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Information on EC 1.3.8.6 - glutaryl-CoA dehydrogenase (ETF) and Organism(s) Homo sapiens

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IUBMB Comments
Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA [EC 1.3.99.32, glutaryl-CoA dehydrogenase (acceptor)].
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
glutaryl-coa dehydrogenase, glutaryl-coenzyme a dehydrogenase, gdhgeo, glutaryl coenzyme a dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutaryl coenzyme A dehydrogenase
glutaryl-CoA dehydrogenase
-
glutaryl-coenzyme A dehydrogenase
additional information
enzyme belongs to the acyl-CoA dehydrogenase family of enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein
show the reaction diagram
structural bases and mechanism of dehydrogenation and decarboxylation reactions, active site structure with and without bound substrate, Glu370 is important
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glutaryl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase (decarboxylating)
Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA [EC 1.3.99.32, glutaryl-CoA dehydrogenase (acceptor)].
CAS REGISTRY NUMBER
COMMENTARY hide
37255-38-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-thiaglutaryl-CoA + acceptor
?
show the reaction diagram
-
-
-
?
4-nitrobutyryl-CoA + acceptor
4-nitro-but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
4-nitrobutyryl-CoA + electron transfer protein
? + CO2 + reduced electron transfer protein
show the reaction diagram
-
-
-
?
5-hexenoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
glutaconyl-CoA + acceptor
crotonyl-CoA + CO2 + reduced acceptor
show the reaction diagram
glutaconyl-CoA + ferrocenium hexafluorophosphate
crotonyl-CoA + CO2 + ferricenium hexafluorophosphate
show the reaction diagram
glutaramyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
glutaryl-CoA + 2,6-dichlorophenol indophenol
crotonoyl-CoA + CO2 + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
glutaryl-CoA + acceptor
crotonoyl-CoA + CO2 + reduced acceptor
show the reaction diagram
glutaryl-CoA + acceptor
crotonyl-CoA + CO2 + reduced acceptor
show the reaction diagram
glutaryl-CoA + electron transfer flavoprotein
(E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
?
glutaryl-CoA + electron transfer flavoprotein
crotonoyl-CoA + CO2 + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
?
glutaryl-CoA + electron transfer protein
crotonoyl-CoA + CO2 + reduced electron transfer protein
show the reaction diagram
-
-
-
?
glutaryl-CoA + electron-transfer flavoprotein
crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein
show the reaction diagram
glutaryl-CoA + FAD
crotonoyl-CoA + CO2 + FADH2
show the reaction diagram
glutaryl-CoA + human electron-transfer flavoprotein
crotonyl-CoA + CO2 + reduced human electron-transfer flavoprotein
show the reaction diagram
-
-
-
-
r
glutaryl-CoA + phenazine methosulfate
crotonyl-CoA + CO2 + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
methyl-glutaryl-CoA + acceptor
methyl-crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
pentanoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
proteo-glutaryl-CoA + acceptor
crotonoyl-CoA + CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
?
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
glutaryl-CoA + acceptor
crotonoyl-CoA + CO2 + reduced acceptor
show the reaction diagram
-
part of the degradative pathway of the amino acids tryptophan, lysine, and hydroxylysine, enzyme deficiency leads to glutaric aciduria type I leading to nonspecific developmental delay, hypotonia, and macrocephaly with cerebral atrophyof prenatal onset
-
-
?
glutaryl-CoA + acceptor
crotonyl-CoA + CO2 + reduced acceptor
show the reaction diagram
glutaryl-CoA + electron transfer flavoprotein
(E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
?
glutaryl-CoA + electron transfer flavoprotein
crotonoyl-CoA + CO2 + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
?
glutaryl-CoA + electron transfer protein
crotonoyl-CoA + CO2 + reduced electron transfer protein
show the reaction diagram
-
-
-
?
glutaryl-CoA + electron-transfer flavoprotein
crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein
show the reaction diagram
overall reaction
-
-
?
