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Oxoglutarate dehydrogenase

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2-oxoglutarate dehydrogenase E1 component (α-Ketoglutarate dehydrogenase)
Symbol(s): OGDH
Other names: Alpha-ketoglutarate dehydrogenase
Genetic data
Locus: Chr. 7 p13-p11.2
Gene type: protein coding
Protein Structure/Function
Molecular Weight: 115942 (Da)
Protein type: Enzyme: Dehydrogenase
Functions: converts Alpha ketoglutarate to succinyl CoA
Domains: Transketolase central region, Dehydrogenase E1 component
Other
Taxa expressing:Homo sapiens; homologs: ubiquitous among oxidatively respiring organisms
Cell types:ubiquitous among aerobic cells
Subcellular localization:mitochondrion, mitochondrial matrix
Pathway(s):Citric acid cycle, Lysine degradation, Tryptophan metabolism
Enzymatic Data
Catalytic activity:2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2)
Cofactor(s):Thiamine pyrophosphate
Enzyme Regulation:Catabolite repressed
Medical/Biotechnological data
Diseases:Alpha-Ketoglutarate Dehydrogenase Deficiency
Database Links
EC number: 1.2.4.2
Codes: EntrezGene 4967; Mendelian Inheritance in Man (OMIM) 203740; RefSeq NM_001003941; UniProt Q02218

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.


Contents

[edit] Properties

[edit] Nomenclature and classification

The official name of this enzyme is oxoglutarate dehydrogenase (OGDC) although it is also commonly known as α-ketoglutarate dehydrogenase (AKGDH).

  • CAS: 9031-02-1

[edit] Metabolic pathways

This enzyme participates in three different pathways:

[edit] Kinetic properties

The following values are from Azotobacter vinelandii (1):

  • KM: 0.14 ± 0.04 mM
  • Vmax : 9 ± 3 μmol.min-1.mg-1

[edit] Citric acid cycle

[edit] Reaction

The reaction catalyzed by this enzyme in the citric acid cycle is:

α-ketoglutarate + NAD+ + CoASuccinyl CoA + CO2 + NADH

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.

[edit] 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.

[edit] References

  1. 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.
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