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Literature summary for 1.2.1.105 extracted from

  • Weitzman, P.D.J.
    Regulation of alpha-ketoglutarate dehydrogenase activity in Acinetobacter (1972), FEBS Lett., 22, 323-326.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP stimulates 2-oxoglutarate dehydrogenase complex Acinetobacter sp.
AMP stimulates 2-oxoglutarate dehydrogenase complex Acinetobacter sp.

Inhibitors

Inhibitors Comment Organism Structure
NADH 0.1 mM, 50% inhibition. 0.2 mM AMP completely overcomes the inhibition Acinetobacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.27
-
2-oxoglutarate in presence of 0.2 mM AMP Acinetobacter sp.
0.43
-
2-oxoglutarate in presence of 0.2 M ADP Acinetobacter sp.
2.5
-
2-oxoglutarate in absence of added nucleotide Acinetobacter sp.

Organism

Organism UniProt Comment Textmining
Acinetobacter sp.
-
-
-
Acinetobacter sp. 4B
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Acinetobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + lipoamide
-
Acinetobacter sp. S-succinyldihydrolipoamide + CO2
-
?
2-oxoglutarate + lipoamide
-
Acinetobacter sp. 4B S-succinyldihydrolipoamide + CO2
-
?