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Literature summary for 1.5.5.1 extracted from

  • Swanson, M.A.; Kathirvelu, V.; Majtan, T.; Frerman, F.E.; Eaton, G.R.; Eaton, S.S.
    Electron transfer flavoprotein domain II orientation monitored using double electron-electron resonance between an enzymatically reduced, native FAD cofactor, and spin labels (2011), Protein Sci., 20, 610-620.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.5.1

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
-
 Paracoccus denitrificans 5743
-
mitochondrial inner membrane
-
 Homo sapiens 5743
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced electron-transferring flavoprotein + ubiquinone Paracoccus denitrificans via FAD electron-transferring flavoprotein + ubiquinol
-
 ?
reduced electron-transferring flavoprotein + ubiquinone Homo sapiens via FAD electron-transferring flavoprotein + ubiquinol
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Paracoccus denitrificans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced electron-transferring flavoprotein + ubiquinone via FAD Paracoccus denitrificans electron-transferring flavoprotein + ubiquinol
-
 ?
reduced electron-transferring flavoprotein + ubiquinone via FAD Homo sapiens electron-transferring flavoprotein + ubiquinol
-
 ?

Synonyms

Synonyms Comment Organism
electron transfer flavoprotein ubiquinone oxidoreductase
-
 Paracoccus denitrificans
electron transfer flavoprotein ubiquinone oxidoreductase
-
 Homo sapiens
ETF-QO
-
 Paracoccus denitrificans
ETF-QO
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD bound by the C-terminal region of the alpha-subunit (domain II) of electron transfer flavoprotein Paracoccus denitrificans
FAD bound by the C-terminal region of the alpha-subunit (domain II) of electron transfer flavoprotein Homo sapiens

General Information

General Information Comment Organism
malfunction defects in human electron transfer flavoprotein or ETF-QO result in a metabolic disease known as multiple acyl-CoA dehydrogenation deficiency (MADD) or glutaric acidemia type 2. Death within the neonatal period occurs if the defects are severe Homo sapiens
additional information electron transfer flavoprotein structure analysis and FAD binding of wild-type and mutants, i.e. alphaA210C, betaA111C, betaA111C/E162A, and alphaA43C, overview Paracoccus denitrificans
additional information electron transfer flavoprotein structure analysis and FAD binding, overview Homo sapiens
physiological function in the mitochondrial matrix, the oxidation of fatty acids and several amino acids including lysine, leucine, valine, and isoleucine is coupled to the main mitochondrial respiratory chain through an electron transfer pathway involving electron transfer flavoprotein, electron transfer flavoprotein ubiqunone oxidoreductase, i.e. ETF-QO, and ubiquinone. Electron transfer flavoprotein contains a flavin adenine dinucleotide cofactor FAD that accepts electrons from 10 flavoprotein dehydrogenases, and transfers them to ETF-QO in the inner mitochondrial membrane. Electrons enter ETF-QO through its [4Fe-4S]-1+21 iron-sulfur cluster, are transferred to an FAD, and finally to ubiquinone Paracoccus denitrificans
physiological function in the mitochondrial matrix, the oxidation of fatty acids and several amino acids including lysine, leucine, valine, and isoleucine is coupled to the main mitochondrial respiratory chain through an electron transfer pathway involving electron transfer flavoprotein, electron transfer flavoprotein ubiqunone oxidoreductase, i.e. ETF-QO, and ubiquinone. Electron transfer flavoprotein contains a flavin adenine dinucleotide cofactor FAD that accepts electrons from 10 flavoprotein dehydrogenases, and transfers them to ETF-QO in the inner mitochondrial membrane. Electrons enter ETF-QO through its [4Fe-4S]-1+21 iron-sulfur cluster, are transferred to an FAD, and finally to ubiquinone Homo sapiens