. 2011 Apr 1;12(5):463–469. doi: 10.1038/embor.2011.43

Table 1. Inhibition of human 2OG oxygenases by R- and S-2HG.

Enzyme	IC₅₀±s.e.m. (μM)
	R-2HG	S-2HG	NOG
FIH	1,500±400^*	189±34	46±8
PHD2	7,300±3,300^*	419±150	0.8±0.2
JMJD2A	24±2 (17±4)	26±3 (33±5)	17±2 (20±3)
JMJD2C	79±7	97±24	14±3
FBXL11	106±22	48±15	252±50
ABH2	424±77	150±20	10±2
BBOX1	13,200±1,100	142±30 (96±10)	19±2
Substrates used in the assays for JMJD2A/JMJD2C, FBXL11, BBOX1, PHD2, FIH and ABH2 were histone H3 fragment substrates H3(7–14)K9me₃ and H3(30–41)K36me₂, γ-butyrobetaine, HIF1αCODD (residues 556–574), HIF1αCAD (residues 786–826) and GCXAGGTCCCGTAGTGCG, where X is 1-methyladenylate, respectively. See Fig 1 for dose–response curves and supplementary Table S1 online for the standard assay conditions used for the individual enzymes. Italicized IC₅₀ values in parentheses were determined at 10-fold higher Fe(II) concentration than the standard assay conditions. ^*Partial dose–response curves.
ABH2, AlkB homologue 2; BBOX1, γ-butyrobetaine hydroxylase 1; FIH, factor inhibiting-hypoxia-inducible factor; HIF, hypoxia-inducible factor; NOG, N-oxalylglycine; 2OG, 2-oxoglutarate; PHD2, prolyl hydroxylase 2; R-2HG, R-enantiomer of 2-hydroxyglutarate; IC₅₀, half-maximal inhibitory concentration.