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Information on EC 4.2.1.100 - cyclohexa-1,5-dienecarbonyl-CoA hydratase
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EC Tree
4.2.1.100 cyclohexa-1,5-dienecarbonyl-CoA hydrataseIUBMB Comments
Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.8.6 [glutaryl-CoA dehydrogenase (ETF)], EC 1.3.7.8 (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA dehydratase).
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Word Map
- 4.2.1.100
- benzoyl-coa
-
thauera
- aromatica
-
denitrifying
-
rhodopseudomonas
- nad+
- palustris
- crotonyl-coa
-
anoxic
-
benzoyl-coenzyme
-
atp-driven
- ferredoxin
- benzoate
- benzene
-
two-electron
- co2
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
1,5-dienoyl-CoA hydratase, cyclohexa-1,5-diene-1-carbonyl-CoA hydratase, Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, DCH, dienoyl-CoA hydratase, EC 4.2.1.102, Ferp_1031, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,5-dienoyl-CoA hydratase
cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
-
-
-
-
Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase
-
-
-
-
DCH
dienoyl-CoA hydratase
EC 4.2.1.102
-
-
formerly
-
Ferp_1031
dienoyl-CoA hydratase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-hydroxycyclohex-1-ene-1-carbonyl-CoA = cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
6-hydroxycyclohex-1-enecarbonyl-CoA hydro-lyase (cyclohexa-1,5-dienecarbonyl-CoA-forming)
Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.8.6 [glutaryl-CoA dehydrogenase (ETF)], EC 1.3.7.8 (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA dehydratase).
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CAS REGISTRY NUMBER
COMMENTARY
214355-79-0
-
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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
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
6-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
cyclohex-1-ene-1-carbonyl-CoA + H2O
2-hydroxycyclohexane-1-carbonyl-CoA
-
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
cyclohexa-1,5-dienecarbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
trans-1,4 water addition, stereochemistry of 6-hydroxycyclohex-1-ene-1-carboxyl-CoA by NMR analysis
-
-
?
cyclohexa-2,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-2-ene-1-carbonyl-CoA
-
only when dithionite is used as an artificial electron donor
-
?
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
6-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
6-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
-
-
-
r
6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
-
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
-
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
-
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
involved in the benzoyl-CoA pathway
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
involved in the benzoyl-CoA pathway
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
involved in the benzoyl-CoA pathway
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
?
additional information
?
-
the 1,5-dienoyl-CoA hydratase hydrated the fluorocyclohexa-1,5-dienoyl-CoA isomers to a mixture of the stable 2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA and the unstable alpha-fluorohydrin 6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA. The latter spontaneously decomposed to HF and 6-oxo-cyclohexa-1-ene-1-carbonyl-CoA
-
-
?
additional information
?
-
the 1,5-dienoyl-CoA hydratase hydrated the fluorocyclohexa-1,5-dienoyl-CoA isomers to a mixture of the stable 2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA and the unstable alpha-fluorohydrin 6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA. The latter spontaneously decomposed to HF and 6-oxo-cyclohexa-1-ene-1-carbonyl-CoA
-
-
?
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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
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
6-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
6-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
6-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
-
-
-
r
6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
-
-
-
r
6-hydroxycyclohexa-1-ene-1-carbonyl-CoA
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
?
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
involved in the benzoyl-CoA pathway
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
involved in the benzoyl-CoA pathway
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
involved in the benzoyl-CoA pathway
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
6-hydroxycyclohex-1-enecarbonyl-CoA
-
-
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
107
purified recombinant enzyme with substrate cyclohexa-1,5-diene-1-carbonyl-CoA, pH and temperature not specified in the publication
110
110
-
reversible reaction with 6-hydroxycyclohex-1-ene-1-carboxyl-CoA as substrat
110
purified recombinant enzyme with substrate 6-hydroxycyclohex-1-ene-1-carbonyl-CoA, pH and temperature not specified in the publication
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
2-fluoro-benzoate- and benzoate-grown cells
