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Literature summary for 1.2.1.105 extracted from

  • Habelhah, H.; Laine, A.; Erdjument-Bromage, H.; Tempst, P.; Gershwin, M.E.; Bowtell, D.D.; Ronai, Z.
    Regulation of 2-oxoglutarate (alpha-ketoglutarate) dehydrogenase stability by the RING finger ubiquitin ligase Siah (2004), J. Biol. Chem., 279, 53782-53788.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
FLAG-tagged enzyme expression in siah2-/- cells and siah2+/+ cells in mitochondria and, by disruption of the mitochondrial targeting sequence, in cytoplasm, in the cytoplasm the enzyme is rapidly proteasome-dependently degraded, overvexpression of hemagglutinin-labeled enzyme E2 in 293T cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information siah2 is the RING finger ubiquitin-protein isopeptide ligase 2, 2-oxoglutarate dehydrogenase component E2 expression and activity are elevated in siah2-/- cells deficient in siah2 expression compared to siah2+/+ cells Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane enzyme E2 overexpression or disruption of mitochondrial membrane potential causes enzyme E2 release from mitochondria to cytoplasm where it is degraded Homo sapiens 5743
-
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
x * 52000, E2, SDS-PAGE Homo sapiens

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 enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
ir
additional information Homo sapiens the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2 ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification enzyme contains a mitochondrial targeting sequence which is cleaved off in the mitochondria resulting in the mature enzyme Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293T cell
-
Homo sapiens
-
HeLa cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
ir
additional information the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2 Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
? x * 52000, E2, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
2-oxoglutarate dehydrogenase complex
-
Homo sapiens
alpha-ketoglutarate dehydrogenase complex
-
Homo sapiens
OGHDC-E2 component of the 2-oxoglutarate dehydrogenase multienzyme complex Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
thiamine diphosphate
-
Homo sapiens