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Information on EC 1.5.5.1 - electron-transferring-flavoprotein dehydrogenase
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1.5.5.1 electron-transferring-flavoprotein dehydrogenaseIUBMB Comments
An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.
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Word Map
- 1.5.5.1
- acyl-coa
- riboflavin
-
glutaric
- dehydrogenases
- flavin
- myopathy
-
late-onset
- carnitine
-
dehydrogenation
- acylcarnitine
- acidemia
-
riboflavin-responsive
-
beta-oxidation
- semiquinone
-
acyl-coenzyme
- butyryl-coa
- paracoccus
- isovaleryl-coa
- glutaryl-coa
-
ethylmalonic
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
electron transfer flavoprotein, etfdh, etf-qo, etf:qo, electron transfer flavoprotein dehydrogenase, etf dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase, etf-ubiquinone oxidoreductase, electron transfer flavoprotein:ubiquinone oxidoreductase, electron-transferring-flavoprotein dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BCAL1468
BCAS0609
electron flavoprotein reductase
-
-
-
-
electron transfer flavoprotein dehydrogenase
electron transfer flavoprotein Q oxidoreductase
-
-
-
-
electron transfer flavoprotein ubiquinone oxidoreductase
electron transfer flavoprotein-ubiquinone oxidoreductase
electron transfer flavoprotein:ubiquinone oxidoreductase
electron-transfer flavoprotein-2,3-dimethoxy-5-methyl-1,4-benzoquinone oxidoreductase
-
-
Electron-transferring-flavoprotein dehydrogenase
ETF dehydrogenase
ETF-QO
ETF-ubiquinone oxidoreductase
ETF:QO
ETF:quinone oxidoreductase
ETF:ubiquinone oxidoreductase
-
-
-
-
EtfA2
ETFDH
ETFDH1
ETFDH2
electron transfer flavoprotein dehydrogenase
-
-
-
-
electron transfer flavoprotein-ubiquinone oxidoreductase
-
-
-
-
electron transfer flavoprotein-ubiquinone oxidoreductase
-
-
Electron-transferring-flavoprotein dehydrogenase
-
-
-
-
ETF dehydrogenase
-
-
-
-
ETF-QO
-
-
-
-
ETF-ubiquinone oxidoreductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
-
-
-
-
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
electrostatic interaction between enzyme and electron-transferring flavoprotein
-
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
when enzyme is reduced to a two-electron reduced state, with one electron at each redox center, it is primed to reduce ubiquinone via FAD
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
electron-transferring-flavoprotein:ubiquinone oxidoreductase
An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.
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CAS REGISTRY NUMBER
COMMENTARY
86551-03-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + ubiquinol
semiquinone electron transferring flavoprotein + ubiquinone
-
-
-
-
r
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol
-
-
-
r
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
reduced electron-transferring flavoprotein + 6-(10-bromodecyl)ubiquinone
electron-transferring flavoprotein + 6-(10-bromodecyl)ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + 6-(10-hydroxydecyl)ubiquinone
electron-transferring flavoprotein + 6-(10-hydroxydecyl)ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + 6-heptylubiquinone
electron-transferring flavoprotein + 6-heptylubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + 6-nonylubiquinone
electron-transferring flavoprotein + 6-nonylubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
electron-transferring flavoprotein + reduced coenzyme Q1
reduced electron-transferring flavoprotein + decylubiquinone
electron-transferring flavoprotein + decylubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + nitro blue tetrazolium
electron transferring-flavoprotein + reduced nitro blue tetrazolium
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
reduced electron-transferring flavoprotein + ubiquinone-4
electron-transferring flavoprotein + ubiquinol-4
-
-
-
-
?
reduced electron-transferring flavoprotein-4'-deoxy-FAD + ubiquinone-1
electron-transferring flavoprotein-4'-deoxy-FAD + ubiquinol-1
-
0.07% of turnover with native electron-transferring flavoprotein
-
?
reduced electron-transferring-flavoprotein + 2,5-dibromo-3-methyl-6-isopropyl-4-benzoquinone
electron-transferring-flavoprotein + 2,5-dibromo-3-methyl-6-isopropyl-4-benzoquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + 6-bis(isoprenyl)ubiquinone
electron-transferring-flavoprotein + 6-bis(isoprenyl)ubiquinol
-
optimal ubiquinone derivative
-
-
?
