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Information on EC 4.2.1.167 - (R)-2-hydroxyglutaryl-CoA dehydratase
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4.2.1.167 (R)-2-hydroxyglutaryl-CoA dehydrataseIUBMB Comments
The enzymes from the bacteria Acidaminococcus fermentans and Clostridium symbiosum are involved in the fermentation of L-glutamate. The enzyme contains [4Fe-4S] clusters, FMNH2 and riboflavin. It must be activated by an activator protein. Once activated, it can catalyse many turnovers.
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The enzyme appears in viruses and cellular organisms
Synonyms
(r)-2-hydroxyglutaryl-coa dehydratase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hgdAB
HgdC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxyglutaryl-CoA = (E)-glutaconyl-CoA + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxyglutaryl-CoA hydro-lyase ((E)-glutaconyl-CoA-forming)
The enzymes from the bacteria Acidaminococcus fermentans and Clostridium symbiosum are involved in the fermentation of L-glutamate. The enzyme contains [4Fe-4S] clusters, FMNH2 and riboflavin. It must be activated by an activator protein. Once activated, it can catalyse many turnovers.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
butynedioyl-CoA
oxaloacetate + CoA
Q9X5B7; Q9X5B8
-
initial products are 2-hydroxyfumaroyl-CoA or 2-hydroxymalyl-CoA which tautomerize to oxaloacetyl-CoA. The latter spontaneously hydrolyzes to oxaloacetate and coenzyme A
-
?
muconyl-CoA
?
Q9X5B7; Q9X5B8
hydration of butynedioyl-CoA most likely leads to 2-oxosuccinyl-CoA, which spontaneously hydrolyzes to oxaloacetate and CoASH
-
-
r
S-(R)-2-hydroxyglutarylpantetheine
S-(E)-glutaconylpantetheine + H2O
Q9X5B7; Q9X5B8
-
-
-
r
(E)-glutaconyl-CoA + H2O
(R)-2-hydroxyglutaryl-CoA
-
-
-
-
r
(E)-glutaconyl-CoA + H2O
(R)-2-hydroxyglutaryl-CoA
Q9X5B7; Q9X5B8
-
-
-
r
(E)-glutaconyl-CoA + H2O
(R)-2-hydroxyglutaryl-CoA
Q9X5B7; Q9X5B8
-
-
-
r
(E)-oxalocrotonyl-CoA + H2O
(2R)-2-hydroxy-5-oxoadipyl-CoA
Q9X5B7; Q9X5B8
-
-
-
r
(E)-oxalocrotonyl-CoA + H2O
(2R)-2-hydroxy-5-oxoadipyl-CoA
Q9X5B7; Q9X5B8
-
-
-
r
(E,E)-muconyl-CoA + H2O
(2R,4E)-2-hydroxy-4-hexenedioyl-CoA
Q9X5B7; Q9X5B8
-
-
-
r
(E,E)-muconyl-CoA + H2O
(2R,4E)-2-hydroxy-4-hexenedioyl-CoA
Q9X5B7; Q9X5B8
-
-
-
r
(R)-2-hydroxyadipyl-CoA
(E)-2-hexenedioyl-CoA + H2O
Q9X5B7; Q9X5B8
-
-
-
r
(R)-2-hydroxyadipyl-CoA
(E)-2-hexenedioyl-CoA + H2O
Q9X5B7; Q9X5B8
-
-
-
r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
?
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
?
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
the enzyme is involved in the fermentation of L-glutamate
-
-
?
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
-
r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
?, r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
the enzyme is involved in the fermentation of L-glutamate
-
-
?
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
-
-
-
?
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
Q9X5B7; Q9X5B8
-
-
-
r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
Q9X5B8; Q9X5B7
-
-
-
r
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
Q9X5B7; Q9X5B8
-
-
-
r
(R)-2-hydroxyglutaryl-N-acetylcysteamine
(E)-glutaconyl-N-acetylcysteamine + H2O
Q9X5B7; Q9X5B8
-
-
-
r
(R)-2-hydroxyglutaryl-N-acetylcysteamine
(E)-glutaconyl-N-acetylcysteamine + H2O
Q9X5B7; Q9X5B8
-
-
-
r
additional information
?
