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Literature summary for 1.2.1.105 extracted from

  • Heckert, L.L.; Butler, M.H.; Reimers, J.M.; Albe, K.R.; Wright, B.E.
    Purification and characterization of the 2-oxoglutarate dehydrogenase complex from Dictyostelium discoideum (1989), J. Gen. Microbiol., 135, 155-161.
    View publication on PubMed
Search for more literature for 1.2.1.105

Activating Compound

Activating Compound Comment Organism Structure
AMP stimulates 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum
GMP activates 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum
GTP activates 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum
UDP activates 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum
UTP activates 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum

Inhibitors

Inhibitors Comment Organism Structure
ATP 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum
NADH
-
 Dictyostelium discoideum
succinyl-CoA
-
 Dictyostelium discoideum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
 2-oxoglutarate
-
 Dictyostelium discoideum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Dictyostelium discoideum 5739
-

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2-oxoglutarate dehydrogenase complex Dictyostelium discoideum

Reaction

Reaction Comment Organism Reaction ID
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) Dictyostelium discoideum
a
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 Dictyostelium discoideum
a

Source Tissue

Source Tissue Comment Organism Textmining
additional information tenfold increase in 2-oxoglutarate dehydrogenase complex activity between the amoeba stage and the aggregation stage, 2fold increase between the aggregation stage and the sorocarp stage Dictyostelium discoideum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 specific activity of the 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + lipoamide
-
 Dictyostelium discoideum S-succinyldihydrolipoamide + CO2
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.004
-
 succinyl-CoA 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum
0.018
-
 NADH 2-oxoglutarate dehydrogenase complex Dictyostelium discoideum