reduced electron-transferring-flavoprotein + 6-isoprenylubiquinone
electron-transferring-flavoprotein + 6-isoprenylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + bromodecylubiquinone
electron-transferring-flavoprotein + bromodecylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + decylubiquinone
electron-transferring-flavoprotein + decylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + duroquinone
electron-transferring-flavoprotein + duroquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + heptylubiquinone
electron-transferring-flavoprotein + heptylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + hydroxydecylubiquinone
electron-transferring-flavoprotein + hydroxydecylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + menadione
electron-transferring-flavoprotein + menadiol
-
-
-
-
?
reduced electron-transferring-flavoprotein + nonylubiquinone
electron-transferring-flavoprotein + nonylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + pentadecylubiquinone
electron-transferring-flavoprotein + pentadecylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + tridecylubiquinone
electron-transferring-flavoprotein + tridecylubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
semiquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
semiquinone electron transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + ubiquinol
-
-
-
-
r
semiquinone electron transferring flavoprotein + ubiquinone Q1
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + ubiquinol Q1
-
-
-
-
r
semiquinone electron-transferring flavoprotein + ubiquinone Q1
electron-transferring flavoprotein + hydroquinone electron-transferring flavoprotein + ubiquinol Q1
-
-
-
-
r
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
-
-
?
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
trivial name ubiquinone-1, enzyme is an efficient electron acceptor for electron-transferring flavoprotein and a reductase of ubiqinone
-
?
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
-
-
?
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
pig liver or Paracoccus denitrificans electron-transferring flavoprotein as electron carrier
-
?
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
-
-
?
reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
-
-
?
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
-
-
-
?
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
reduced electron-transferring flavoprotein + 2,6-dichloroindophenol
electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
-
-
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
electron-transferring flavoprotein + reduced coenzyme Q1
-
-
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
electron-transferring flavoprotein + reduced coenzyme Q1
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
electron-transferring flavoprotein + reduced coenzyme Q1
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
group I electron-transferring flavoprotein, ETF
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
group I electron-transferring flavoprotein, ETF
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
electron transfer via flavin cofactor
-
-
r
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
via FAD
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
via FAD
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
electron-transferring flavoprotein alpha- and beta-subunits contain a FAD cofactor and an AMP molecule, respectively
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
electron transfer via flavin cofactor
-
-
r
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
-
ETF is the intermediate electron carrier between dehydrogenases and the enzyme, enzyme mediates between eleven mitochondrial proteins and the ubiquinone pool
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
-
ubiquinone is 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
?
semiquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
-
-
?
semiquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
-
-
?
semiquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol
-
disproportion and comproportion with ubiqinone-1 as the terminal oxidant
-
r
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
-
-
?
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
-
-
?
additional information
?
-
Agrobacterium tumefaciens C58 / ATCC 33970
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
-
-
?
additional information
?
-
-
assay method uses dichlorophenolindophenol, DCPIP, as substrate
-
-
?
additional information
?
-
enzyme deficiency leads to glutaric acidemia type II
-
-
?
additional information
?
-
-
enzyme deficiency leads to glutaric acidemia type II
-
-
?
additional information
?
-
-
specificity for different ubiquinone derivatives, overview
-
-
?
additional information
?
-
-
the electron-transferring flavoprotein beta-D128N mutation occurs in a beta-turn located near the AMP binding site, a region that is involved in intersubunit contacts and establishes outer-sphere interactions with the FAD cofactor, namely at the level of the isoalloxazine moiety. Namely ETF b-D128N and ETF b-R191C,would have an impacton reactive oxygen species generation.The ETF variants show about 70% decreased activity in comparison with the wild-type protein, and establish a rationale for their functional defects
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
mechanism of superoxide formation by ETF-QO, reduction potentials of redox centres, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
group I electron-transferring flavoprotein, ETF
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
group I electron-transferring flavoprotein, ETF
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
via FAD
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
via FAD
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
-
electron transfer via flavin cofactor
-
-
r
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
-
ETF is the intermediate electron carrier between dehydrogenases and the enzyme, enzyme mediates between eleven mitochondrial proteins and the ubiquinone pool
-
-
?
additional information
?