-
in the presence of ATP one electron is transferred from flavodoxin hydroquinone via the [4Fe-4S]1+/2+ cluster of the activator protein to Mo(VI) of heterodimeric dehydratase, which is thereby reduced to Mo(V)
-
-
?
additional information
?
-
in the presence of ATP one electron is transferred from flavodoxin hydroquinone via the [4Fe-4S]1+/2+ cluster of the activator protein to Mo(VI) of heterodimeric dehydratase, which is thereby reduced to Mo(V)
-
-
?
additional information
?
-
-
no activity with 3-methylglutaconyl-CoA. The dehydratase is not specific for the CoA-moiety because (R)-2-hydroxyglutaryl-thioesters of N-acetylcysteamine and pantetheine serve as almost equal substrates
-
-
?
additional information
?
-
Q9X5B7; Q9X5B8
no activity with 3-methylglutaconyl-CoA. The dehydratase is not specific for the CoA-moiety because (R)-2-hydroxyglutaryl-thioesters of N-acetylcysteamine and pantetheine serve as almost equal substrates
-
-
?
additional information
?
-
-
no activity with 3-methylglutaconyl-CoA. The dehydratase is not specific for the CoA-moiety because (R)-2-hydroxyglutaryl-thioesters of N-acetylcysteamine and pantetheine serve as almost equal substrates
-
-
?
additional information
?
-
Q9X5B7; Q9X5B8
no activity with 3-methylglutaconyl-CoA. The dehydratase is not specific for the CoA-moiety because (R)-2-hydroxyglutaryl-thioesters of N-acetylcysteamine and pantetheine serve as almost equal substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
the enzyme is involved in the fermentation of L-glutamate
-
-
?
(R)-2-hydroxyglutaryl-CoA
(E)-glutaconyl-CoA + H2O
the enzyme is involved in the fermentation of L-glutamate
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
alternative electron donor besides flavodoxin is a two [4Fe-4S]1+/2+-cluster-containing ferredoxin, with redox potentials of 405 mV and 340mV. The flavodoxin is the dominant electron donor protein under iron-limiting conditions. The concentration of ferredoxin increases stepwise from about 0.2 micromol/g at 713 microM Fe to 1.1 micromol/g at 1745 microM Fe
-
flavodoxin
dominant electron donor protein under iron-limiting conditions
-
riboflavin 5'-phosphate
1 mol per mol of heterodimeric dehydratase
riboflavin 5'-phosphate
the actual dehydration is mediated by component D, which contains 1.0 [4Fe-4S]2+ cluster, 1.0 reduced riboflavin-5'-phosphate and about 0.1 molybdenum (VI) per heterodimer
riboflavin 5'-phosphate
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
the enzyme contains 1.0 mol of riboflavin 5'-phosphate per mol of heterodimeric enzyme
[4Fe-4S]-center
each active component contains an oxygen sensitive diamagnetic [4Fe-4S]2+ cluster. Reduction of the [4Fe-4S]2+ cluster of the activator protein with dithionite yields a paramagnetic [4Fe-4S]1+ cluster with the unusual electron spin ground state S=3/2. Under air the activator protein looses its activity within seconds due to irreversible degradation of its [4Fe-4S]2+ cluster to a [2Fe-2S]2+ cluster. The [4Fe-4S]2+ cluster of the heterodimeric dehydratase cannot be reduced to a [4Fe-4S]1+ cluster
[4Fe-4S]-center
the actual dehydration is mediated by component D, which contains 1.0 [4Fe-4S]2+ cluster, 1.0 reduced riboflavin-5'-phosphate and about 0.1 molybdenum (VI) per heterodimer
[4Fe-4S]-center
the reduced [4Fe-4S]+ cluster containing activator protein transfers one electron to the dehydratase driven by ATP hydrolysis, which activates the enzyme. With a tenfold excess of titanium(III) citrate at pH 8.0 the activator can be further reduced, yielding about 50% of a superreduced [4Fe-4S]0 cluster in the all-ferrous state. The superreduced cluster has apparent spectroscopic similarities with the corresponding [4Fe-4S]0 cluster described for the nitrogenase Fe-protein. Only one-electron transfer steps are involved in dehydratase catalysis
[4Fe-4S]-center
the [4Fe-4S](1+/2+) cluster of the activator protein is exposed to the solvent. Upon exchange of the bound ADP by ATP, the chelation rate by iron chelators is 8fold enhanced, indicating a large conformational change. Oxidized activator exhibits ATPase activity of 6 s(-1), which is completely abolished upon reduction by one electron
