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Literature summary for 1.2.1.105 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 1.2.1.105

Localization

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

Organism UniProt Comment Textmining
Homo sapiens A0A024R713 and A0A024R6C9 and Q02218 A0A024R713 i.e dihydrolipoyl dehydrogenase component E3, cf. EC 1.8.1.4, A0A024R6C9 i.e. dihydrolipoyllysine-residue succinyltransferase component E2, cf. EC 2.3.1.61, Q02218 i.e. 2-oxoglutarate dehydrogenase component hE1o, cf. EC 1.2.4.2
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Homo sapiens Q02218 E1 component of the 2-oxoglutarate dehydrogenase complex, cf. EC 1.2.4.2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoadipate + CoA + NAD+
-
 Homo sapiens glutaryl-CoA + CO2 + NADH
-
 ?
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
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 Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
-
 ?
2-oxoglutarate + CoA + NAD+
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 Homo sapiens succinyl-CoA + CO2 + NADH
-
 ?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
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 Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?

Synonyms

Synonyms Comment Organism
E1o
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 Homo sapiens
OGDH cf. EC 1.2.4.2 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

General Information

General Information Comment Organism
metabolism hE1o can also utilize 2-oxoadipate (OA) as a substrate. Both E1o-specific and overall complex activities (NADH production) are detected using OA as a substrate. hE1o forms the thiamine diphosphate-enamine and the C2alpha-hydroxyalkyl-thiamine diphosphate with nearly identical rates for 2-oxoglutarate OG and OA, and both OG and OA can reductively acylate lipoyl domain created from dihydrolipoyl succinyltransferase (E2o). Dioxygen can oxidize the thiamine diphosphate-derived enamine from both OG and OA, leading to thiamine diphosphate-enamine radical and generation of superoxide and H2O2. The efficiency of superoxide/H2O2 production is 7-times larger from OA than from OG 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