-
enzyme deficiency leads to glutaric acidemia type II
-
-
?
additional information
?
-
-
enzyme deficiency leads to glutaric acidemia type II
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4Fe-4S-center
-
iron-sulfur flavoprotein that contains a single [4Fe-4S]2+,1+
iron-sulfur center
enzyme ETFDH is a monomer containing a FAD molecule and an iron-sulfur cluster
FAD
-
the enzyme contains one FAD, FAD is involved in electron transfer to ubiquinone but not in electron transfer from electron-transferring flavoprotein to ETF-QO
FAD
-
bound by the C-terminal region of the alpha-subunit (domain II) of electron transfer flavoprotein
FAD
-
bound by the C-terminal region of the alpha-subunit (domain II) of electron transfer flavoprotein
FAD
enzyme ETFDH is a monomer containing a FAD molecule and an iron-sulfur cluster
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S
-
the enzyme contains one [4Fe-4S]2+,1+, the iron-sulfur cluster is the immediate acceptor from electron-transferring flavoprotein
4Fe-4S centre
Fe2+
Fe2+/Fe3+
Iron
Fe2+
enzyme ETFDH is a monomer containing a FAD molecule and an iron-sulfur cluster
Fe2+/Fe3+
-
enzyme contains one ferredoxin-type 4Fe-4S1+,2+ cluster. The cluster is diamagnetic in the isolated oxidized enzyme, and becomes paramagnetic if enzymatically or dithionite reduced. The enzyme accepts a maximum of 2 electrons from electron-transferring flavoprotein whereas it can be reduced by 3 electrons with dithionite or photochemically
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
-
inhibitory to thiolated enzyme, no inhibition of unmodified enzyme
p-chloromercuribenzoate
-
complete inhibition of ubiquinone reductase activity, 70% inhibition of disproportion activity
additional information
-
Klebsiella pneumoniae NifA-dependent promotor regulation of fixABCX operon
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
Klebsiella pneumoniae NifA-dependent promotor regulation of fixABCX operon
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
substrate binding and steady-state reaction kinetics
-
0.0042
electron-transferring flavoprotein
-
comproportionation at pH 7.4, acetylated enzyme
0.0058
electron-transferring flavoprotein
-
disproportionation of semiquinone electron-transferring flavoprotein
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
78
electron-transferring flavoprotein
-
comproportionation of electron-transferring flavoprotein and hydroquinone electron-transferring flavoprotein
200
electron-transferring flavoprotein
-
disproportion of semiquinone electron-transferring flavoprotein
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.21
-
deletion mutant enzyme lacking 74 amino acids, disproportionation of semiquinone electron-transferring flavoprotein
0.33
-
C561A mutant enzyme, disproportionation of semiquinone electron-transferring flavoprotein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fixABCX operon, genes fixC and fixX encode the enzyme's N-terminus and C-terminus, respectively
-
-
brenda
subunit alpha, bifunctional electron transferring flavoprotein/butyryl-CoA dehydrogenase
UniProt
brenda
subunit alpha, bifunctional electron transferring flavoprotein/butyryl-CoA dehydrogenase
UniProt
brenda
-
-
-
brenda
ETF-QO; patients suffering glutaric acidemia type II due to a mutational defect in the ETF:QO gene
SwissProt
brenda
gene is located to chromosome 4q33, deficiency of the enzyme causes glutaric acidemia type II
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
bound to via ubiquinone binding domain, overview
brenda
-
ETFDH is an inner mitochondrial membrane localized enzyme
brenda
Magnaporthe oryzae ETF and ETFDH co-localization with the mitochondrial marker ATP1-RFP, but almost not with the peroxysomal marker PTS1-RFP
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
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
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
malfunction
-
evaluations of the mutant phenotypes following carbon starvation induced by extended darkness identify similarities to those exhibited by mutants of the ETF/ETFQO complex, metabolic profiling, overview
malfunction
a small number of conidia are formed by ETF and ETFDH deletion mutants growing on different media, the conidial germination and appressoria formation on hydrophobic surface do not show any variations compared to the wild-type. Sprayed onto live barley and rice seedlings, the mutant conidia are almost completely non-pathogenic, despite producing a few non-extended necroses on the host surface. ETF and ETFDH mutants display growth and conidiation defects. ETF mutant etfb- cells exhibit reduced turgor pressure in 2-4 M glycerol, reduced ATP synthesis, and the ETF mutant etfb- is more sensitive to host oxidative stress (by H2O2 in host cells). ETF mutant etfb- shows lipid body accumulation. Phenotypes, overview
