Information on EC 1.5.5.1 - electron-transferring-flavoprotein dehydrogenase

New: Word Map on EC 1.5.5.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.5.5.1
-
RECOMMENDED NAME
GeneOntology No.
electron-transferring-flavoprotein dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oxidative phosphorylation
-
-
SYSTEMATIC NAME
IUBMB Comments
electron-transferring-flavoprotein:ubiquinone oxidoreductase
An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.
CAS REGISTRY NUMBER
COMMENTARY hide
86551-03-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fixABCX operon, genes fixC and fixX encode the enzyme's N-terminus and C-terminus, respectively
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene CG12140
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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-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
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
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
-
iron-sulfur flavoprotein that contains a single [4Fe-4S]2+,1+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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+/Fe3+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(3-methylpentyl)-4,6-dinitrophenol
-
; noncompetitive
2-n-heptyl-4-hydroxyquinoline N-oxide
-
-
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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
Klebsiella pneumoniae NifA-dependent promotor regulation of fixABCX operon
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 0.0084
decylubiquinone
0.0195
duroquinone
-
recombinant enzyme, pH 7.4, 25C
0.00013 - 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
0.0163
menadione
-
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 - 0.0154
semiquinone electron-transferring flavoprotein
0.0265
tridecylubiquinone
-
recombinant enzyme, pH 7.4, 25C
0.0045 - 6900
ubiquinone-1
0.0023 - 0.0049
ubiquinone-2
0.0148
ubiquinone-4
-
-
additional information
additional information
-
substrate binding and steady-state reaction kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
210
6-(10-bromodecyl)ubiquinone
Sus scrofa
-
-
132
6-(10-hydroxydecyl)ubiquinone
Sus scrofa
-
-
68.7
6-bis(isoprenyl)ubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
182
6-heptylubiquinone
Sus scrofa
-
-
34.5
6-isoprenylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
246
6-nonylubiquinone
Sus scrofa
-
-
60.8
bromodecylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
59.9 - 74.3
decylubiquinone
18.1
duroquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
21.4 - 200
electron-transferring flavoprotein
54
heptylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
67
hydroxydecylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
6.6
menadione
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
61.3
nonylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
7.4
pentadecylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
8 - 8.9
reduced electron-transferring flavoprotein
81.4
semiquinone electron-transferring flavoprotein
Homo sapiens
-
-
-
31.5
tridecylubiquinone
Homo sapiens
-
recombinant enzyme, pH 7.4, 25C
78.8
ubiqinone-2
Homo sapiens
-
-
33.5 - 115
ubiquinone-1
162
ubiquinone-2
Sus scrofa
-
-
35.5
ubiquinone-4
Homo sapiens
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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]
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
RNA transcribed in somatic gonads
Manually annotated by BRENDA team
-
RNA transcribed
Manually annotated by BRENDA team
-
RNA transcribed
Manually annotated by BRENDA team
-
RNA transcribed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
sequence contains a mitochondrial targeting peptide of 32 amino acids
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 1-2 mg/ml protein, 20% glycerol, several months, no loss in activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified
-
Q-Sepharose colmn chromatography and Source 15Q column chromatography
-
recombinant enzyme from Sf9 insect cells
-
recombinant enzyme, DEAE-Sepharose, HA-Ultrogel, Mono Q
-
submitochondrial particles, cholate extract, ammonium sulfate, DEAE-Bio gel, hydroxyapatite
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
deletion mutant enzyme lacking 74 amino acids among them C561, and a C561A mutant
-
expressed from a baculovirus vector, expressed in Sf9 cells
-
expressed in Escherichia coli C43
-
expressed in Escherichia coli C43 cells
-
expressed in Escherichia coli strain C43
-
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
-
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
C561A
-
mutant enzyme has no ubiquinone reductase activity
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
L377P
-
the mutation is involved in the myopathic form of CoQ10 deficiency
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (1182 entries)
Please use the Sequence Search for a certain query.