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Literature summary extracted from

  • Bunik, V.; Westphal, A.H.; 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 (2000), Eur. J. Biochem., 267, 3583-3591.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.105 2-oxoglutarate substrate inhibition above 4 mM Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.105 additional information
-
 additional information two substrate-binding modes are revealed at different degrees of saturation of the enzyme with 2-oxoglutarate. At low substrate concentrations, 0.001-0.01 mM, the binding mainly depends on the interaction of the enzyme with the substrate carbonyl groups. At 0.1-1 mM the relative contribution of the 2-oxo group in the binding increases Azotobacter vinelandii
1.2.1.105 0.15
-
 2-oxoglutarate
-
 Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.105 103000
-
 x * 103000, 2-oxoglutarate dehydrogenase subunit, SDS-PAGE Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.105 Azotobacter vinelandii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.105 2-oxoglutarate dehydrogenase complex Azotobacter vinelandii

Reaction

EC Number Reaction Comment Organism Reaction ID
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 Azotobacter vinelandii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.105 additional information
-
 specific activity of the 2-oxoglutarate dehydrogenase complex Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + lipoamide
-
 Azotobacter vinelandii S-succinyldihydrolipoamide + CO2
-
 ?
1.2.1.105 additional information enzyme complex is also active with 2-oxoadipate Azotobacter vinelandii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.105 ? x * 103000, 2-oxoglutarate dehydrogenase subunit, SDS-PAGE Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.105 thiamine diphosphate formation of a precatalytic complex SE between the substrate and the 2-oxoglutarate dehydrogenase component before the catalytic complex ES, in which the substrate is added to the thiamin diphosphate cofactor Azotobacter vinelandii