Information on EC 1.5.5.1 - electron-transferring-flavoprotein dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.5.5.1
-
RECOMMENDED NAME
GeneOntology No.
electron-transferring-flavoprotein dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
show the reaction diagram
electrostatic interaction between enzyme and electron-transferring flavoprotein
-
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
electron-transferring-flavoprotein:ubiquinone oxidoreductase
An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
electron flavoprotein reductase
-
-
-
-
electron transfer flavoprotein
-
-
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-ubiquinone oxidoreductase
-
-
electron transfer flavoprotein-ubiquinone oxidoreductase
-
-
electron transfer flavoprotein: ubiquinone oxidoreductase
-
-
electron transfer flavoprotein:ubiquinone oxidoreductase
-
-
electron transfer flavoprotein:ubiquinone oxidoreductase
Q16134
-
electron transfer flavoprotein:ubiquinone oxidoreductase
-
-
electron-transfer flavoprotein-2,3-dimethoxy-5-methyl-1,4-benzoquinone oxidoreductase
-
-
electron-transfer flavoprotein-ubiquinone oxidoreductase
-
-
electron-transfer flavoprotein:ubiquinone oxidoreductase
-
-
electron-transferring flavoprotein dehydrogenase
-
-
Electron-transferring-flavoprotein dehydrogenase
-
-
-
-
Electron-transferring-flavoprotein dehydrogenase
-
-
ETF dehydrogenase
-
-
-
-
ETF-QO
-
-
-
-
ETF-ubiquinone oxidoreductase
-
-
-
-
ETF-ubiquinone oxidoreductase
-
-
ETF:QO
Q16134
-
ETF:ubiquinone oxidoreductase
-
-
-
-
ETFDH
-
-
CAS REGISTRY NUMBER
COMMENTARY
86551-03-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
fixABCX operon, genes fixC and fixX encode the enzyme's N-terminus and C-terminus, respectively
-
-
Manually annotated by BRENDA team
gene CG12140
-
-
Manually annotated by BRENDA team
ETF-QO; patients suffering glutaric acidemia type II due to a mutational defect in the ETF:QO gene
SwissProt
Manually annotated by BRENDA team
gene is located to chromosome 4q33, deficiency of the enzyme causes glutaric acidemia type II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
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
-
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
physiological function
-
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
-
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
-
the enzyme is maternally required for Drosophila embryogenesis
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
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
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
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
additional information
-
electron transfer flavoprotein structure analysis and FAD binding, overview
additional information
-
electron transfer flavoprotein structure analysis and FAD binding of wild-type and mutants, i.e. alphaA210C, betaA111C, betaA111C/E162A, and alphaA43C, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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-pentyl-1,4-benzoquinone
electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol
show the reaction diagram
-
-
-
r
reduced electron-transferring flavoprotein + 6-(10-bromodecyl)ubiquinone
electron-transferring flavoprotein + 6-(10-bromodecyl)ubiquinol
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + 6-(10-hydroxydecyl)ubiquinone
electron-transferring flavoprotein + 6-(10-hydroxydecyl)ubiquinol
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + 6-heptylubiquinone
electron-transferring flavoprotein + 6-heptylubiquinol
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + 6-nonylubiquinone
electron-transferring flavoprotein + 6-nonylubiquinol
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + decylubiquinone
electron-transferring flavoprotein + decylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + nitro blue tetrazolium
electron transferring-flavoprotein + reduced nitro blue tetrazolium
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
electron transfer via flavin cofactor
-
-
r
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
electron transfer via flavin cofactor
-
-
r
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
via FAD
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-2
electron-transferring flavoprotein + ubiquinol-2
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone-4
electron-transferring flavoprotein + ubiquinol-4
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein-4'-deoxy-FAD + ubiquinone-1
electron-transferring flavoprotein-4'-deoxy-FAD + ubiquinol-1
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + 6-bis(isoprenyl)ubiquinone
electron-transferring-flavoprotein + 6-bis(isoprenyl)ubiquinol
show the reaction diagram
-
optimal ubiquinone derivative
-
-
?
