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Information on EC 1.5.5.1 - electron-transferring-flavoprotein dehydrogenase and Organism(s) Homo sapiens and UniProt Accession Q16134

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IUBMB Comments
An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.
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Homo sapiens
UNIPROT: Q16134
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
electron transfer flavoprotein dehydrogenase
-
electron transfer flavoprotein:ubiquinone oxidoreductase
-
ETF:quinone oxidoreductase
-
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-2,3-dimethoxy-5-methyl-1,4-benzoquinone oxidoreductase
-
-
electron-transfer flavoprotein-ubiquinone oxidoreductase
-
-
Electron-transferring-flavoprotein dehydrogenase
ETF dehydrogenase
-
-
-
-
ETF-QO
ETF-ubiquinone oxidoreductase
ETF:ubiquinone oxidoreductase
-
-
-
-
ETFDH
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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
-
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 + 2,6-dichloroindophenol
electron-transferring flavoprotein + reduced 2,6-dichloroindophenol
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + coenzyme Q1
electron-transferring flavoprotein + reduced coenzyme Q1
show the reaction diagram
-
-
-
?
reduced electron-transferring flavoprotein + ubiquinone
electron-transferring flavoprotein + ubiquinol
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 + decylubiquinone
electron-transferring flavoprotein + decylubiquinol
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 + ubiquinone Q1
electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + ubiquinol Q1
show the reaction diagram
-
-
-
-
r
semiquinone electron-transferring flavoprotein + ubiquinone Q1
electron-transferring flavoprotein + hydroquinone electron-transferring flavoprotein + ubiquinol Q1
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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 + ubiquinone
electron-transferring flavoprotein + ubiquinol
show the reaction diagram
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
-
ETF is the intermediate electron carrier between dehydrogenases and the enzyme, enzyme mediates between eleven mitochondrial proteins and the ubiquinone pool
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ubiquinone
[4Fe-4S]-center
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S centre
-
contains a single [4Fe-4S]2+,1+ cluster
Fe2+
-
enzyme contains iron-sulfur clusters
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(3-methylpentyl)-4,6-dinitrophenol
-
-
Pentachlorophenol
-
-
2-(3-methylpentyl)-4,6-dinitrophenol
-
noncompetitive
2-n-heptyl-4-hydroxyquinoline N-oxide
-
-
p-chloromercuribenzoate
-
complete inhibition of ubiquinone reductase activity, 70% inhibition of disproportion activity
Pentachlorophenol
-
noncompetitive
additional information
-
inhibition mechanism
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
6-bis(isoprenyl)ubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0095
6-isoprenylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0089
bromodecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0079 - 0.0084
decylubiquinone
0.0195
duroquinone
-
recombinant enzyme, pH 7.4, 25°C
0.00013 - 0.0113
electron-transferring flavoprotein
0.0082
heptylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0099
hydroxydecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0163
menadione
-
recombinant enzyme, pH 7.4, 25°C
0.0073
nonylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0023
pentadecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0154
semiquinone electron-transferring flavoprotein
-
-
-
0.0265
tridecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
0.0081
ubiquinone-1
-
-
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
68.7
6-bis(isoprenyl)ubiquinone
-
recombinant enzyme, pH 7.4, 25°C
34.5
6-isoprenylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
60.8
bromodecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
59.9 - 74.3
decylubiquinone
18.1
duroquinone
-
recombinant enzyme, pH 7.4, 25°C
21.4
electron-transferring flavoprotein
-
-
54
heptylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
67
hydroxydecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
6.6
menadione
-
recombinant enzyme, pH 7.4, 25°C
61.3
nonylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
7.4
pentadecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
81.4
semiquinone electron-transferring flavoprotein
-
-
-
31.5
tridecylubiquinone
-
recombinant enzyme, pH 7.4, 25°C
78.8
ubiqinone-2
-
-
33.5
ubiquinone-1
-
-
35.5
ubiquinone-4
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046
2-(3-methylpentyl)-4,6-dinitrophenol
-
recombinant enzyme, pH 7.4, 25°C
0.0077
Pentachlorophenol
-
recombinant enzyme, pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from thigh and limb
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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
-
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
additional information
-
electron transfer flavoprotein structure analysis and FAD binding, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ETFD_HUMAN
617
0
68495
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
67000
-
x * 67000, immunoprecipitation after in vitro translation, deduced from nucletide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
C561A
-
mutant enzyme has no ubiquinone reductase activity
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIPL by nickel affinity chromatography in presence of FAD
recombinant enzyme from Sf9 insect cells
-
recombinant enzyme, DEAE-Sepharose, HA-Ultrogel, Mono Q
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goodman, S.I.; Axtell, K.M.; Bindoff, L.A.; Beard, S.E.; Gill, R.E.; Frerman, F.E.
Molecular cloning and expression of a cDNA encoding human electron transfer flavoprotein-ubiquinone oxidoreductase
Eur. J. Biochem.
219
277-286
1994
Homo sapiens
Manually annotated by BRENDA team
Beard, S.E.; Doodman, S.I.; Bemelen, K.; Frerman, F.E.
Characterization of mutation that abolishes quinone reduction by electron transfer flavoprotein-ubiquinone oxidoreductase
Hum. Mol. Genet.
