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Structure — human OGDH E1 (shown in 3D)
Human 2-oxoglutarate dehydrogenase E1 (α-ketoglutarate dehydrogenase) holoenzyme bound to TPP and Mg²⁺ — 8I0K (Wang J et al., Mol Cell 2025, PMID:39889707). The TPP cofactor and its pocket residues (His311, Arg312, His513) come straight from this structure.
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Mechanism review — E1/E2/E3 catalysis
The α-KG dehydrogenase complex shares the PDH-complex architecture and mechanism (TPP decarboxylation → lipoyl transsuccinylation → FAD/NAD⁺ reoxidation) — Patel MS, Nemeria NS, Furey W & Jordan F, "The pyruvate dehydrogenase complexes: structure-based function and regulation", J Biol Chem 2014, PMID:24798336. E3 (DLD) is the identical enzyme in both complexes.
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Sequence
Human OGDH (E1) UniProt Q02218 · DLST (E2) UniProt P36957 · DLD (E3) UniProt P09622 · NCBI Gene 4967 (OGDH)
› The 3D protein is the real OGDH E1 holoenzyme (PDB 8I0K) with its genuine TPP / Mg²⁺. Substrates, products and the E2/E3 arm chemistry are drawn as compact schematic molecules posed at the active-site pocket and are labeled [schematic].