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Literature summary for 1.5.5.1 extracted from

  • Alves, E.; Henriques, B.J.; Rodrigues, J.V.; Prudencio, P.; Rocha, H.; Vilarinho, L.; Martinho, R.G.; Gomes, C.M.
    Mutations at the flavin binding site of ETF:QO yield a MADD-like severe phenotype in Drosophila (2012), Biochim. Biophys. Acta, 1822, 1284-1292.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene CG12140, mapping and cloning of ETF:QO alleles, expression of the two subunits ETFA and ETFB in Escherichia coli strain BL21 Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
additional information three independent mutant alleles, corresponding to three distinct point mutations in ETF:QO, are lethal as a result of a specific knockdown of FAD binding by direct disruption of the cofactor binding motif within the nucleotide binding Rossmann fold, a nucleotide binding structural domain also present in ETF:QO, which comprises a beta-strand connected by a short loop to an alpha-helix, and includes an expanded sequence motif (V/IxGx1–2GxxGxxxG/A) that affords both FAD binding and stabilisation of the secondary structure elements involved, overview Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced electron-transferring flavoprotein + ubiquinone Drosophila melanogaster
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electron-transferring flavoprotein + ubiquinol
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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gene CG12140
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information assay method uses dichlorophenolindophenol, DCPIP, as substrate Drosophila melanogaster ?
-
?
reduced electron-transferring flavoprotein + ubiquinone
-
Drosophila melanogaster electron-transferring flavoprotein + ubiquinol
-
?

Synonyms

Synonyms Comment Organism
electron transfer flavoprotein:ubiquinone oxidoreductase
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Drosophila melanogaster
ETF:QO
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Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Drosophila melanogaster

Cofactor

Cofactor Comment Organism Structure
FAD
-
Drosophila melanogaster

General Information

General Information Comment Organism
malfunction ETF:QO mutant alleles faileto identify developmental defects, but a complete dysfunction of the ETF:QO protein leads to abnormal mitochondrial fatty acid oxidation. Acylcarnitine levels in ETF:QO mutant embryos display a profile typical of MADD, i.e. multiple acyl-CoA dehydrogenase deficiency, a metabolic disease of bet-oxidation, with a broad range of clinical phenotypes, varying from embryonic lethal to mild forms in humans. Fly mutant phentypes, overview Drosophila melanogaster
additional information the Rossmann fold is a nucleotide binding structural domain present in ETF:QO, it comprises a beta-strand connected by a short loop to an alpha-helix, and includes an expanded sequence motif (V/IxGx1-2GxxGxxxG/A) that affords both FAD binding and stabilisation of the secondary structure elements involved Drosophila melanogaster
physiological function the enzyme is maternally required for Drosophila embryogenesis Drosophila melanogaster