glutaryl-CoA + FAD
crotonoyl-CoA + CO2 + FADH2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
electron transferring flavoprotein
ETF, the GCDH natural electron acceptor
phenazine methosulfate
PMS, an artificial electron acceptor
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-pentynoyl-CoA
mechanism-based inactivation, inhibition kinetics
3-thiaglutaryl-CoA
non-oxidizable analogue, which competes with 2-pentynoyl-CoA for the binding site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
4-nitrobutyryl-CoA
-
-
0.105
5-hexenoyl-CoA
-
-
0.004
crotonyl-CoA
-
-
0.0002 - 0.0011
electron transfer flavoprotein
0.003
glutaconyl-CoA
-
-
0.0066
glutaramyl-CoA
-
-
0.003 - 0.0481
glutaryl-CoA
0.085
hexanoyl-CoA
-
-
0.042
human electron-transfer flavoprotein
-
-
-
0.02
methyl-glutaryl-CoA
-
-
0.024
pentanoyl-CoA
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
4-nitrobutyryl-CoA
-
oxidase activity
4.8
dichlorophenolindophenol
-
-
5.7
electron-transfer flavoprotein
-
-
7.5
ferrocenium hexafluorophosphate
-
-
2.04 - 5.5
glutaconyl-CoA
0.023 - 13.2
glutaryl-CoA
3.1
human electron-transfer flavoprotein
-
recombinant protein
-
4.8
phenazine methosulfate
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.4 - 146.92
glutaryl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069 - 0.0228
3-thiaglutaryl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00036
-
recombinant mutant T429M, crude enzyme extract
0.00086
-
recombinant mutant A421V, crude enzyme extract
0.00151
-
recombinant mutant A321T, crude enzyme extract
0.00174
-
recombinant wild-type enzyme, crude enzyme extract
0.0097
-
recombinant mutant A433V, crude enzyme extract
112
recombinant mutant R227P with PMS, pH 7.8, temperature not specified in the publication
1683
recombinant mutant V400M with PMS, pH 7.8, temperature not specified in the publication
205
recombinant wild-type enzyme with ETF, pH 7.8, temperature not specified in the publication
2224
recombinant wild-type enzyme with PMS, pH 7.8, temperature not specified in the publication
5
recombinant mutant R227P with ETF, pH 7.8, temperature not specified in the publication
70
recombinant mutant V400M with ETF, pH 7.8, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8
-
assay at, electron acceptor 2,6-dichlorophenol indophenol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
overexpression of GCDH
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
glutaryl-CoA dehydrogenase belongs to the acyl-CoA dehydrogenase enzyme family
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GCDH_HUMAN
438
0
48127
Swiss-Prot
Mitochondrion (Reliability: 1), Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
256000
-
gel filtration
43600
-
4 * 43600, recombinant wild-type enzyme, SDS-PAGE
58800
-
4 * 58800, SDS-PAGE
additional information
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
15 mg/ml purified recombinant enzyme in 20 mM HEPES, pH 7.5, 100 mM NaCl, enzyme is free or in complex with 4-nitrobutyryl-CoA, hanging drop vapour diffusion method, equal volumes of protein and precipitant solution, the latter containing 100 mM MES, pH 6.5, 30% PEG monomethyl ether 5000, 0.2 M ammonium sulfate, 19°C, addition of 0.1% octyl beta-D-glucopyranoside, 0.4 mM acetoacetyl-CoA, with or without addition of 0.4 mM 4-nitrobutyryl-CoA, X-ray diffraction structure determination and analysis at 2.1 A and 2.6 A resolution, respectively
hanging drop vapour diffusion method with 100 mM MES buffer, pH 6.5, 30% poly(ethyleneglycol) monomethyl ether 5000, and 0.2 M ammonium sulfate, at 19°C, in complex with 4-nitrobutyric acid
purified GDH, hanging drop vapor diffusion method, 10 mg/ml protein in 10 mM MES, pH 6.0, 0.5 M KCl, 10% w/v glycerol, 1 mM DTT, 1 mM FAD, and glutaryl-CoA, are mixed with an equal volume of reservoir solution containing 15% v/v MPD, 0.1 M imidazole, pH 6.5, 0.2 M KCl, and 2% PEG 3350, at 4°C, 2 days, X-ray diffraction structure determination and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A293T
-
naturally occruing mutation in GCDH
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