malfunction
-
deficiency of ETF or ETFDH leads to dysfunction of acyl-CoA dehydrogenase, resulting in accumulation of long- and medium-chain fatty acids. Multiple acyl-CoA dehydrogenation deficiency (glutaric aciduria type II, MADD) occurs due to a mutation of electron transfer flavoprotein-dehydrogenase in a cat, that presented with symptoms characteristic of MADD including hypoglycemia, hyperammonemia, vomiting, diagnostic organic aciduria, and accumulation of medium- and long-chain fatty acids in plasma, phenotype, overview
malfunction
deficiency of ETF or ETFDH leads to dysfunction of acyl-CoA dehydrogenase, resulting in accumulation of long- and medium-chain fatty acids. Multiple acyl-CoA dehydrogenation deficiency (MADD) occurs due to mutations of electron transfer flavoprotein-dehydrogenase, including c.250G>A, c.380T>A, c.770A>G, c.1601C>T, and c.524G>A. Lipid storage myopathy (LSM) is a genetically heterogeneous group with variable clinical phenotypes. Late-onset multiple acyl-coenzyme A dehydrogenation deficiency (MADD) is a rather common form of LSM in China, phenotypewith neuromuscular disorders, overview
malfunction
depletion of enzyme ETFDH leads to growth inhibition in Burkholderia cenocepacia. In the DELTAetfdh2 mutant strain, growth is unaffected as long as gene etfdh1 is expressed, but falls to 13% of wild-type activity in the absence of rhamnose, suggesting that gene etfdh2 partially complements gene etfdh1. The morphology seen when EtfAB or ETF dehydrogenase is depleted is not due to a general defect of respiration
malfunction
impairment of lysine-specific reduction of ETF reduces the ability of AtETF to mediate electron transfer between ETF-dependent dehydrogenases and ETF-QO
malfunction
multiple acyl-coenzyme A dehydrogenase deficiency (MADD), also known as glutaric acidemia type 2 (GA2), is a rare autosomal recessive disorder whose biochemical abnormalities result from a deficiency of one of the two electron transfer flavoproteins (ETF and ETFDH) that transfer electrons from acyl-CoA dehydrogenases to the respiratory chain. Bezafibrate (BEZ) is a hypolipidemic drug that is as an agonist of the peroxisome proliferating activator receptor, and is beneficial in Japanese children with ETFDH gene mutations exhibiting GA2. BEZ, L-carnitine, and riboflavin each show partial effectiveness and produce partial remission in a patient with GA2. The disorder affects multiple metabolic pathways involving branched amino acids, fatty acids, and tryptophan, and results in a variety of distinctive organic acids being discharged. The heterogeneous clinical features of patients with GA2 fall into three subclasses: two neonatal-onset forms (types I/ II) and a late-onset form (type III), phenotypes, overview
malfunction
Agrobacterium tumefaciens C58 / ATCC 33970
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impairment of lysine-specific reduction of ETF reduces the ability of AtETF to mediate electron transfer between ETF-dependent dehydrogenases and ETF-QO
-
malfunction
-
depletion of enzyme ETFDH leads to growth inhibition in Burkholderia cenocepacia. In the DELTAetfdh2 mutant strain, growth is unaffected as long as gene etfdh1 is expressed, but falls to 13% of wild-type activity in the absence of rhamnose, suggesting that gene etfdh2 partially complements gene etfdh1. The morphology seen when EtfAB or ETF dehydrogenase is depleted is not due to a general defect of respiration
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metabolism
-
both isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an ETF/ETFQO-mediated route, overview. The ETF/ETFQO system can be regarded as a branch of the electron transport system with multiple input sites from seven acyl-CoA dehydrogenases and two N-methyl dehydrogenases, namely, isovaleryl-CoA dehydrogenase and 2-methyl branched-chain acyl-CoA dehydrogenase, as well as glutaryl-CoA dehydrogenase and sarcosine and dimethylglycine dehydrogenases
metabolism
group I electron-transferring flavoproteins (ETFs) funnel electrons from a variety of species-specific primary dehydrogenases to the ETF dehydrogenase (ETFDH) from which they enter the electron transport chain at the ubiquinone pool. Group II ETFs divert electrons away from primary dehydrogenases towards nitrogenase reductase, overview
metabolism
