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Literature summary for 1.3.5.1 extracted from

  • Rutter, J.; Winge, D.R.; Schiffman, J.D.
    Succinate dehydrogenase - Assembly, regulation and role in human disease (2010), Mitochondrion, 10, 393-401.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Tcm62 importance in SDH assembly Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
genes encoding subunits SdhC, SdhD, and SdhB are located at 1q21,11q23, and 1p35-36.1 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane the membrane domain consists of two subunits SdhC and SdhD. The membrane domain contains a bound heme b moiety at the subunit interface with SdhC and SdhD each providing one of the two axial His ligands Homo sapiens 5743
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center, heme b Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinate + FAD Homo sapiens
-
fumarate + FADH2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinate + FAD
-
Homo sapiens fumarate + FADH2
-
?

Subunits

Subunits Comment Organism
More the catalytic core SdhA and SdhB subunits contain the redox cofactors that participate in electron transfer to ubiquinone. Sdh1 contains the covalently bound FAD cofactor and the binding site for succinate. Sdh2 contains the three Fe-S centers that mediate electron transfer to ubiquinone in the complex of succinate-ubiquinone dehydrogenase, EC 1.3.5.1, regulation of SDH, overview.The membrane domain consists of two subunits SdhC and SdhD. The membrane domain contains a bound heme b moiety at the subunit interface with SdhC and SdhD each providing one of the two axial His ligands Homo sapiens

Synonyms

Synonyms Comment Organism
SDH
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens
Fe-S center the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center Homo sapiens
heme b
-
Homo sapiens