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Literature summary for 1.2.1.105 extracted from

  • Shiio, I.; Ujigawa-Takeda, U.
    Presence and regulation of alphe-ketoglutarate dehydrogenase complex in a glutamate-producing bacterium Brevibacterium flavum (1980), Agric. Biol. Chem., 44, 1897-1904.
No PubMed abstract available
Search for more literature for 1.2.1.105

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA activates, 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
Cys activates, 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum

General Stability

General Stability Organism
2-oxoglutarate dehydrogenase complex is stabilized by glycerol, Mg2+ and thiamine diphosphate [Brevibacterium] flavum

Inhibitors

Inhibitors Comment Organism Structure
cis-aconitate 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
K+ 50 mM KCl, 63% inhibition of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
Na+ 50 mM NaCl, 34% inhibition of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
Na2HPO4 50 mM KCl, 38% inhibition of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
Na2SO4 50 mM KCl, 4.5% inhibition of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
NADH 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
NADPH 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
NH4+ 50 mM NH4Cl, 21% inhibition of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
oxalacetate 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
pyruvate 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
succinyl-CoA 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
Tris-HCl 50 mM, 26% inhibition of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.076
-
 2-oxoglutarate 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum
0.08
-
 2-oxoglutarate 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 7000000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, gel filtration [Brevibacterium] flavum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + lipoamide [Brevibacterium] flavum addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex S-succinyldihydrolipoamide + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
[Brevibacterium] flavum
-
-
-

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) [Brevibacterium] flavum
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 [Brevibacterium] flavum
a
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 mechanism of the enzyme complex is bi bi uni uni ping pong [Brevibacterium] flavum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + lipoamide
-
 [Brevibacterium] flavum S-succinyldihydrolipoamide + CO2
-
 ?
2-oxoglutarate + lipoamide addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum S-succinyldihydrolipoamide + CO2
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 7.7 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 pH 6.5: about 60% of maximal activity, pH 8.5: about 30% of maximal activity, 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate required , 2-oxoglutarate dehydrogenase complex [Brevibacterium] flavum