reduced electron-transferring-flavoprotein + 6-isoprenylubiquinone
electron-transferring-flavoprotein + 6-isoprenylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + bromodecylubiquinone
electron-transferring-flavoprotein + bromodecylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + decylubiquinone
electron-transferring-flavoprotein + decylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + duroquinone
electron-transferring-flavoprotein + duroquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + heptylubiquinone
electron-transferring-flavoprotein + heptylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + hydroxydecylubiquinone
electron-transferring-flavoprotein + hydroxydecylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + menadione
electron-transferring-flavoprotein + menadiol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + nonylubiquinone
electron-transferring-flavoprotein + nonylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + pentadecylubiquinone
electron-transferring-flavoprotein + pentadecylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + tridecylubiquinone
electron-transferring-flavoprotein + tridecylubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
show the reaction diagram
-
ETF is the intermediate electron carrier between dehydrogenases and the enzyme, enzyme mediates between eleven mitochondrial proteins and the ubiquinone pool, 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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
-
disproportion and comproportion with ubiqinone-1 as the terminal oxidant
-
r
additional information
?
-
Q16134
enzyme deficiency leads to glutaric acidemia type II
-
-
-
additional information
?
-
-
genetic regulatory model
-
-
-
additional information
?
-
-
specificity for different ubiquinone derivatives, overview
-
-
-
additional information
?
-
-
assay method uses dichlorophenolindophenol, DCPIP, as substrate
-
-
-
additional information
?
-
-
mechanism of superoxide formation by ETF-QO, reduction potentials of redox centres, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
electron transfer via flavin cofactor
-
-
r
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
-
via FAD
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
show the reaction diagram
-
-
-
-
?
reduced electron-transferring-flavoprotein + ubiquinone
electron-transferring-flavoprotein + ubiquinol
show the reaction diagram
-
ETF is the intermediate electron carrier between dehydrogenases and the enzyme, enzyme mediates between eleven mitochondrial proteins and the ubiquinone pool
-
-
?
additional information
?
-
Q16134
enzyme deficiency leads to glutaric acidemia type II
-
-
-
additional information
?
-
-
genetic regulatory model
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4Fe-4S-center
-
iron-sulfur flavoprotein that contains a single [4Fe-4S]2+,1+
FAD
-
binding sequence
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
-
contains one FAD
FAD
-
contains one equivalent of FAD
FAD
-
the flavin serves as the immediate reductant of ubiquinone
FAD
-
bound by the C-terminal region of the alpha-subunit (domain II) of electron transfer flavoprotein
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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
-
contains a single [4Fe-4S]2+,1+ cluster
Fe2+
-
enzyme contains iron-sulfur clusters
Fe2+
-
a [4Fe-4S]+1+2 cluster
Fe2+/Fe3+
-
enzyme contains a single 4Fe-1S cluster per subunit and flavin
Fe2+/Fe3+
-
enzyme contains a single 4Fe-1S cluster per subunit and flavin
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
Iron
-
4Fe-4S center
Iron
-
iron-sulfur protein with 4Fe-4S center
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-(3-methylpentyl)-4,6-dinitrophenol
-
; noncompetitive
N-ethylmaleimide
-
inhibitory to thiolated enzyme, no inhibition of unmodified enzyme
N-Succinimidyl 3-(2-pyridyldithio)propionate
-
partial inactivation
p-chloromercuribenzoate
-
complete inhibition of ubiquinone reductase activity, 70% inhibition of disproportion activity
Pentachlorophenol
-
; noncompetitive
2-n-heptyl-4-hydroxyquinoline N-oxide
-
-
additional information
-
inhibition mechanism
-
additional information
-
Klebsiella pneumoniae NifA-dependent promotor regulation of fixABCX operon
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
Klebsiella pneumoniae NifA-dependent promotor regulation of fixABCX operon
