Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Meixner-Monori, B.; Kubicek, C.P.; Habison, A.; Kubicek-Pranz, E.M.; Roehr, M.
    Presence and regulation of the alpha-ketoglutarate dehydrogenase multienzyme complex in the filamentous fungus Aspergillus niger (1985), J. Bacteriol., 161, 265-271.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
1.2.1.105 2-oxoglutarate stabilizes against dilution Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.105 cis-aconitate 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 K+ 50 mM, 56% inhibition, 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 Na+ 50 mM, 48% inhibition, 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 NADH 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 NH4+ 50 mM, 70% inhibition, 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 oxalacetate 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 succinate 2-oxoglutarate dehydrogenase complex Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.105 0.4
-
 2-oxoglutarate
-
 Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.105 Aspergillus niger
-
-
-

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 Aspergillus niger
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.105 mycelium highest activity found in rapidly growing mycelium, glucose-NH4+ or glucose-peptone medium Aspergillus niger
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + lipoamide
-
 Aspergillus niger S-succinyldihydrolipoamide + CO2
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.105 8
-
 2-oxoglutarate dehydrogenase complex Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.105 7 8.5 pH 7.0: about 70% of maximal activity, pH 8.5: about 70% of maximal activity, 2-oxoglutarate dehydrogenase complex Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.105 thiamine diphosphate required , 2-oxoglutarate dehydrogenase complex Aspergillus niger
1.2.1.105 thiamine diphosphate Km: 0.3 mM Aspergillus niger