1.3.8.6: glutaryl-CoA dehydrogenase (ETF)
This is an abbreviated version!
For detailed information about glutaryl-CoA dehydrogenase (ETF), go to the full flat file.
Word Map on EC 1.3.8.6
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1.3.8.6
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glutaric
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aciduria
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3-hydroxyglutaric
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striatal
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dystonia
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encephalopathic
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ga1
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macrocephaly
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inborn
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neurometabolic
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crises
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glutarylcarnitine
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hydroxylysine
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carnitine
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crotonyl-coa
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glutaconic
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intercurrent
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3-oh-ga
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frontotemporal
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neuroradiological
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acylcarnitine
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excretors
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medicine
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glutaconyl-coa
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acidaemia
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subdural
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isovaleryl-coa
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glutarylation
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sylvian
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pharmacology
- 1.3.8.6
-
glutaric
- aciduria
-
3-hydroxyglutaric
- striatal
- dystonia
-
encephalopathic
- ga1
-
macrocephaly
-
inborn
-
neurometabolic
- crises
-
glutarylcarnitine
- hydroxylysine
- carnitine
- crotonyl-coa
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glutaconic
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intercurrent
-
3-oh-ga
-
frontotemporal
-
neuroradiological
- acylcarnitine
-
excretors
- medicine
- glutaconyl-coa
-
acidaemia
-
subdural
- isovaleryl-coa
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glutarylation
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sylvian
- pharmacology
Reaction
Synonyms
decarboxylating glutaryl-coenzyme A dehydrogenase, EC 1.3.99.7, GCD, GCDH, GDH, GDHGeo, glutaryl coenzyme A dehydrogenase, glutaryl-CoA dehydrogenase, glutaryl-coenzyme A dehydrogenase, More
ECTree
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General Information
General Information on EC 1.3.8.6 - glutaryl-CoA dehydrogenase (ETF)
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evolution
malfunction
metabolism
physiological function
additional information
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glutaryl-CoA dehydrogenase belongs to the acyl-CoA dehydrogenase enzyme family
evolution
glutaryl-CoA dehydrogenase belongs to the acyl-CoA dehydrogenase enzyme family, phylogenetic tree, overview
evolution
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the enzyme is a member of the acyl-CoA dehydrogenase (ACD) family of flavoproteins
evolution
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glutaryl-CoA dehydrogenase belongs to the acyl-CoA dehydrogenase enzyme family, phylogenetic tree, overview
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injection of (3H)-labeled 3-hydroxyglutaric acid into 6 week-old Gcdh knockout mice, a model of glutaric aciduria type 1, reveal a low recovery in kidney, liver, or brain tissue that does not differ from control mice. Significant amounts of 3-hydroxyglutaric acid are found to be excreted via the intestinal tract. Exposure of knockout mice to a high protein diet leads to an encephalopathic crisis, vacuolization in the brain, and death after 4-5 days. Under these conditions, high amounts of injected 3H-3-hydroxyglutaric acid are found in kidneys of Gcdh knockout mice, whereas the radioactivity recovered in brain and blood is reduced. The data demonstrate that under conditions mimicking encephalopathic crises the blood-brain barrier appears to remain intact
malfunction
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defects in glutaryl-CoA dehydrogenase are involved in glutaric acidemia type 1, an inherited metabolic disorder which can cause macrocephaly, muscular rigidity, spastic paralysis and other progressive movement disorders in humans
malfunction
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in glutaric aciduria type 1, glutaryl-CoA dehydrogenase deficiency is responsible for the accumulation of glutaric acid and striatal degeneration, GA1-induced striatal degeneration is partially caspase-dependent, mechanism, overview
malfunction
glutaric aciduria type I (GA-I) is an autosomal recessive neurometabolic disease caused by mutations in the GCDH gene that encodes for glutaryl-CoA dehydrogenase (GCDH), a flavoprotein involved in the metabolism of tryptophan, lysine and hydroxylysin
malfunction
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in glutaric aciduria type 1, glutaryl-CoA dehydrogenase deficiency is responsible for the accumulation of glutaric acid and striatal degeneration, GA1-induced striatal degeneration is partially caspase-dependent, mechanism, overview
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glutaryl-coenzyme A dehydrogenases involved in amino acid degradation catalyze both the dehydrogenation and decarboxylation of glutaryl-CoA to crotonoyl-CoA and CO2
metabolism
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the enzyme catalyzes an intermediate step in the metabolic breakdown of lysine and tryptophan
metabolism
the enzyme catalyzes an intermediate step in the metabolic breakdown of lysine and tryptophan
metabolism
glutaryl-CoA dehydrogenase (GCDH), a flavoprotein, is involved in the metabolism of tryptophan, lysine and hydroxylysin
metabolism
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the enzyme catalyzes an intermediate step in the metabolic breakdown of lysine and tryptophan
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glutaryl-CoA dehydrogenase activity is required for the catabolism of the essential ketogenic amino acids lysine and tryptophan
physiological function
GCDH interacts directly, among others, with mitochondrial proteins, dihydrolipoamide S-succinyltransferase involved in the formation of glutaryl-CoA, and the beta-subunit of the electron transfer flavoprotein serving as electron acceptordihydrolipoamide S-succinyltransferase involved in the formation of glutaryl-CoA, and the beta-subunit of the electron transfer flavoprotein serving as electron acceptor
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glutaric aciduria type 1, GA 1, cause by glutaryl-CoA dehydrogenase deficiency, is an inherited disorder of lysine and tryptophan catabolism that typically manifests in infants with acute cerebral injury associated with intercurrent illness, phenotypoes in black South African population, overview
additional information
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Glutaryl-CoA dehydrogenase deficiency causes glutaric aciduria type 1, GA1, an autosomal recessive disorder of mitochondrial lysine and tryptophan degradation. In glutaric aciduria type 1, glutaryl-CoA and its derivatives are produced from intracerebral lysine and entrapped at high concentrations within the brain, where they interfere with energy metabolism. Biochemical toxicity triggers stroke-like striatal degeneration in susceptible children under 2 years of age. Although metabolic toxicity appears central to the pathophysiology of striatal necrosis, cerebrovascular changes probably also contribute to the process. Cerebral haemodynamics and the glutaric aciduria type 1 toxidrome, phenotype with atrophic striatal lesions, increased cerebrospinal fluid volume, interstitial brain oedema, acute striatal degeneration, low regional cerebral blood volume and signs of ischaemia, detailed overview in Amish population patients
additional information
the apo structure of GCDH from Burkholderia pseudomallei reveals a loss of secondary structure and increased disorder in the cofactor-binding pocket relative to the ternary complex of the highly homologous human GCDH
additional information
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the apo structure of GCDH from Burkholderia pseudomallei reveals a loss of secondary structure and increased disorder in the cofactor-binding pocket relative to the ternary complex of the highly homologous human GCDH
additional information
structure comparisons of wild-type and mutant enzyme proteins, FAD binding structures, overview
additional information
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structure comparisons of wild-type and mutant enzyme proteins, FAD binding structures, overview
additional information
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the apo structure of GCDH from Burkholderia pseudomallei reveals a loss of secondary structure and increased disorder in the cofactor-binding pocket relative to the ternary complex of the highly homologous human GCDH
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