-
site-directed mutagenesis, altered Km, kcat is only slightly affected, slightly reduced activity compared to the wild-type enzyme
A421V
-
site-directed mutagenesis, altered Km, kcat is only slightly affected, reduced activity compared to the wild-type enzyme
A433E
-
site-directed mutagenesis, nearly inactive mutant
A433V
-
site-directed mutagenesis, altered Km, kcat is only slightly affected, reduced activity compared to the wild-type enzyme
C1296T
-
the mutation leads to glutaryl-CoA dehydrogenase deficiency
E370D
E370Q
F236L/S259P
-
this genotype exhibits 3% GCDH activity
G171W/V410M
-
this genotype exhibits 8% GCDH activity
M1V/R227P
-
this genotype exhibits 4% GCDH activity
M263V
-
analysis of a naturally occurring mutation in a Turkish patient with glutaric aciduria type I
Q59P
-
naturally occruing mutation in GCDH
R161Q/C228R
-
this genotype exhibits 25% GCDH activity
R227P
R402W
-
naturally occruing mutation in GCDH
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
S225W
-
this genotype exhibits 6% GCDH activity
T385M
naturally occurring mutation from patient with glutaric acidemia type I, dissociation to inactive monomers or dimers
T429M
-
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
Y155H/A421V
-
this genotype exhibits 5% GCDH activity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43 - 53
apparent thermal denaturation midpoint (Tm) of GCDH wild -type and mutants using different techniques, overview
51.9
-
denaturation of mutant A421V, pH 7.0
52
-
denaturation of mutant A433V, pH 7.0
53.7
-
denaturation of mutant T429M, pH 7.0
55.7
-
denaturation of mutant A421T, pH 7.0
63.8
-
denaturation of recombinant wild-type enzyme, pH 7.0
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Escherichia coli, except for mutant A433E, different yields from recombinant cell culture
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
-
GCDH genotyping in black South African population, overview
-
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
wild type and mutant of patient with glutaric acidemia type I
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lenich, A.C.; Goodman, S.I.
The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver
J. Biol. Chem.
261
4090-4096
1986
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Liesert, M.; Zschocke, J.; Hoffmann, G.F.; Muhlhauser, N.; Buckel, W.
Biochemistry of glutaric aciduria type I: activities of in vitro expressed wild-type and mutant cDNA encoding human glutaryl-CoA dehydrogenase
J. Inherit. Metab. Dis.
22
256-258
1999
Homo sapiens
Manually annotated by BRENDA team
Goodman, S.I.; Kratz, L.E.; DiGiulio, K.A.; Biery, B.J.; Goodman, K.E.; Isaya, G.; Frerman, F.E.
Cloning of glutaryl-CoA dehydrogenase cDNA, and expression of wild type and mutant enzymes in Escherichia coli
Hum. Mol. Genet.
4
1493-1498
1995
Homo sapiens
Manually annotated by BRENDA team
Goodman, S.I.; Stein, D.E.; Schlesinger, S.; Christensen, E.; Schwartz, M.; Greenberg, C.R.; Elpeleg, O.N.
Glutaryl-CoA dehydrogenase mutations in glutaric acidemia (type I): Review and report of thirty novel mutations
Hum. Mutat.
12
141-144
1998
Homo sapiens
Manually annotated by BRENDA team
Dwyer, T.M.; Rao, K.S.; Goodman, S.I.; Frerman, F.E.
Proton abstraction reaction, steady-state kinetics, and oxidation-reduction potential of human glutaryl-CoA dehydrogenase
Biochemistry
39
11488-11499
2000
Homo sapiens
Manually annotated by BRENDA team
Westover, J.B.; Goodman, S.I.; Frerman, F.E.
Binding, hydration, and decarboxylation of the reaction intermediate glutaconyl-Coenzyme A by human Glutaryl-CoA dehydrogenase
Biochemistry
40
14106-14114
2001
Homo sapiens
Manually annotated by BRENDA team
Rao, K.S.; Vander Velde, D.; Dwyer, T.M.; Goodman, S.I.; Frerman, F.E.
Alternate substrates of human glutaryl-CoA dehydrogenase: Structure and reactivity of substrates, and identification of a novel 2-enoyl-CoA product
Biochemistry
41
1274-1284
2002
Homo sapiens
Manually annotated by BRENDA team
Dwyer, T.M.; Rao, K.S.; Westover, J.B.; Kim, J.J.P.; Frerman, F.E.
