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
-
glutaconic
-
intercurrent
-
3-oh-ga
-
frontotemporal
-
neuroradiological
- acylcarnitine
-
excretors
- medicine
- glutaconyl-coa
-
acidaemia
-
subdural
- isovaleryl-coa
-
glutarylation
-
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
1.3.8.6 glutaryl-CoA dehydrogenase (ETF)Advanced search results
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results (Engineering
Engineering on EC 1.3.8.6 - glutaryl-CoA dehydrogenase (ETF)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A377T
naturally occurring mutation from patient with glutaric acidemia type I, dissociation to inactive monomers or dimers
A377V
naturally occurring mutation from patient with glutaric acidemia type I, dissociation to inactive monomers or dimers
A389E
naturally occurring mutation from patient with glutaric acidemia type I, dissociation to inactive monomers or dimers
A389V
naturally occurring mutation from patient with glutaric acidemia type I, dissociation to inactive monomers or dimers
A421T
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site-directed mutagenesis, altered Km, kcat is only slightly affected, slightly reduced activity compared to the wild-type enzyme
A421V
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site-directed mutagenesis, altered Km, kcat is only slightly affected, reduced activity compared to the wild-type enzyme
A433V
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site-directed mutagenesis, altered Km, kcat is only slightly affected, reduced activity compared to the wild-type enzyme
E370D
E370Q
M263V
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analysis of a naturally occurring mutation in a Turkish patient with glutaric aciduria type I
R227P
R88A
expression of mutant results in the disruption of mitochondrial architecture forming longitudinal structures composed of stacks of cristae and partial loss of the outer mitochondrial membrane
R88C
expression of mutant results in the disruption of mitochondrial architecture forming longitudinal structures composed of stacks of cristae and partial loss of the outer mitochondrial membrane
R88K
expression of mutant results in the disruption of mitochondrial architecture forming longitudinal structures composed of stacks of cristae and partial loss of the outer mitochondrial membrane
R88M
expression of mutant results in the disruption of mitochondrial architecture forming longitudinal structures composed of stacks of cristae and partial loss of the outer mitochondrial membrane
T385M
naturally occurring mutation from patient with glutaric acidemia type I, dissociation to inactive monomers or dimers
T429M
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site-directed mutagenesis, altered Km, kcat is only slightly affected, reduced activity compared to the wild-type enzyme
V400M
a naturally occuring GCDH disease-related mutation involved in glutaric aciduria type I (GA-I). Heterozygous patients harbouring the two mutations GCDH-p.Arg227Pro and GCDH-p.Val400Met show increased residual enzymatic activity in relation to homozygous patients with only one of the mutations, suggesting a complementation effect between the two. Thermal stress affects cofactor binding in the GCDH-p.Val400Met mutant. In vivo the p.Val400Met variant displays impaired interaction with the partner ETF, resulting in the lower values observed in patient fibroblasts. The mutant shows 24% reduced activity compared to wild-type
Y155H
mutant exhibits a reduced interaction with dihydrolipoamide succinyl transferase
E370Q
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site-directed mutagenesis, the mutant shows highy reduced activity compared to the wild-type enzyme
additional information
E370D
mutant is more sensitive against inactivation by 3-thiaglutaryl-CoA compared to the wild-type enzyme, irreversible inactivation
E370D
the mutation results in a 24% decrease in the rate constant for proton abstraction at C-2 of 3-thiaglutaryl-CoA, the net rate constant for flavin reduction due to hydride transfer from C-3 of the natural substrate decreases by 81% due to the mutation
E370Q
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does not catalyze detectable exchange of 4c methyl protons of crotonyl-CoA
E370Q
the dienolate intermediate observed upon decarboxylation of glutaconyl-CoA can be detected with E370Q GCD but not with wild-type, because the crotonyl-CoA dienolate forms a charge-transfer complex with the oxidized FAD and the substitution of a glutamine residue for Glu370 prevents rapid protonation of the dienolate
R227P
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naturally occurring mutation leading to reduced enzyme activity, mildly altered phenotype, physiological analysis, absence of glutarate and 3-hydroxyglutarate in serum and in urine, overview
R227P
a naturally occuring GCDH disease-related mutation involved in glutaric aciduria type I (GA-I). Heterozygous patients harbouring the two mutations GCDH-p.Arg227Pro and GCDH-p.Val400Met show increased residual enzymatic activity in relation to homozygous patients with only one of the mutations, suggesting a complementation effect between the two. The mutant shows 95% reduced activity compared to wild-type
additional information
the CIBdgcdR mutant strain is unable to grow in pimelate, glutarate or benzoate as sole carbon sources
additional information
studies of 18 missense mutations identified in glutaric aciduria type 1 patients affecting surface amino acids. The stability of half of the GCDH mutants is significantly reduced. None of the mutations impairs the 3D structure of GCDH. All GCDH mutants are correctly translocated into mitochondria
additional information
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studies of 18 missense mutations identified in glutaric aciduria type 1 patients affecting surface amino acids. The stability of half of the GCDH mutants is significantly reduced. None of the mutations impairs the 3D structure of GCDH. All GCDH mutants are correctly translocated into mitochondria
additional information
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constructionof a lentiviral vector containing short hairpin RNA targeted against the GCDH gene expression (lentivirus-shRNA) in neurons
additional information
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constructionof a lentiviral vector containing short hairpin RNA targeted against the GCDH gene expression (lentivirus-shRNA) in neurons
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