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S centre
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
the enzyme contains two [4Fe4S]2+ clusters. It is likely that the alpha and beta subunits are bridged by a [4Fe4S]2+ cluster. The enzyme contains 7.5 non-heme iron and 8.1 acid labile sulfur/heterodimer, symmetric cube-type structures
Fe-S cluster
Q9X5B7; Q9X5B8
7.3 mol iron per mol of heterodimeric enzyme
Molybdenum
protein contains about 0.1 molybdenum (VI) per heterodimer. The enzyme has to be activated by the extremely oxygensensitive [4Fe-4S]1+/2+-cluster-containing homodimeric component A, which generates Mo(V) by an ATP/Mg2+-induced one-electron transfer
[4Fe-4S]2+ cluster
additional information
[4Fe-4S]2+ cluster
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
7.3 mol iron per mol heterodimeric enzyme, 8.1 mol sulfur per mol heterodimeric enzyme
additional information
Q9X5B7; Q9X5B8
molybdenum or copper not detected
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Activator protein
the enzyme must be activated by an activator protein. Once activated, it can catalyse many turnovers
-
(R)-2-hydroxyglutaryl-CoA dehydratase component A
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
-
-
(R)-2-hydroxyglutaryl-CoA dehydratase component A
Q9X5B7; Q9X5B8
activator protein, UniProt ID Q9X5B6
-
activator protein HgdC
-
the enzyme is activated by ATP, MgCl2, and Ti(III)citrate by an activator protein (HgdC) that is present in the organism at very low concentrations. It is suggested that during the activation step, the electron of this cycle is fed into the enzyme by Ti(III)citrate and energized by hydrolysis of ATP. Both functions are apparently catalysed by the activator. The enzyme remains in this activated state for several turnovers
-
FMNH2
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
1 mol per mol heterodimeric enzyme
riboflavin
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
0.3 mol per mol heterodimeric enzyme
additional information
enzyme requires an activator protein HgdC for activity. Dehydratase activity is stimulated at least tenfold by cell-free extracts of Escherichia coli cells transformed with a plasmid carrying hgdC. On the chromosome the HgdC gene is located just before the catalytic subunits hgdA and hgdB
-
additional information
-
enzyme requires an activator protein HgdC for activity. Dehydratase activity is stimulated at least tenfold by cell-free extracts of Escherichia coli cells transformed with a plasmid carrying hgdC. On the chromosome the HgdC gene is located just before the catalytic subunits hgdA and hgdB
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
(E)-oxalocrotonyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.57
(E,E)-muconyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.115
(R)-2-hydroxyglutaryl-N-acetylcysteamine
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.09
S-(R)-2-hydroxyglutarylpantetheine
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.25
(E)-glutaconyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.1
(R)-2-hydroxyadipyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.052
(R)-2-hydroxyglutaryl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
2.1
butynedioyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
82
(R)-2-hydroxyglutaryl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
(E)-oxalocrotonyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
8.2
(E,E)-muconyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
560
(R)-2-hydroxyglutaryl-N-acetylcysteamine
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
800
S-(R)-2-hydroxyglutarylpantetheine
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
27
(E)-glutaconyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
440
(R)-2-hydroxyadipyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
1600
(R)-2-hydroxyglutaryl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
0.14
butynedioyl-CoA
Q9X5B7; Q9X5B8
strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
strictly anaerobic conditions, substrate (R)-2-hydroxyglutaryl-CoA, 200 mM potassium phosphate pH 7.0, 22°C
