The mutant enzyme acquires the activity to convert α-KG to D-2-hydroxyglutarate (D-2-HG), an oncometabolite that competitively inhibits the α-KG dependent enzymes by the high structural similarities.13 Processes involved in chondrosarcoma progression make these cells independent of the mutant IDH enzymes, as treatment with AGI-5198, a specific IDH1 mutant inhibitor, did not influence the tumourigenic properties of these cells.14 Therefore, we propose to exploit the metabolic vulnerability caused by the IDH1/2 mutations as therapeutic strategy for chondrosarcoma. The gene discussed is IDH2; the disease is chondrosarcoma.