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malfunction
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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
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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
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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
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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
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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
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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
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malfunction
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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
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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
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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
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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
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the enzyme is maternally required for Drosophila embryogenesis
physiological function
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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
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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
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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
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physiological function
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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
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physiological function
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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
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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
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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
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enzyme protein structure homology-modeling, overview