fets, L., et al. 2022. Commun Biol. 5: 1019. PMID: 36167803
  10. Structural analysis of the 2-oxoglutarate binding site of the circadian rhythm linked oxygenase JMJD5.  |  Islam, MS., et al. 2022. Sci Rep. 12: 20680. PMID: 36450832
  11. A high-throughput effector screen identifies a novel small molecule scaffold for inhibition of ten-eleven translocation dioxygenase 2.  |  Palei, S., et al. 2022. RSC Med Chem. 13: 1540-1548. PMID: 36545435
  12. Formaldehyde reacts with N-terminal proline residues to give bicyclic aminals.  |  John, T., et al. 2023. Commun Chem. 6: 12. PMID: 36698022
  13. Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66.  |  Türkmen, VA., et al. 2023. RSC Chem Biol. 4: 235-243. PMID: 36908702

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

N-Oxalylglycine, 10 mg

sc-202720
10 mg
$52.00

N-Oxalylglycine, 100 mg

sc-202720A
100 mg
$150.00