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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.[1] 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.2 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).[3],[4],[5],[6] It can also inhibit the prolyl hydroxylase domain-containing proteins PHD1 and PHD2 with IC50 values of 2.1 and 5.6 μM, respectively.[4],[5],[6]

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