enzyme catalyzes the reduction of one crotonyl-CoA and two ferredoxins by two NADH within a flavin-based electron-bifurcating process. NADH reduces beta-FAD, which bifurcates. One electron goes to ferredoxin and one to alpha-FAD, which swings over to reduce delta-FAD to the semiquinone. Repetition affords a second reduced ferredoxin and delta-FADH-, which reduces crotonyl-CoA
metabolism
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group I electron-transferring flavoproteins (ETFs) funnel electrons from a variety of species-specific primary dehydrogenases to the ETF dehydrogenase (ETFDH) from which they enter the electron transport chain at the ubiquinone pool. Group II ETFs divert electrons away from primary dehydrogenases towards nitrogenase reductase, overview
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metabolism
-
enzyme catalyzes the reduction of one crotonyl-CoA and two ferredoxins by two NADH within a flavin-based electron-bifurcating process. NADH reduces beta-FAD, which bifurcates. One electron goes to ferredoxin and one to alpha-FAD, which swings over to reduce delta-FAD to the semiquinone. Repetition affords a second reduced ferredoxin and delta-FADH-, which reduces crotonyl-CoA
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physiological function
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three cis-regulatory sequences (pha-site, rep-site, and act-site) are identified. Phylogenetic footprinting of each site indicates that they are conserved between four Caenorhabditis species. Results show that let-721 is under complex transcriptional control
physiological function
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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
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
physiological function
-
the enzyme is maternally required for Drosophila embryogenesis
physiological function
-
the functional electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO) complex supports respiration during carbon starvation. The enzyme is involved in the process of dark-induced senescence
physiological function
electron-transferring flavoprotein (ETF) and its dehydrogenase (ETFDH) are highly conserved electron carriers which mainly function in mitochondrial fatty acid beta oxidation. Besides catalyzing dehydrogenation, acyl-CoA dehydrogenases also transfer electrons to an electron-transferring flavoprotein (ETF), which, through the electron-transferring flavoprotein dehydrogenase (ETFDH), finally delivers the electrons to the ubiquinone pool in the terminal respiratory system for ATP synthesis. Thus, ETF and ETFDH link the fatty acids oxidation with respiratory system
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
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
physiological function
-
ETFDH transfer electrons from ETF to ubiquinone, which exists in the inner mitochondrial membrane and participates in electron transport system to produce ATP. In this process, electrons enter through the flavin center of ETFDH and exit via the 4Fe-4S cluster for delivery to ubiquinone
physiological function
group I ETF-alpha-coding gene, etfA, and group I ETF-beta-coding gene, etfB, are essential for Burkholderia cenocepacia, ETFDH funnels electrons from ETFs to ubiquinone, entering the electron transport chain at the ubiquinone pool. ENzyme ETF dehydrogenase induces a rod-to-sphere change in morphology, like the ETFalpha/beta proteins
physiological function
group I ETF-alpha-coding gene, etfA, and group I ETF-beta-coding gene, etfB, are essential for Burkholderia cenocepacia, ETFDH funnels electrons from ETFs to ubiquinone, entering the electron transport chain at the ubiquinone pool. Enzyme ETF dehydrogenase induces a rod-to-sphere change in morphology, like the ETFalpha/beta proteins. None of the genes found on the third chromosome of Burkholderia cenocepacia, including etfdh2, are likely to be essential
physiological function
in THP-1 monocytes during acute (16 h) and chronic (72 h) hypoxia, levels of electron-transferring flavoproteins are elevated. Expression of ETFDH decreases under acute hypoxia, but increases under chronic conditions. siRNA-mediated knockdown of ETFDH lowers mitochondrial respiration under chronic hypoxia
physiological function
Agrobacterium tumefaciens C58 / ATCC 33970
-
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
-
physiological function
-
group I ETF-alpha-coding gene, etfA, and group I ETF-beta-coding gene, etfB, are essential for Burkholderia cenocepacia, ETFDH funnels electrons from ETFs to ubiquinone, entering the electron transport chain at the ubiquinone pool. ENzyme ETF dehydrogenase induces a rod-to-sphere change in morphology, like the ETFalpha/beta proteins
-
physiological function
-