The function of Arg-94 in the oxidation and decarboxylation of glutaryl-CoA by human glutaryl-CoA dehydrogenase
J. Biol. Chem.
276
133-138
2001
Homo sapiens
Manually annotated by BRENDA team
Fu, Z.; Wang, M.; Paschke, R.; Rao, K.S.; Frerman, F.E.; Kim, J.J.
Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions
Biochemistry
43
9674-9684
2004
Homo sapiens (Q92947), Homo sapiens
Manually annotated by BRENDA team
Rao, K.S.; Albro, M.; Vockley, J.; Frerman, F.E.
Mechanism-based inactivation of human glutaryl-CoA dehydrogenase by 2-pentynoyl-CoA: rationale for enhanced reactivity
J. Biol. Chem.
278
26342-26350
2003
Homo sapiens (Q92947), Homo sapiens
Manually annotated by BRENDA team
Muehlhausen, C.; Christensen, E.; Schwartz, M.; Muschol, N.; Ullrich, K.; Lukacs, Z.
Severe phenotype despite high residual glutaryl-CoA dehydrogenase activity: a novel mutation in a Turkish patient with glutaric aciduria type I
J. Inherit. Metab. Dis.
26
713-714
2003
Homo sapiens
Manually annotated by BRENDA team
Treacy, E.P.; Lee-Chong, A.; Roche, G.; Lynch, B.; Ryan, S.; Goodman, S.
Profound neurological presentation resulting from homozygosity for a mild glutaryl-CoA dehydrogenase mutation with a minimal biochemical phenotype
J. Inherit. Metab. Dis.
26
72-74
2003
Homo sapiens
Manually annotated by BRENDA team
Westover, J.B.; Goodman, S.I.; Frerman, F.E.
Pathogenic mutations in the carboxyl-terminal domain of glutaryl-CoA dehydrogenase: effects on catalytic activity and the stability of the tetramer
Mol. Genet. Metab.
79
245-256
2003
Homo sapiens
Manually annotated by BRENDA team
Rao, K.S.; Albro, M.; Zirrolli, J.A.; Vander Velde, D.; Jones, D.N.M.; Frerman, F.E.
Protonation of crotonyl-CoA dienolate by human glutaryl-CoA dehydrogenase occurs by solvent-derived protons
Biochemistry
44
13932-13940
2005
Homo sapiens
Manually annotated by BRENDA team
Rao, K.S.; Albro, M.; Dwyer, T.M.; Frerman, F.E.
Kinetic mechanism of glutaryl-CoA dehydrogenase
Biochemistry
45
15853-15861
2006
Homo sapiens (Q92947)
Manually annotated by BRENDA team
Yeh, C.S.; Wang, J.Y.; Cheng, T.L.; Juan, C.H.; Wu, C.H.; Lin, S.R.
Fatty acid metabolism pathway play an important role in carcinogenesis of human colorectal cancers by Microarray-Bioinformatics analysis
Cancer Lett.
233
297-308
2006
Homo sapiens
Manually annotated by BRENDA team
Rao, K.S.; Fu, Z.; Albro, M.; Narayanan, B.; Baddam, S.; Lee, H.J.; Kim, J.J.; Frerman, F.E.
The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate
Biochemistry
46
14468-14477
2007
Homo sapiens (Q92947)
Manually annotated by BRENDA team
Strauss, K.A.; Lazovic, J.; Wintermark, M.; Morton, D.H.
Multimodal imaging of striatal degeneration in Amish patients with glutaryl-CoA dehydrogenase deficiency
Brain
130
1905-1920
2007
Homo sapiens
Manually annotated by BRENDA team
Koelker, S.; Christensen, E.; Leonard, J.V.; Greenberg, C.R.; Burlina, A.B.; Burlina, A.P.; Dixon, M.; Duran, M.; Goodman, S.I.; Koeller, D.M.; Mueller, E.; Naughten, E.R.; Neumaier-Probst, E.; Okun, J.G.; Kyllerman, M.; Surtees, R.A.; Wilcken, B.; Hoffmann, G.F.; Burgard, P.
Guideline for the diagnosis and management of glutaryl-CoA dehydrogenase deficiency (glutaric aciduria type I)
J. Inherit. Metab. Dis.
30
5-22
2007
Homo sapiens
Manually annotated by BRENDA team
Sauer, S.W.
