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Literature summary for 1.2.1.105 extracted from

  • Sheu, K.F.R.; Blass, J.P.
    The alpha-ketoglutarate dehydrogenase complex (1999), Ann. N. Y. Acad. Sci., 893, 61-78.
    View publication on PubMed
Search for more literature for 1.2.1.105

Activating Compound

Activating Compound Comment Organism Structure
spermine enhances activity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
4-hydroxy-2-nonenal
-
 Homo sapiens
H2O2
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4
-
 2-oxoglutarate
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ Ca2+ and Mg2+ together synergistically reduce the Km-value for 2-oxoglutarate by over 10fold Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + lipoamide Saccharomyces cerevisiae
-
 S-succinyldihydrolipoamide + CO2
-
 ?
2-oxoglutarate + lipoamide Homo sapiens the 2-oxoglutarate dehydrogenase complex catalyzes a critical step in the Krebs tricarboxylic acid cycle, which is also a step in the metabolism of the potentially excitotoxic neurotransmitter glutamate. Deficiencies of the 2-oxoglutarate dehydrogenase complex are likely to impair energy metabolism and therfore brain function, and lead to manifestations of brain disease. Neurons that are enriched in the 2-oxoglutarate dehydrogenase complex may be selectively vulnerable in Alzheimer‘s disease. Variations in 2-oxoglutarate dehydrogenase complex that are not deleterious during reproductive life become deleterious with aging, perhaps by predisposing this mitochondrial metabolon to oxidative damage S-succinyldihydrolipoamide + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

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 Homo sapiens
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 Saccharomyces cerevisiae
a

Source Tissue

Source Tissue Comment Organism Textmining
brain neurons that appear slectively vulnerable in human temporal cortex in Alzheimer's disease are enriched in the 2-oxoglutarate dehydrogenase complex Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + lipoamide
-
 Saccharomyces cerevisiae S-succinyldihydrolipoamide + CO2
-
 ?
2-oxoglutarate + lipoamide reaction is physiologically irreversible, due to the volatility of CO2 Homo sapiens S-succinyldihydrolipoamide + CO2
-
 ir
2-oxoglutarate + lipoamide the 2-oxoglutarate dehydrogenase complex catalyzes a critical step in the Krebs tricarboxylic acid cycle, which is also a step in the metabolism of the potentially excitotoxic neurotransmitter glutamate. Deficiencies of the 2-oxoglutarate dehydrogenase complex are likely to impair energy metabolism and therfore brain function, and lead to manifestations of brain disease. Neurons that are enriched in the 2-oxoglutarate dehydrogenase complex may be selectively vulnerable in Alzheimer‘s disease. Variations in 2-oxoglutarate dehydrogenase complex that are not deleterious during reproductive life become deleterious with aging, perhaps by predisposing this mitochondrial metabolon to oxidative damage Homo sapiens S-succinyldihydrolipoamide + CO2
-
 ?

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
 Saccharomyces cerevisiae
thiamine diphosphate thiamine diphosphate is tightly but not covalently bound to the 2-oxoglutarate dehydrogenase component Homo sapiens