group I ETF-alpha-coding gene, etfA, and group I ETF-beta-coding gene, etfB, are essential for Burkholderia cenocepacia, ETFDH funnels electrons from ETFs to ubiquinone, entering the electron transport chain at the ubiquinone pool. Enzyme ETF dehydrogenase induces a rod-to-sphere change in morphology, like the ETFalpha/beta proteins. None of the genes found on the third chromosome of Burkholderia cenocepacia, including etfdh2, are likely to be essential
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additional information
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electron transfer flavoprotein structure analysis and FAD binding of wild-type and mutants, i.e. alphaA210C, betaA111C, betaA111C/E162A, and alphaA43C, overview
additional information
-
electron transfer flavoprotein structure analysis and FAD binding, overview
additional information
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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
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
67000
-
x * 67000, immunoprecipitation after in vitro translation, deduced from nucletide sequence
64000
-
x * 64000, assumed to be a monomer in the mitochondrial membrane, immunoblot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 64000, assumed to be a monomer in the mitochondrial membrane, immunoblot
?
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x * 67000, immunoprecipitation after in vitro translation, deduced from nucletide sequence
additional information
proteins ETFB and ETFDH contain an ETF domain and an ETFDH domain, respectively, while protein ETFA also contains a FAD binding domain in addition to the ETF domain
additional information
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proteins ETFB and ETFDH contain an ETF domain and an ETFDH domain, respectively, while protein ETFA also contains a FAD binding domain in addition to the ETF domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
sequence contains a mitochondrial targeting peptide of 32 amino acids
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray structure of the (EtfAB/Bcd)4 complex in the dehydrogenase-conducting D-state, alpha-FAD (bound to domain II of EtfA) and delta-FAD (bound to butyryl-CoA dehydrogenase Bcd) being 8 A apart. A rotation of domain II of nearly 80° is observed, further rotation by 10° brings EtfAB into the bifurcating B-state, alpha-FAD and beta-FAD (bound to EtfB) being 14 A apart
with and without substrate ubiquinone. Molecule forms a single structural domain binding FAD, the 4Fe-4S cluster and ubiquinone in three functional regions that are closely packed and share structural elements
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G362E
-
mutation occurs in one of two beta-sheets that form the structure of the FAD binding domain likely disrupting the secondary structur. Phenotype of homozygous let-721 mutant is maternal effects lethality. F1 homozygotes have no gross morphological or developmental defects. The maternal effect lethal manifests as the self-fertilized offspring arrest as unhatched embryos. F1 worms are also self semi-sterile, as unmated homozygous mutants produce significantly fewer embryos than wild-type worms
S61F
-
affected residue lies within a conserved domain that interacts with the adenine monophosphate moiety of the FAD prosthetic group. Phenotype of homozygous let-721 mutant is maternal effects lethality. F1 homozygotes have no gross morphological or developmental defects. The maternal effect lethal manifests as the self-fertilized offspring arrest as unhatched embryos. F1 worms are also self semi-sterile, as unmated homozygous mutants produce significantly fewer embryos than wild-type worms
N338A
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the mutation has no impact on the reduction potential for the iron-sulfur cluster and leads to a slight increase in disproportionation activity (110% relative to wild type activity)
N338T
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the mutation has no impact on the reduction potential for the iron-sulfur cluster and leads to a slight increase in disproportionation activity (110% relative to wild type activity)
T525A
-
the mutation decreases the midpoint potentials of the iron-sulfur cluster resulting in a decrease in steady-state ubiquinone reductase activity and in electron transfer flavoprotein semiquinone disproportionation, there is no detectable effect of the mutation on the flavin midpoint potentials
Y501F
-
the mutation decreases the midpoint potentials of the iron-sulfur cluster resulting in a decrease in steady-state ubiquinone reductase activity and in electron transfer flavoprotein semiquinone disproportionation, there is no detectable effect of the mutation on the flavin midpoint potentials
