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Literature summary for 1.5.5.1 extracted from

  • Malecki, J.; Dahl, H.A.; Moen, A.; Davydova, E.; Falnes, P.O.
    The METTL20 homologue from Agrobacterium tumefaciens is a dual specificity protein-lysine methyltransferase that targets ribosomal protein L7/L12 and the beta subunit of electron transfer flavoprotein (ETFbeta) (2016), J. Biol. Chem., 291, 9581-9595 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloning of a putative ETF-QO orthologue, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus(DE3)-RIPL Agrobacterium tumefaciens
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus(DE3)-RIPL Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced electron-transferring flavoprotein + ubiquinone Homo sapiens
-
electron-transferring flavoprotein + ubiquinol
-
?
reduced electron-transferring flavoprotein + ubiquinone Agrobacterium tumefaciens
-
electron-transferring flavoprotein + ubiquinol
-
?
reduced electron-transferring flavoprotein + ubiquinone Agrobacterium tumefaciens C58 / ATCC 33970
-
electron-transferring flavoprotein + ubiquinol
-
?

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens A9CJL8
-
-
Agrobacterium tumefaciens C58 / ATCC 33970 A9CJL8
-
-
Homo sapiens Q16134
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIPL by nickel affinity chromatography in presence of FAD Homo sapiens
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIPL by nickel affinity chromatography in presence of FAD Agrobacterium tumefaciens

Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information although Agrobacterium tumefaciens ETF-mediated electron transfer to 2,6-DCIP is observed with a number of different dehydrogenases, the reduction of coenzyme Q1 through the DH/ETF/ETF-QO system is only observed with dimethylglycine dehydrogenase, but not with any of the tested Agrobacterium tumefaciens acyl-CoA dehydrogenases Agrobacterium tumefaciens ?
-
?
additional information the recombinant human enzyme is able to transfer electrons from the ETF protein from Agrobacterium tumefaciens strain C58 to 2,6-dichloroindophenol or coenzyme Q1 in an in vitro system Homo sapiens ?
-
?
additional information although Agrobacterium tumefaciens ETF-mediated electron transfer to 2,6-DCIP is observed with a number of different dehydrogenases, the reduction of coenzyme Q1 through the DH/ETF/ETF-QO system is only observed with dimethylglycine dehydrogenase, but not with any of the tested Agrobacterium tumefaciens acyl-CoA dehydrogenases Agrobacterium tumefaciens C58 / ATCC 33970 ?
-
?
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
-
Homo sapiens electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
-
?
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
-
Agrobacterium tumefaciens electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
-
?
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
-
Agrobacterium tumefaciens C58 / ATCC 33970 electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
-
Homo sapiens electron-transferring flavoprotein + reduced coenzyme Q1
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
-
Agrobacterium tumefaciens electron-transferring flavoprotein + reduced coenzyme Q1
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
-
Agrobacterium tumefaciens C58 / ATCC 33970 electron-transferring flavoprotein + reduced coenzyme Q1
-
?
reduced electron-transferring flavoprotein + ubiquinone
-
Homo sapiens electron-transferring flavoprotein + ubiquinol
-
?
reduced electron-transferring flavoprotein + ubiquinone
-
Agrobacterium tumefaciens electron-transferring flavoprotein + ubiquinol
-
?
reduced electron-transferring flavoprotein + ubiquinone
-
Agrobacterium tumefaciens C58 / ATCC 33970 electron-transferring flavoprotein + ubiquinol
-
?

Synonyms

Synonyms Comment Organism
ETF-QO
-
Homo sapiens
ETF-QO
-
Agrobacterium tumefaciens
ETF:quinone oxidoreductase
-
Homo sapiens
ETF:quinone oxidoreductase
-
Agrobacterium tumefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Homo sapiens
22
-
assay at room temperature Agrobacterium tumefaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Homo sapiens
7.2
-
assay at Agrobacterium tumefaciens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens
FAD
-
Agrobacterium tumefaciens
ubiquinone
-
Homo sapiens
ubiquinone
-
Agrobacterium tumefaciens
[4Fe-4S]-center
-
Homo sapiens
[4Fe-4S]-center
-
Agrobacterium tumefaciens

General Information

General Information Comment Organism
malfunction impairment of lysine-specific reduction of ETF reduces the ability of AtETF to mediate electron transfer between ETF-dependent dehydrogenases and ETF-QO Agrobacterium tumefaciens
physiological function electron-transferring flavoprotein, ETF, mediates transfer of electrons from several mitochondrial FAD-containing dehydrogenases to the ETF:quinone oxidoreductase, ETF-QO, leading to reduction of the quinone pool of the mitochondrial respiratory chain Homo sapiens
physiological function electron-transferring flavoprotein, ETF, mediates transfer of electrons from several mitochondrial FAD-containing dehydrogenases to the ETF:quinone oxidoreductase, ETF-QO, leading to reduction of the quinone pool of the mitochondrial respiratory chain Agrobacterium tumefaciens