Information on EC 1.3.8.6 - glutaryl-CoA dehydrogenase (ETF)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.8.6
-
RECOMMENDED NAME
GeneOntology No.
glutaryl-CoA dehydrogenase (ETF)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(E)-glutaconyl-CoA = crotonyl-CoA + CO2
show the reaction diagram
(1b)
-
-
-
glutaryl-CoA + electron-transfer flavoprotein = (E)-glutaconyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
(1a)
-
-
-
glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
-
-
Biosynthesis of antibiotics
-
-
Fatty acid degradation
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Tryptophan metabolism
-
-
tryptophan metabolism
-
-
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 4.1.1.70, 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).
CAS REGISTRY NUMBER
COMMENTARY hide
37255-38-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CIB
UniProt
Manually annotated by BRENDA team
strain CIB
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
an FeIII reducing organism
-
-
Manually annotated by BRENDA team
strain KT2440
-
-
Manually annotated by BRENDA team
strains KB 740, K 172
-
-
Manually annotated by BRENDA team
fruit-eating bat
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
-
glutaryl-CoA dehydrogenase activity is required for the catabolism of the essential ketogenic amino acids lysine and tryptophan
additional information
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
-
-
-
-
?
butyryl-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 + FAD
(E)-but-2-enoyl-CoA + CO2 + FADH2
show the reaction diagram
glutaryl-CoA + FAD
crotonoyl-CoA + CO2 + FADH2
show the reaction diagram
glutaryl-CoA + ferricenium hexafluorophosphate
crotonyl-CoA + CO2 + ferrocenium hexafluorophosphate
show the reaction diagram
glutarylpantetheine + acceptor
crotonylpantetheine + reduced acceptor
show the reaction diagram
hexanoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
isovaleryl-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 SUBSTRATES
NATURAL PRODUCTS
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
Q92947
-
-
-
?
glutaryl-CoA + FAD
(E)-but-2-enoyl-CoA + CO2 + FADH2
show the reaction diagram
glutaryl-CoA + FAD
crotonoyl-CoA + CO2 + FADH2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
-
additional information
-
electron acceptor: 2,6-dichlorophenol indophenol
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-pentynoyl-CoA
3-Butynoylpantetheine
-
irreversible
3-Pentynoylpantetheine
-
irreversible
3-thiaglutaryl-CoA
-
non-oxidizable analogue, which competes with 2-pentynoyl-CoA for the binding site
Co2+
-
-
crotonyl-CoA
-
-
Cu2+
-
-
glutaconyl-CoA
-
-
oct-2-yn-4-enoyl-CoA
-
irreversible and most likely involved covalent modification of the apoenzyme
p-chloromercuribenzoate
-
-
Zn2+
-
-
additional information
-
no inhibition by glutaconyl-CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
exogenous
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
0.0011 - 0.0025
electron-transfer flavoprotein
0.003 - 0.011
glutaconyl-CoA
0.0066
glutaramyl-CoA
-
-
0.0012 - 3.8
glutaryl-CoA
2
Glutarylpantetheine
-
-
0.085
Hexanoyl-CoA
-
-
0.042
human electron transfer protein
-
-
-
0.02
methyl-glutaryl-CoA
-
-
0.024
pentanoyl-CoA
-
-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
4-nitrobutyryl-CoA
Homo sapiens
-
oxidase activity
4.8
dichlorophenolindophenol
Homo sapiens
-
-
14.3 - 16
electron transfer flavoprotein
5.7
electron transfer protein
Homo sapiens
-
-
-
7.5
ferrocenium hexafluorophosphate
Homo sapiens
-
-
2.04 - 5.5
glutaconyl-CoA
0.004 - 13.2
glutaryl-CoA
3.1
human electron transfer protein
Homo sapiens
-
recombinant protein
-
4.8
phenazine methosulfate
Homo sapiens
-
-
16
phenylmethylsulfonyl fluoride
Paracoccus denitrificans
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 950
glutaryl-CoA
656
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069 - 0.0228
3-thiaglutaryl-CoA
additional information
additional information
-
inhibition kinetics
-
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
0.028
in cells grown in 0.2% (w/v) pyruvate
0.169
in cells grown in 3 mM pimelate
0.19
in cells grown in 0.2% (w/v) pyruvate and 3 mM pimelate
0.216
in cells grown in 3 mM benzoate
2.3
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
glutaryl-CoA + methylene blue
7.5
-
assay at
7.5 - 8
-
-
8
-
assay at, electron acceptor 2,6-dichlorophenol indophenol
8 - 8.5
-
glutaryl-CoA + electron-transfer flavoprotein
8.6
-
glutaryl-CoA + electron-transfer flavoprotein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
28
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
overexpression of GCDH
Manually annotated by BRENDA team
additional information
-
distribution in various tissues
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
4 * 41000, SDS-PAGE
43000
-
4 * 43000, SDS-PAGE
43600
-
4 * 43600, recombinant wild-type enzyme, SDS-PAGE
45000
SDS-PAGE
47000
-
4 * 47000, SDS-PAGE
58800
-
4 * 58800, SDS-PAGE
170000
-
gel filtration
180000
-
gel filtration
190500
-
gel filtration
200000
-
gel filtration
256000
-
gel filtration
additional information
-
-
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
4 * 43000-44000
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified detagged recombinant apoenzyme without FAD, sitting drop vapor diffusion method, 26 mg/ml protein in 25 mM Tris pH 8.0, 200 mM NaCl, 1% glycerol, and 1 mM TCEP, with reservoir solution consisting of 20% PEG 3000, 100 mM HEPES, 200 mM NaCl, pH 7.5, 16C, X-ray diffraction structure determination and analysis at 1.99-2.40 A resolution
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, 19C, 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 19C, 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 4C, 2 days, X-ray diffraction structure determination and analysis
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
rapid loss of activity at pH over 7
391409
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM potassium phosphate, 150 mM NaCl, pH 6.4, several months without loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme GDHGeo from benzoate-grown cells by two different steps of anion exchange chromatography and gel filtration
-
partial
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli, except for mutant A433E, different yields from recombinant cell culture
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination annd analysis, phylogenetic tree, expression with a cleavable 6-His fusion tag followed by the human rhinovirus 3C protease-cleavage sequence in Escherichia coli strain BL21 (DE3)
expressed in Escherichia coli
-
expressed in Escherichia coli D5alpha and MC4100 cells
expressed in the Azoarcus sp. CIBdgcdR mutant strain
-
expression of wild-type and mutant enzymes in Escherichia coli
-
GCDH genotyping in black South African population, overview
-
wild type and mutant of patient with glutaric acidemia type I
-
ENGINEERING
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
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
-
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
R402W
-
naturally occruing mutation in GCDH
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
Y155H/A421V
-
this genotype exhibits 5% GCDH activity
E370A
-
site-directed mutagenesis, inactive mutant
E370Q
-
site-directed mutagenesis, the mutant shows highy reduced activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
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