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Literature summary extracted from

  • Pettit, F.H.; Hamilton, L.; Munk, P.; Namihira, G.; Eley, M.H.; Willms, C.R.; Reed, L.J.
    alpha-Keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex (1973), J. Biol. Chem., 248, 5282-5290.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.105 additional information
-
 2470000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, sucrose density gradient centrifugation Escherichia coli
1.2.1.105 190000
-
 2-oxoglutarate dehydrogenase component, equilibrium sedimentation Escherichia coli
2.3.1.61 1000000
-
 sucrose density gradient centrifugation, sedimentation equilibrium Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.61 succinyl-CoA + dihydrolipoamide Escherichia coli
-
 CoA + S-succinyldihydrolipoamide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.105 Escherichia coli
-
-
-
2.3.1.61 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4) Escherichia coli
a
1.2.1.105 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + lipoamide
-
 Escherichia coli S-succinyldihydrolipoamide + CO2
-
 ?
2.3.1.61 succinyl-CoA + dihydrolipoamide
-
 Escherichia coli CoA + S-succinyldihydrolipoamide
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.105 More in solution at pH 7.0, the 2-oxoglutarate dehydrogenase component exists as a stable dimer Escherichia coli
2.3.1.61 polymer made up of 24 similar structurally identical polypeptide chains Escherichia coli
2.3.1.61 polymer 24 * 47000-51000, SDS-PAGE Escherichia coli
2.3.1.61 polymer 24 * 39000-42000, sedimentation equilibrium analysis Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.61 Lipoyl-protein transsuccinylase core consists of 24 similar polypeptide chains, 12 of these chains contain a covalently bound lipoyl moiety Escherichia coli