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0026
-
6-(10-bromodecyl)ubiquinone
-
-
0.0018
-
6-(10-hydroxydecyl)ubiquinone
-
-
0.0069
-
6-bis(isoprenyl)ubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.002
-
6-heptylubiquinone
-
-
0.0095
-
6-isoprenylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0016
-
6-nonylubiquinone
-
-
0.0089
-
bromodecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0079
-
decylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0084
-
decylubiquinone
-
-
0.0195
-
duroquinone
-
recombinant enzyme, pH 7.4, 25C
0.00013
-
electron-transferring flavoprotein
-
-
0.0002
-
electron-transferring flavoprotein
-
comproportionation at about pH 7.0
0.00032
-
electron-transferring flavoprotein
-
-
0.0005
-
electron-transferring flavoprotein
-
comproportionation at about pH 9.0
0.00197
-
electron-transferring flavoprotein
-
-
0.0042
-
electron-transferring flavoprotein
-
comproportionation at pH 7.4, acetylated enzyme
0.0058
-
electron-transferring flavoprotein
-
disproportionation of semiquinone electron-transferring flavoprotein
0.0113
-
electron-transferring flavoprotein
-
ubiquinone-1 reduction
5400
-
electron-transferring flavoprotein
-
-
0.0082
-
heptylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.00031
-
hydroquinone electron-transferring flavoprotein
-
-
-
0.0099
-
hydroxydecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0073
-
nonylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0023
-
pentadecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0077
-
semiquinone electron-transferring flavoprotein
-
-
-
0.0154
-
semiquinone electron-transferring flavoprotein
-
-
-
0.0265
-
tridecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0045
-
ubiquinone-1
-
-
0.0081
-
ubiquinone-1
-
-
0.0571
-
ubiquinone-1
-
-
6900
-
ubiquinone-1
-
-
0.0023
-
ubiquinone-2
-
-
0.0049
-
ubiquinone-2
-
-
0.0148
-
ubiquinone-4
-
-
0.0163
-
menadione
-
recombinant enzyme, pH 7.4, 25C
additional information
-
additional information
-
substrate binding and steady-state reaction kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
210
-
6-(10-bromodecyl)ubiquinone
-
-
132
-
6-(10-hydroxydecyl)ubiquinone
-
-
68.7
-
6-bis(isoprenyl)ubiquinone
-
recombinant enzyme, pH 7.4, 25C
182
-
6-heptylubiquinone
-
-
34.5
-
6-isoprenylubiquinone
-
recombinant enzyme, pH 7.4, 25C
246
-
6-nonylubiquinone
-
-
60.8
-
bromodecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
59.9
-
decylubiquinone
-
recombinant enzyme, pH 7.4, 25C
74.3
-
decylubiquinone
-
-
18.1
-
duroquinone
-
recombinant enzyme, pH 7.4, 25C
21.4
-
electron-transferring flavoprotein
-
-
40
-
electron-transferring flavoprotein
-
comproportionation at about pH 7.0
78
-
electron-transferring flavoprotein
-
comproportionation of electron-transferring flavoprotein and hydroquinone electron-transferring flavoprotein
90
-
electron-transferring flavoprotein
-
-
120
-
electron-transferring flavoprotein
-
comproportionation at about pH 8.5
200
-
electron-transferring flavoprotein
-
disproportion of semiquinone electron-transferring flavoprotein
54
-
heptylubiquinone
-
recombinant enzyme, pH 7.4, 25C
67
-
hydroxydecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
6.6
-
menadione
-
recombinant enzyme, pH 7.4, 25C
61.3
-
nonylubiquinone
-
recombinant enzyme, pH 7.4, 25C
7.4
-
pentadecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
8
-
reduced electron-transferring flavoprotein
-
wild type enzyme
8.8
-
reduced electron-transferring flavoprotein
-
mutant enzyme N338A
8.9
-
reduced electron-transferring flavoprotein
-
mutant enzyme N338T
81.4
-
semiquinone electron-transferring flavoprotein
-
-
-
31.5
-
tridecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
78.8
-
ubiqinone-2
-
-
33.5
-
ubiquinone-1
-
-
84
-
ubiquinone-1
-
-
115
-
ubiquinone-1
-
-
162
-
ubiquinone-2
-
-
35.5
-
ubiquinone-4
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0046
-
2-(3-methylpentyl)-4,6-dinitrophenol
-
recombinant enzyme, pH 7.4, 25C
0.0077
-
Pentachlorophenol
-
recombinant enzyme, pH 7.4, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.093
-
-
-
0.139
-
-
ubiquinone reduction
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
0.68
-
-
disproportionation of semiquinone electron-transferring flavoprotein
1.3
-
-
disproportionation of semiquinone electron-transferring flavoprotein
17.6