54
Q9X5B7; Q9X5B8
substrate (R)-2-hydroxyglutaryl-CoA, strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
[Clostridium] symbiosum HB 25
Q9X5B8: subunit beta (hgdB), Q9X5B7: subunit alpha (hgdA)
Q9X5B8; Q9X5B7
UniProt
brenda
P11569 i.e. subunit alpha, P11570 i.e. subunit beta
UniProt
brenda
P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein
UniProt
brenda
P11569: alpha-subunit, P11570: beta-subunit
UniProt
brenda
P11569 i.e. subunit alpha, P11570 i.e. subunit beta
UniProt
brenda
P11569 i.e. subunit alpha, P11570 i.e. subunit beta, P11568 i.e. activator protein
UniProt
brenda
Q9X5B8: subunit beta (hgdB), Q9X5B7: subunit alpha (hgdA)
Q9X5B8; Q9X5B7
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the enzyme is involved in the fermentation of L-glutamate
metabolism
-
the enzyme is involved in the fermentation of L-glutamate
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HGDA_ACIFV
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4)
477
0
53896
Swiss-Prot
-
HGDB_ACIFV
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4)
379
0
42028
Swiss-Prot
-
A0A644X0U4_9ZZZZ
46
0
5028
TrEMBL
other Location (Reliability: 1)
A0A644WCJ2_9ZZZZ
492
0
54799
TrEMBL
other Location (Reliability: 1)
A0A645HH28_9ZZZZ
66
0
7343
TrEMBL
other Location (Reliability: 2)
A0A6S6Y0G4_9FIRM
386
0
43203
TrEMBL
-
A0A644WBM4_9ZZZZ
376
0
41896
TrEMBL
other Location (Reliability: 1)
A0A645CNL3_9ZZZZ
88
0
9780
TrEMBL
other Location (Reliability: 2)
A0A645D2Q8_9ZZZZ
274
0
30630
TrEMBL
Mitochondrion (Reliability: 5)
A0A6S6XD00_9FIRM
384
0
42739
TrEMBL
-
A0A645BDS1_9ZZZZ
272
0
30461
TrEMBL
other Location (Reliability: 5)
A0A644Z6Q9_9ZZZZ
427
0
47318
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
43033
Q9X5B7; Q9X5B8
1 * 53981 (gene hgdA) + 1 * 43033 (gene hgdB), calculation from amino acid sequence
53981
Q9X5B7; Q9X5B8
1 * 53981 (gene hgdA) + 1 * 43033 (gene hgdB), calculation from amino acid sequence
54000
55000
42000
2 * 55000 (alpha), + 2 * 42000 (beta), SDS-PAGE
55000
2 * 55000 (alpha), + 2 * 42000 (beta), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
tetramer
heterodimer
Q9X5B7; Q9X5B8
1 * 53981 (gene hgdA) + 1 * 43033 (gene hgdB), calculation from amino acid sequence
heterodimer
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
1 * 54000, 1 * 42000, SDS-PAGE
heterodimer
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
1 * 54000 (alpha) + 1 * 42000 (beta), SDS-PAGE
heterodimer
-
1 * 53981 (gene hgdA) + 1 * 43033 (gene hgdB), calculation from amino acid sequence
-
tetramer
2 * 55000 (alpha), + 2 * 42000 (beta), SDS-PAGE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitive with a half-life of 2 days under aerobic conditions
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
733766
the enzyme is oxygen sensitive with a half-life of 2 days under aerobic conditions
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
733766
under anaerobic conditions at 4°C for about 1 week without loss of activity
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
733766
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, frozen with liquid nitrogen, stable
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
-80°C, liquid nitrogen, long-term storage
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
4°C anaerobic conditions, 1 week stable
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
4°C, 1 week, anaerobic conditions, stable
Q9X5B7; Q9X5B8, Q9X5B8; Q9X5B7
homodimeric activator, in the presence of 5 mM MgCl2 and 1 mM ADP or ATP, can be stabilized and stored for 4 days at 4°C without loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of genes for the production of glutaconate from 2-oxoglutarate in Escherichia coli
Q9X5B7; Q9X5B8
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Djurdjevic, I.; Zelder, O.; Buckel, W.
Production of glutaconic acid in a recombinant Escherichia coli strain
Appl. Environ. Microbiol.
77
320-322
2011
[Clostridium] symbiosum (Q9X5B7 and Q9X5B8), [Clostridium] symbiosum DSM 934 (Q9X5B7 and Q9X5B8)
brenda
Parthasarathy, A1.; Pierik, A.J.; Kahnt, J.; Zelder, O.; Buckel, W.