Biochemistry and bioenergetics of glutaryl-CoA dehydrogenase deficiency
J. Inherit. Metab. Dis.
30
673-680
2007
Homo sapiens
Manually annotated by BRENDA team
Lopez-Laso, E.; Garcia-Villoria, J.; Martin, E.; Duque, P.; Cano, A.; Ribes, A.
Classic and late-onset neurological disease in two siblings with glutaryl-CoA dehydrogenase deficiency
J. Inherit. Metab. Dis.
30
979
2007
Homo sapiens
Manually annotated by BRENDA team
McClelland Verity , M.V.; Gissen Pau, G.P.; Hendriksz Chri, H.C.; Chakrapani Anupa, C.A.
Glutaryl-CoA dehydrogenase deficiency
Pediatr. Res.
61
134-135
2007
Homo sapiens
-
Manually annotated by BRENDA team
Koelker, S.; Garbade, S.F.; Boy, N.; Maier, E.M.; Meissner, T.; Muehlhausen, C.; Hennermann, J.B.; Luecke, T.; Haeberle, J.; Baumkoetter, J.; Haller, W.; Muller, E.; Zschocke, J.; Burgard, P.; Hoffmann, G.F.
Decline of acute encephalopathic crises in children with glutaryl-CoA dehydrogenase deficiency identified by newborn screening in Germany
Pediatr. Res.
62
357-363
2007
Homo sapiens
Manually annotated by BRENDA team
Wischgoll, S.; Demmer, U.; Warkentin, E.; Guenther, R.; Boll, M.; Ermler, U.
Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme A dehydrogenases
Biochemistry
49
5350-5357
2010
Homo sapiens (Q92947)
Manually annotated by BRENDA team
Strauss, K.A.; Donnelly, P.; Wintermark, M.
Cerebral haemodynamics in patients with glutaryl-coenzyme A dehydrogenase deficiency
Brain
133
76-92
2010
Homo sapiens
Manually annotated by BRENDA team
van der Watt, G.; Owen, E.P.; Berman, P.; Meldau, S.; Watermeyer, N.; Olpin, S.E.; Manning, N.J.; Baumgarten, I.; Leisegang, F.; Henderson, H.
Glutaric aciduria type 1 in South Africa-high incidence of glutaryl-CoA dehydrogenase deficiency in black South Africans
Mol. Genet. Metab.
101
178-182
2010
Homo sapiens
Manually annotated by BRENDA team
Begley, D.W.; Davies, D.R.; Hartley, R.C.; Hewitt, S.N.; Rychel, A.L.; Myler, P.J.; Van Voorhis, W.C.; Staker, B.L.; Stewart, L.J.
Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening
Acta Crystallogr. Sect. F
67
1060-1069
2011
Homo sapiens, Burkholderia pseudomallei (Q3JP94), Burkholderia pseudomallei, Burkholderia pseudomallei 1710b (Q3JP94)
Manually annotated by BRENDA team
Schmiesing, J.; Lohmoeller, B.; Schweizer, M.; Tidow, H.; Gersting, S.W.; Muntau, A.C.; Braulke, T.; Muehlhausen, C.
Disease-causing mutations affecting surface residues of mitochondrial glutaryl-CoA dehydrogenase impair stability, heteromeric complex formation and mitochondria architecture
Hum. Mol. Genet.
26
538-551
2017
Homo sapiens (Q92947), Homo sapiens
Manually annotated by BRENDA team
Schmiesing, J.; Schlueter, H.; Ullrich, K.; Braulke, T.; Muehlhausen, C.
Interaction of glutaric aciduria type 1-related glutaryl-CoA dehydrogenase with mitochondrial matrix proteins
PLoS ONE
9
e87715
2014
Homo sapiens (Q92947), Homo sapiens
Manually annotated by BRENDA team
Ribeiro, J.; Lucas, T.; Bross, P.; Gomes, C.; Henriques, B.
Potential complementation effects of two disease-associated mutations in tetrameric glutaryl-CoA dehydrogenase is due to inter subunit stability-activity counterbalance
Biochim. Biophys. Acta
1868
140269
2020
Homo sapiens (Q92947), Homo sapiens
Manually annotated by BRENDA team