Domain mappings support broad catalysis and FAD binding, with direct biochemical corroboration.

The mitochondrial IBD lies on the human target lineage.

The mapping supplies a broad mitochondrial location, not direct matrix resolution.

Human cell imaging supports mitochondrial residence without isoform resolution.

The human target matches the nonsaccharomycete alternative of the current rule.

Rat purification and human expression establish D-2-hydroxyglutarate oxidation; additional substrate and ion effects are biochemical observations.

Human disease variants markedly impair the measured enzyme activity.

Mutant overexpression in mild D-2-hydroxyglutaric aciduria shows reduced enzyme activity.

D2HGDH mutations were detected in 24 of 50 patients; all mutation-positive patients had impaired enzyme activity, and patients with normal enzyme activity had no detected mutations.

The D2HGDH N terminus confers degradation susceptibility and supports inhibitor-triggered activation of an engineered CARD8 fusion.

Human structural and mutational evidence defines the catalytic pocket and discriminates measured additional substrate activities.

Human multistrategy proteomics supports mitochondrial localization and peripheral association.

D2HGDH catalyzes D-2-hydroxyglutarate oxidation in the curated matrix reaction.

The pathway includes D2HGDH-mediated formation of 2-oxoglutarate.

Authored navigation to primary sources, literal target table cells and database assertions; not independent experimental support.

Authored navigation to matrix, cofactor and mutant-assay originals; not an independent experiment.