4
157-161
1995
Homo sapiens
Manually annotated by BRENDA team
Dwyer, T.M.; Mortl, S.; Kemter, K.; Bacher, A.; Fauqu, A.; Frerman, F.E.
The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer
Biochemistry
38
9735-9745
1999
Homo sapiens
Manually annotated by BRENDA team
Spector, E.B.; Seltzer, W.K.; Goodman, S.I.
Assignment of electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) to human chromosome 4q33 by fluorescence in situ hybridization and somatic cell hybridization
Mol. Genet. Metab.
67
364-367
1999
Homo sapiens
Manually annotated by BRENDA team
Simkovic, M.; Degala, G.D.; Eaton, S.S.; Frerman, F.E.
Expression of human electron transfer flavoprotein-ubiquinone oxidoreductase from baculovirus vector: kinetic and spectral characterization of the human protein
Biochem. J.
364
659-667
2002
Homo sapiens
Manually annotated by BRENDA team
Simkovic, M.; Frerman, F.E.
Alternative quinone substrates and inhibitors of human electron-transfer flavoprotein-ubiquinone oxidoreductase
Biochem. J.
378
633-640
2004
Homo sapiens
Manually annotated by BRENDA team
Goodman, S.I.; Binard, R.J.; Woontner, M.R.; Frerman, F.E.
Glutaric acidemia type II: gene structure and mutations of the electron transfer flavoprotein:ubiquinone oxidoreductase (ETF:QO) gene
Mol. Genet. Metab.
77
86-90
2002
Homo sapiens (Q16134), Homo sapiens
Manually annotated by BRENDA team
Gempel, K.; Topaloglu, H.; Talim, B.; Schneiderat, P.; Schoser, B.G.; Hans, V.H.; Palmafy, B.; Kale, G.; Tokatli, A.; Quinzii, C.; Hirano, M.; Naini, A.; DiMauro, S.; Prokisch, H.; Lochmueller, H.; Horvath, R.
The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene
Brain
130
2037-2044
2007
Homo sapiens
Manually annotated by BRENDA team
Fielding, A.J.; Usselman, R.J.; Watmough, N.; Simkovic, M.; Frerman, F.E.; Eaton, G.R.; Eaton, S.S.
Electron spin relaxation enhancement measurements of interspin distances in human, porcine, and Rhodobacter electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO)
J. Magn. Reson.
190
222-232
2008
Cereibacter sphaeroides, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Rodrigues, J.V.; Gomes, C.M.
Mechanism of superoxide and hydrogen peroxide generation by human electron-transfer flavoprotein and pathological variants
Free Radic. Biol. Med.
53
12-19
2012
Homo sapiens
Manually annotated by BRENDA team
Swanson, M.A.; Kathirvelu, V.; Majtan, T.; Frerman, F.E.; Eaton, G.R.; Eaton, S.S.
Electron transfer flavoprotein domain II orientation monitored using double electron-electron resonance between an enzymatically reduced, native FAD cofactor, and spin labels
Protein Sci.
20
610-620
2011
Homo sapiens, Paracoccus denitrificans
Manually annotated by BRENDA team
Liu, X.Y.; Jin, M.; Wang, Z.Q.; Wang, D.N.; He, J.J.; Lin, M.T.; Fu, H.X.; Wang, N.
Skeletal muscle magnetic resonance imaging of the lower limbs in late-onset lipid storage myopathy with electron transfer flavoprotein dehydrogenase gene mutations
Chin. Med. Sci.
129
1425-1431
2016
Homo sapiens (Q16134), Homo sapiens
Manually annotated by BRENDA team
Malecki, J.; Dahl, H.A.; Moen, A.; Davydova, E.; Falnes, P.O.
The METTL20 homologue from Agrobacterium tumefaciens is a dual specificity protein-lysine methyltransferase that targets ribosomal protein L7/L12 and the beta subunit of electron transfer flavoprotein (ETFbeta)
J. Biol. Chem.
291
9581-9595
2016
Agrobacterium tumefaciens (A9CJL8), Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970 (A9CJL8), Homo sapiens (Q16134), Homo sapiens
Manually annotated by BRENDA team
Shioya, A.; Takuma, H.; Yamaguchi, S.; Ishii, A.; Hiroki, M.; Fukuda, T.; Sugie, H.; Shigematsu, Y.; Tamaoka, A.
Amelioration of acylcarnitine profile using bezafibrate and riboflavin in a case of adult-onset glutaric acidemia type 2 with novel mutations of the electron transfer flavoprotein dehydrogenase (ETFDH) gene
J. Neurol. Sci.
346
350-352
2014
Homo sapiens (Q16134)
Manually annotated by BRENDA team
Fuhrmann, D.C.; Olesch, C.; Kurrle, N.; Schnuetgen, F.; Zukunft, S.; Fleming, I.; Bruene, B.
Chronic hypoxia enhances beta-oxidation-dependent electron transport via electron transferring flavoproteins
Cells
8
172
2019
Homo sapiens (Q16134)
Manually annotated by BRENDA team
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.
16
185
2017
Homo sapiens (Q16134), Homo sapiens
Manually annotated by BRENDA team