| Identification | Back Directory | [Name]
N-OXALYL GLYCINE | [CAS]
5262-39-5 | [Synonyms]
NOG
SYM1
SYNS1
N-OXALYL GLYINE
N-OXALYL GLYCINE
Human NOG Protein, Fc Tag
N-OXALYL GLYCINE USP/EP/BP
Human NOG Protein, His Tag
Glycine,N-(carboxycarbonyl)-
2-((Carboxymethyl)amino)-2-oxoacetic acid | [Molecular Formula]
C4H5NO5 | [MDL Number]
MFCD00913253 | [MOL File]
5262-39-5.mol | [Molecular Weight]
147.09 |
| Chemical Properties | Back Directory | [density ]
1.638±0.06 g/cm3(Predicted) | [storage temp. ]
Sealed in dry,Room Temperature | [solubility ]
deionized water: >10mg/mL | [form ]
solid | [pka]
2.83±0.20(Predicted) | [color ]
White to off-white | [Water Solubility ]
deionized water: >10mg/mL |
| Hazard Information | Back Directory | [Uses]
The jumonji domain-containing protein 2 (JMJD2) subfamily of histone demethylases have been shown to catalyze demethylation of the methylated forms of histone 3 lysine 9 (H3K9) and H3K36 in vitro and in cells. Because histone demethylases are implicated in certain diseases, including cancer, selective inhibitors are candidate anticancer agents as well as potential tools for elucidating the biological functions of JMJDs. N-Oxalylglycine, the amide analog of α-ketoglutarate, is a cell permeable inhibitor of α-ketoglutarate-dependent enzymes, including JMJD2A, JMJD2C, and JMJD2E (IC50s = 250, 500, and 24 μM, respectively). It can also inhibit the prolyl hydroxylase domain-containing proteins PHD1 and PHD2 with IC50 values of 2.1 and 5.6 μM, respectively.[Cayman Chemical] | [Definition]
ChEBI: An amino dicarboxylic acid that is iminodiacetic acid with an oxo substituent. It is used as an inhibitor of alpha-ketoglutarate dependent (EC 1.14.11.*) enzymes. | [Biological Activity]
n-oxalylglycine, as known as nog, is a cell permeable inhibitor of α-ketoglutarate-dependent enzymes which include jmjd2a, jmjd2c, and jmjd2e. nog also blocks the prolyl hydroxylase domain-containing proteins phd1 and phd2. demethylation of the methylated forms of histone 3 lysine 9 (h3k9) and h3k36 can be catalyzed by jmjd2 subfamily of histone demethylases. since histone demethylases are related to certain diseases, including cancer, selective inhibitors functions as anticancer agents and potential tools for clarifying the biological functions of jmjds. | [Biochem/physiol Actions]
N-Oxalylglycine is an inhibitor of α-ketoglutarate-dependent enzymes and mimics the initial steps but does not initiate the hydroxylation process. N-Oxalylglycine has been used to inhibit Jumonji C-domain-containing histone lysine demethylases. | [in vitro]
nog was identified as a natural product and presented in plants, including rheum rhabarbarum (rhubarb) and spinach oleracea (spinach) leaves. however, there was no nog observed human embryonic kidney cells (hek 293t) or escherchia coli. nog regulated gene expression via blocking 2-oxoglutarate-dependent oxygenases [1]. | [IC 50]
250 μm: inhibits α-ketoglutarate-dependent enzyme jumonji domain-containing protein 2 (jmjd2) a. | [storage]
Store at -20°C | [References]
[1]. al-qahtani, k., jabeen, b., sekirnik, r., riaz, n., claridge, t., schofield, c., & mccullagh, j. the broad spectrum 2-oxoglutarate oxygenase inhibitor n-oxalylglycine is present in rhubarb and spinach leaves. phytochemistry. 2015; 117: 456-461. |
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