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Literature summary for 1.2.4.2 extracted from

  • Nemeria, N.S.; Gerfen, G.; Guevara, E.; Nareddy, P.R.; Szostak, M.; Jordan, F.
    The human Krebs cycle 2-oxoglutarate dehydrogenase complex creates an additional source of superoxide/hydrogen peroxide from 2-oxoadipate as alternative substrate (2017), Free Radic. Biol. Med., 108, 644-654 .
    View publication on PubMed
Search for more literature for 1.2.4.2

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition of enzyme-specific activity is observed at concentrations of 2-oxoadipate up to 8 mM Homo sapiens

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Homo sapiens
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens Q02218 E1 component of the 2-oxoglutarate dehydrogenase complex
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoadipate + 2,6-dichlorophenolindophenol
-
 Homo sapiens ? + reduced 2,6-dichlorophenolindophenol
-
 ?
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
-
 ?
2-oxoglutarate + 2,6-dichlorophenolindophenol
-
 Homo sapiens ? + reduced 2,6-dichlorophenolindophenol
-
 ?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?

Synonyms

Synonyms Comment Organism
2-oxoglutarate dehydrogenase complex
-
 Homo sapiens
E1o
-
 Homo sapiens
OGDH
-
 Homo sapiens
OGDHC
-
 Homo sapiens
ThDP-dependent 2-oxoglutarate dehydrogenase
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5
-
 2-oxoadipate enzyme-specific activity, pH 7.5, 37°C Homo sapiens
3.6
-
 2-oxoadipate overall-assay, pH 7.5, 37°C Homo sapiens
4.2
-
 2-oxoglutarate enzyme-specific activity, pH 7.5, 37°C Homo sapiens
18.4
-
 2-oxoglutarate overall-assay, pH 7.5, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism the enzyme creates an additional source of superoxide/hydrogen peroxide from 2-oxoadipate as alternative substrate Homo sapiens
physiological function the OGDH complex behaves as a 2-oxoadipate dehydrogenase, in addition to its usual 2-oxoglutarate dehydrogenase activity. Human E1o by itself and when assembled into the OGDH complex can serve as a source of superoxide/H2O2 generation in mitochondria from 2-oxoadipate. A H2O2 generating activity from 2-oxoadipate of 2.668 nmol/min/mg hE1o is estimated for assembled OGDH complex and is more than 7fold higher than that with 2-oxoglutarate Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7
-
 2-oxoadipate overall-assay, pH 7.5, 37°C Homo sapiens
12.9
-
 2-oxoadipate enzyme-specific activity, pH 7.5, 37°C Homo sapiens
123
-
 2-oxoglutarate overall-assay, pH 7.5, 37°C Homo sapiens
247
-
 2-oxoglutarate enzyme-specific activity, pH 7.5, 37°C Homo sapiens