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Literature summary extracted from

  • Watmough, N.J.; Frerman, F.E.
    The electron transfer flavoprotein: ubiquinone oxidoreductases (2010), Biochim. Biophys. Acta, 1797, 1910-1916.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.5.1 crystal structure analysis Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.5.1 mitochondrial inner membrane bound to via ubiquinone binding domain, overview Sus scrofa 5743
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.5.5.1 Fe2+ a [4Fe-4S]+1+2 cluster Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.5.1 reduced electron-transferring flavoprotein + ubiquinone Sus scrofa electron transfer via flavin cofactor electron-transferring flavoprotein + ubiquinol
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.5.5.1 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.5.1 kidney
-
Sus scrofa
-
1.5.5.1 liver
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.5.1 additional information mechanism of superoxide formation by ETF-QO, reduction potentials of redox centres, overview Sus scrofa ?
-
?
1.5.5.1 reduced electron-transferring flavoprotein + ubiquinone electron transfer via flavin cofactor Sus scrofa electron-transferring flavoprotein + ubiquinol
-
r

Synonyms

EC Number Synonyms Comment Organism
1.5.5.1 electron transfer flavoprotein: ubiquinone oxidoreductase
-
Sus scrofa
1.5.5.1 electron transfer flavoprotein:ubiquinone oxidoreductase
-
Sus scrofa
1.5.5.1 ETF-QO
-
Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.5.1 FAD the flavin serves as the immediate reductant of ubiquinone Sus scrofa

General Information

EC Number General Information Comment Organism
1.5.5.1 malfunction enzyme deficiency can cause multiple acyl-CoA dehydrogenase deficiency, MADD. The inability to oxidize fatty acids prevents the synthesis of ketone bodies, an essential alternate energy source for the heart. Affected individuals frequently die in early infancy with a severe, frequently fatal, metabolic acidosis that is often accompanied by a stress-induced hypertrophic cardiomyopathy and lipid accumulation in the heart, and secondary carnitine deficiency Sus scrofa
1.5.5.1 additional information the enzyme is a component of the mitochondrial respiratory chain that together with electron transfer flavoprotein (ETF) forms a short pathway that transfers electrons from 11 different mitochondrial flavoprotein dehydrogenases to the ubiquinone pool, ETF:QO enzyme structure and its quinone binding site, domain organisation, overview Sus scrofa