-
-
recombinant enzyme, ubiquinone-1 reduction
28.6
-
-
octanoyl-CoA:ubiquinone-1 assay
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
-
7.4
-
-
assay at
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
RNA transcribed in somatic gonads
Manually annotated by BRENDA team
-
high level expression
Manually annotated by BRENDA team
-
high level expression
Manually annotated by BRENDA team
-
accumulation during long-term darkness
Manually annotated by BRENDA team
-
high level expression
Manually annotated by BRENDA team
-
RNA transcribed in body wall muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
bound to via ubiquinone binding domain, overview
Manually annotated by BRENDA team
-
inner mitochondrial membrane
Manually annotated by BRENDA team
-
inner mitochondrial membrane
Manually annotated by BRENDA team
-
ETFDH is an inner mitochondrial membrane localized enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 65000, SDS-PAGE; x * 66000, gel filtration in the presence of 6 M guanidine HCl
?
-
x * 69000, SDS-PAGE
?
-
x * 64000, mature enzyme, immunoblotting; x * 67000, immunoprecipitation after in vitro translation, deduced from nucletide sequence
?
-
x * 64000, assumed to be a monomer in the mitochondrial membrane, immunoblot
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
sequence contains a mitochondrial targeting peptide of 32 amino acids
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure analysis
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, 1-2 mg/ml protein, 20% glycerol, several months, no loss in activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from Sf9 insect cells
-
recombinant enzyme, DEAE-Sepharose, HA-Ultrogel, Mono Q
-
partially purified
-
Q-Sepharose colmn chromatography and Source 15Q column chromatography
-
submitochondrial particles, cholate extract, ammonium sulfate, DEAE-Bio gel, hydroxyapatite
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
deletion mutant enzyme lacking 74 amino acids among them C561, and a C561A mutant
-
expressed from a baculovirus vector, expressed in Sf9 cells
-
expression in insect Sf9 cells via transfection using the baculovirus system
-
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
-
expression in Sf9 insect cells
-
gene ETF:QO, DNA and amino acid sequence determination and analysis, localization on chromosome 4q33, 13 exons
Q16134
expressed in Escherichia coli C43
-
expressed in Escherichia coli C43 cells
-
expressed in Escherichia coli strain C43
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
C561A
-
mutant enzyme has no ubiquinone reductase activity
D218N
Q16134
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
Q16134
homozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
I31T
Q16134
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
Q16134
homozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
L334P
Q16134
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
Q16134
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II
L377P
-
the mutation is involved in the myopathic form of CoQ10 deficiency
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
Q16134
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
Q16134
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II
R452K
Q16134
homozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II
S82F/D218N
Q16134
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
Q16134
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
Q16134
mutations on different alleles, naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, reduced antigen detected in fibroblasts
Y49C
Q16134
heterozygous, naturally occurring mutation of gene ETF:QO in patients with glutaric acidemia type II, no antigen detected in fibroblasts
N338A
-
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
-
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
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
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
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
M1T
Q16134
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
additional information
Q16134
determination and analysis of diverse naturally occurring mutations of gene ETF:QO in patients with glutaric acidemia type II, phenotypic effects, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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