|-
| align="center" colspan="2" |
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| colspan="2" bgcolor="#dddddd" | Identifiers
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| bgcolor="#e7dcc3" | Symbol(s)
| bgcolor="#eeeeee" | [OGDH]
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| bgcolor="#e7dcc3" | Entrez
| bgcolor="#eeeeee" | [4967]
|- class="hiddenStructure"
| bgcolor="#e7dcc3" | OMIM
| bgcolor="#eeeeee" | [203740]
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| bgcolor="#e7dcc3" | RefSeq
| bgcolor="#eeeeee" | [NM_001003941]
|-
| bgcolor="#e7dcc3" | UniProt
| bgcolor="#eeeeee" | [Q02218]
|- class="hiddenStructure"
| bgcolor="#e7dcc3" | PDB
| bgcolor="#eeeeee" | []
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| colspan="2" bgcolor="#dddddd" | Other data
|- class="hiddenStructure"
| bgcolor="#e7dcc3" | EC number
| bgcolor="#eeeeee" | [1.2.4.2]
|-
| bgcolor="#e7dcc3" | Locus
| bgcolor="#eeeeee" | Chr. 7[p13-p11.2]
|-
|}
Oxoglutarate dehydrogenase (aka α-ketoglutarate dehydrogenase) is an enzyme (EC [1.2.4.2]) most commonly known for its role in the citric acid cycle. Much like pyruvate dehydrogenase, this enzyme forms a complex composed of three components: E1, E2 and E3, which use thiamine pyrophosphate, lipoic acid and FAD as coenzymes, respectively. In fact three classes of thesse multienzyme complexes have been characterized, one specific for pyruvate, a second specific for 2-oxoglutarate and a third specific branched-chain α-keto acids.
This reaction proceeds in three steps: decarboxylation of α-ketoglutarate, oxidation and subsequent transfer to CoA, which forms the end product, succinyl CoA. ΔG°' for this reaction is -7.2 kcal mol-1.
Regulation
Oxoglutarate dehydrogenase is a key control point in the citric acid cycle. It is inhibited by its products, succinyl CoA and NADH. A high energy charge in the cell will also be inhibitive.
References
Bunik V, Westphal AH, de Kok A: Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate. Eur J Biochem 2000; 267(12): 3583-91. PMID 10848975.