Y501F/T525A
-
the mutation decreases the midpoint potentials of the iron-sulfur cluster resulting in a decrease in steady-state ubiquinone reductase activity and in electron transfer flavoprotein semiquinone disproportionation, there is no detectable effect of the mutation on the flavin midpoint potentials
F231C
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naturally occuring mutation, the feline patient-specific mutation c.692T>G (p.F231C) in enzyme ETFDH in feline ETFDH is completely conserved in eukaryotes, and is located on the apical surface of enzyme ETFDH, receiving electrons from electron-transferring flavoprotein (ETF) causing multiple acyl-CoA dehydrogenation deficiency (MADD) in the cat, phenotype, overview
A84T/S307C
mutations identified in a chinese woman with late-onset glutaric aciduria type II. The muscle biopsy of the patient reveals lipid storage myopathy. Blood biochemical test and urine organic acid analyses are consistent with glutaric aciduria type II
D218N
heterozygous, with a deletion on the other allele, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
G611E
homozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
I31T
neutral naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no effect on enzyme activity or expression, occurs together with other mutantions, overview
L262F
homozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
L334P
homo- or heterozygous, the latter with a deletion on the other allele, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, reduced antigen detected in fibroblasts
L334P/Q222P
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II
M1T
homo- and heterozygous, the latter with a deletion on the other allele, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
P456L
-
the mutation affects most likely the catalytic activity and the stability of the tetramer
P483L
-
the mutation affects most likely the catalytic activity and the stability of the tetramer
P562L
heterozygous, with a deletion on the other allele, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
R41X/L138R
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II
R452K
homozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II
S82F/D218N
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, reduced antigen detected in fibroblasts
S82P/H346R
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
W182X/P456L
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, reduced antigen detected in fibroblasts
Y49C
heterozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
additional information
additional information
-
enzyme disruption mutant, mutant plants show a dramatic reduction in the ability to withstand extended darkness, resulting in senescence and death within 10 days after transfer. Leaves of mutants have a decline in sugar levels but significant accumulation of several amino acids and phytanoyl-CoA
additional information
-
identification of mutants of the ETF/ETFQO complex
additional information
construction of strain Detfdh2 K56-2 DBCAS0609 through deletion of putative ETF dehydrogenase and of strain Cetfdh1 K56-2 rhaP::BCAL1468/Tpr, showing rhamnose-dependent etfdh1 expression in K56 background, in the latter in the presence of etfdh2, lack of etfdh1 expression reduces growth to 29% of growth with rhamnose
additional information
construction of strain Detfdh2 K56-2 DBCAS0609 through deletion of putative ETF dehydrogenase and of strain Cetfdh1 K56-2 rhaP::BCAL1468/Tpr, showing rhamnose-dependent etfdh1 expression in K56 background, in the latter in the presence of etfdh2, lack of etfdh1 expression reduces growth to 29% of growth with rhamnose
additional information
-
construction of strain Detfdh2 K56-2 DBCAS0609 through deletion of putative ETF dehydrogenase and of strain Cetfdh1 K56-2 rhaP::BCAL1468/Tpr, showing rhamnose-dependent etfdh1 expression in K56 background, in the latter in the presence of etfdh2, lack of etfdh1 expression reduces growth to 29% of growth with rhamnose
additional information
-
construction of strain Detfdh2 K56-2 DBCAS0609 through deletion of putative ETF dehydrogenase and of strain Cetfdh1 K56-2 rhaP::BCAL1468/Tpr, showing rhamnose-dependent etfdh1 expression in K56 background, in the latter in the presence of etfdh2, lack of etfdh1 expression reduces growth to 29% of growth with rhamnose
-
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/IxGx12GxxGxxxG/A) that affords both FAD binding and stabilisation of the secondary structure elements involved, overview
additional information