Substrate specificity of 2-hydroxyglutaryl-CoA dehydratase from Clostridium symbiosum: toward a bio-based production of adipic acid
Biochemistry
50
3540-3550
2011
[Clostridium] symbiosum, [Clostridium] symbiosum (Q9X5B7 and Q9X5B8), [Clostridium] symbiosum DSM 934, [Clostridium] symbiosum DSM 934 (Q9X5B7 and Q9X5B8)
brenda
Buckel, W.
The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate
Eur. J. Biochem.
106
439-447
1980
Acidaminococcus fermentans, Acidaminococcus fermentans (P11569 and P11570), Acidaminococcus fermentans DSM 20731 (P11569 and P11570), [Clostridium] symbiosum
brenda
Schweiger, G.; Dutscho R.; Buckel, W.
Purification of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. An iron-sulfur protein
Eur. J. Biochem.
169
441-448
1987
Acidaminococcus fermentans (P11569 and P11570), Acidaminococcus fermentans, Acidaminococcus fermentans DSM 20731 (P11569 and P11570)
brenda
Hans, M.; Sievers, J.; Mller, U.; Bill, E.; Vorholt, J.A.; Linder, D.; Buckel, W.
2-Hydroxyglutaryl-CoA dehydratase from Clostridium symbiosum
Eur. J. Biochem.
265
404-414
1999
[Clostridium] symbiosum (Q9X5B7 and Q9X5B8), [Clostridium] symbiosum (Q9X5B8 AND Q9X5B7), [Clostridium] symbiosum HB 25 (Q9X5B8 AND Q9X5B7), [Clostridium] symbiosum DSM 934 (Q9X5B7 and Q9X5B8)
brenda
Hans, M.; Buckel, W.; Bill, E.
The iron-sulfur clusters in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemical and spectroscopic investigations
Eur. J. Biochem.
267
7082-7093
2000
Acidaminococcus fermentans (P11569 and P11570 and P11568), Acidaminococcus fermentans DSM 20731 (P11569 and P11570 and P11568)
brenda
Thamer, W.; Cirpus, I.; Hans, M.; Pierik, A.J.; Selmer, T.; Bill, E.; Linder, D.; Buckel, W.
A two [4Fe-4S]-cluster-containing ferredoxin as an alternative electron donor for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
Arch. Microbiol.
179
197-204
2003
Acidaminococcus fermentans (P11569 and P11570), Acidaminococcus fermentans DSM 20731 (P11569 and P11570)
brenda
Hans, M.; Bill, E.; Cirpus, I.; Pierik, A.J.; Hetzel, M.; Alber, D.; Buckel, W.
Adenosine triphosphate-induced electron transfer in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
Biochemistry
41
5873-5882
2002
Acidaminococcus fermentans (P11569 and P11570), Acidaminococcus fermentans DSM 20731 (P11569 and P11570)
brenda
Muller, U.; Buckel, W.
Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
Eur. J. Biochem.
230
698-704
1995
Acidaminococcus fermentans, Acidaminococcus fermentans ATCC 25085
brenda
Bendrat, K.; Mueller, U.; Klees, A.G.; Buckel, W.
Identification of the gene encoding the activator of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans by gene expression in Escherichia coli
FEBS Lett.
329
329-331
1993
Acidaminococcus fermentans (P11569 and P11570 and P11568), Acidaminococcus fermentans, Acidaminococcus fermentans DSM 20731 (P11569 and P11570 and P11568)
brenda
Hans, M.; Buckel, W.; Bill, E.
Spectroscopic evidence for an all-ferrous [4Fe-4S]0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
J. Biol. Inorg. Chem.
13
563-574
2008
Acidaminococcus fermentans (P11569 and P11570 and P11568), Acidaminococcus fermentans DSM 20731 (P11569 and P11570 and P11568)
brenda
Locher, K.P.; Hans, M.; Yeh, A.P.; Schmid, B.; Buckel, W.; Rees, D.C.
Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A
J. Mol. Biol.
307
297-308
2001
Acidaminococcus fermentans
brenda
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