determination and analysis of diverse naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, phenotypic effects, overview
additional information
-
determination and analysis of diverse naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, phenotypic effects, overview
additional information
generation of gene deletion mutants of the two ETF genes (ETFA and ETFB) and the ETFDH gene (ETFDH) by targeted gene deletion mutagenesis, mutant are named etfa?, etfb? and etfdh? respectively. ETF and ETFDH mutants display growth and conidiation defects, phenotypes, overview
additional information
-
generation of gene deletion mutants of the two ETF genes (ETFA and ETFB) and the ETFDH gene (ETFDH) by targeted gene deletion mutagenesis, mutant are named etfa?, etfb? and etfdh? respectively. ETF and ETFDH mutants display growth and conidiation defects, phenotypes, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
no loss in activity after 1 h between pH 7.0 and pH 9.0, 19% loss of activity after 1 h at pH 6.0 or pH 10.0, complete loss of activity at pH 5.5
392484
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose colmn chromatography and Source 15Q column chromatography
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIPL by nickel affinity chromatography in presence of FAD
submitochondrial particles, cholate extract, ammonium sulfate, DEAE-Bio gel, hydroxyapatite
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIPL by nickel affinity chromatography in presence of FAD
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIPL by nickel affinity chromatography in presence of FAD
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
cloning of the electron-transferring flavoprotein (ETF) alpha and beta subunit encoding genes ETFA and ETFB and enzyme ETFDH encoding gene ETFDH from Magnaporthe oryzae, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GFP-tagged genes ETFA, ETFB, and ETFDH in Magnaporthe oryzae cells
deletion mutant enzyme lacking 74 amino acids among them C561, and a C561A mutant
-
expression in Saccharomyces cerevisiae, the enzyme is synthesized as a 67000 Da precursor which is targeted to mitochondria and processed in a single step to a 64000 Da mature form
-
fixABCX operon, DNA and sequence determination and analysis, analysis of promotor activation and regulation
-
gene CG12140, mapping and cloning of ETF:QO alleles, expression of the two subunits ETFA and ETFB in Escherichia coli strain BL21
-
gene ETF:QO, DNA and amino acid sequence determination and analysis, localization on chromosome 4q33, 13 exons
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus(DE3)-RIPL
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
mutations in the ETFDH gene lead to a secondary myopathic form of CoQ10 deficiency and to the late-onset form of glutaric aciduria type II
medicine
in THP-1 monocytes during acute (16 h) and chronic (72 h) hypoxia, levels of electron-transferring flavoproteins are elevated. Expression of ETFDH decreases under acute hypoxia, but increases under chronic conditions. siRNA-mediated knockdown of ETFDH lowers mitochondrial respiration under chronic hypoxia
medicine
mutations A84T/S307C identified in a chinese woman with late-onset glutaric aciduria type II reveal lipid storage myopathy. Blood biochemical test and urine organic acid analyses are consistent with glutaric aciduria type II
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AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Drosophila melanogaster
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Homo sapiens
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Homo sapiens (Q16134), Homo sapiens
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Agrobacterium tumefaciens (A9CJL8), Agrobacterium tumefaciens, Homo sapiens (Q16134), Homo sapiens, Agrobacterium tumefaciens C58 / ATCC 33970 (A9CJL8)
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Homo sapiens (Q16134)
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Xue, Y.; Zhou, Y.; Zhang, K.; Li, L.; Kayoumu, A.; Chen, L.; Wang, Y.; Lu, Z.
Compound heterozygous mutations in electron transfer flavoprotein dehydrogenase identified in a young Chinese woman with late-onset glutaric aciduria type II
Lipids Health Dis.
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Homo sapiens (Q16134), Homo sapiens
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Demmer, J.K.; Pal Chowdhury, N.; Selmer, T.; Ermler, U.; Buckel, W.
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1577
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Clostridioides difficile (A0A125V455), Clostridioides difficile DSM 1296 (A0A125V455)
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