brenda
additional information
-
2-fluoro-benzoate- and benzoate-grown cells
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme is involved in benzoyl-coenzyme A degradation
metabolism
the enzyme is involved in the biodegradation of the environmentally hazardous fluoroaromatics. The 1,5-dienoyl-CoA hydratase (DCH) hydrates the fluoro-1,5-dienoyl-CoA isomers to a mixture of the stable 2-fluoro-6-hydroxy-1-enoyl-CoA and the unstable alpha-fluorohydrin 6-fluoro-6-hydroxy-1-enoyl-CoA. The latter spontaneously decomposes to HF and 6-oxo-cyclohex-1-enoyl-CoA, a common intermediate of the benzoyl-coenzyme A (BzCoA) degradation pathway. 6-Oxo-cyclohex-1-enoyl-CoA hydrolase/hydratase catalyzes the defluorination of 2-fluoro-6-hydroxycyclohex-1-enoyl-CoA to 2-oxo-6-hydroxycyclohex-1-enoyl-CoA and HF again via water addition to an fluorocyclohex-1-enoyl-CoA functionality. Formation of both 3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA and 5-fluorocyclohexa-1,5-diene-1-carbonyl-CoA suggesting a low regioselectivity of benzoyl-coenzyme A (BzCoA) reductase (BCR) for fluorinated BzCoA analogues. Enzyme DCH and bifunctional 6-oxo-cyclohex-1-enoyl-CoA hydrolase (OAH) both initiate defluorination of the 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA intermediate by 1,4-hydration. Enzyme OAH is competent to hydrate both fluorinated cyclohexa-1,5-diene-carbonyl-CoA isomers and exhibits a similar reactivity as enzyme DCH, and OAH alone is capable of defluorinating both fluorinated cyclohexa-1,5-diene-carbonyl-CoA isomers formed by BCR. Detailed pathway overview
metabolism
-
the enzyme is involved in benzoyl-coenzyme A degradation
-
metabolism
-
the enzyme is involved in the biodegradation of the environmentally hazardous fluoroaromatics. The 1,5-dienoyl-CoA hydratase (DCH) hydrates the fluoro-1,5-dienoyl-CoA isomers to a mixture of the stable 2-fluoro-6-hydroxy-1-enoyl-CoA and the unstable alpha-fluorohydrin 6-fluoro-6-hydroxy-1-enoyl-CoA. The latter spontaneously decomposes to HF and 6-oxo-cyclohex-1-enoyl-CoA, a common intermediate of the benzoyl-coenzyme A (BzCoA) degradation pathway. 6-Oxo-cyclohex-1-enoyl-CoA hydrolase/hydratase catalyzes the defluorination of 2-fluoro-6-hydroxycyclohex-1-enoyl-CoA to 2-oxo-6-hydroxycyclohex-1-enoyl-CoA and HF again via water addition to an fluorocyclohex-1-enoyl-CoA functionality. Formation of both 3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA and 5-fluorocyclohexa-1,5-diene-1-carbonyl-CoA suggesting a low regioselectivity of benzoyl-coenzyme A (BzCoA) reductase (BCR) for fluorinated BzCoA analogues. Enzyme DCH and bifunctional 6-oxo-cyclohex-1-enoyl-CoA hydrolase (OAH) both initiate defluorination of the 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA intermediate by 1,4-hydration. Enzyme OAH is competent to hydrate both fluorinated cyclohexa-1,5-diene-carbonyl-CoA isomers and exhibits a similar reactivity as enzyme DCH, and OAH alone is capable of defluorinating both fluorinated cyclohexa-1,5-diene-carbonyl-CoA isomers formed by BCR. Detailed pathway overview
-
physiological function
the enzyme is involved in the biodegradation of the environmentally hazardous fluoroaromatics. The 1,5-dienoyl-CoA hydratase (DCH) hydrates the fluorocyclohexa-1,5-diene-1-carbonyl-CoA isomers to a mixture of the stable 2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA and the unstable alpha-fluorohydrin 6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA. The latter spontaneously decomposes to HF and 6-oxo-cyclohexa-1-ene-1-carbonyl-CoA, a common intermediate of the benzoyl-coenzyme A (BzCoA) degradation pathway. 6-Oxo-cyclohexa-1-ene-1-carbonyl-CoA hydrolase/hydratase catalyzes the defluorination of 2-fluoro-6-hydroxy-1-enoyl-CoA to 2-oxo-6-hydroxy-1-enoyl-CoA and HF again via water addition to an fluoro-enoyl-CoA functionality
physiological function
-
the enzyme is involved in the biodegradation of the environmentally hazardous fluoroaromatics. The 1,5-dienoyl-CoA hydratase (DCH) hydrates the fluorocyclohexa-1,5-diene-1-carbonyl-CoA isomers to a mixture of the stable 2-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA and the unstable alpha-fluorohydrin 6-fluoro-6-hydroxycyclohexa-1-ene-1-carbonyl-CoA. The latter spontaneously decomposes to HF and 6-oxo-cyclohexa-1-ene-1-carbonyl-CoA, a common intermediate of the benzoyl-coenzyme A (BzCoA) degradation pathway. 6-Oxo-cyclohexa-1-ene-1-carbonyl-CoA hydrolase/hydratase catalyzes the defluorination of 2-fluoro-6-hydroxy-1-enoyl-CoA to 2-oxo-6-hydroxy-1-enoyl-CoA and HF again via water addition to an fluoro-enoyl-CoA functionality
-
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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). I4C3Q1_DESTA
Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1)
259
0
28642
TrEMBL
-
A0A1V5BIF6_9FIRM
254
0
27706
TrEMBL
-
A0A7U6Y591_9PROT
256
0
27374
TrEMBL
-
A0A557S0M7_9GAMM
256
0
27655
TrEMBL
-
A0A3B0RCK5_9ZZZZ
255
0
27381
TrEMBL
other Location (Reliability: 5)
A0A0B6X3L7_9BACT
258
0
28704
TrEMBL
-
S0G4H5_9DELT
256
0
28122
TrEMBL
-
Q1IS86_KORVE
Koribacter versatilis (strain Ellin345)
265
0
29003
TrEMBL
-
A0A1V5BXR7_9FIRM
254
0
27498
TrEMBL
-
A0A1Q9NP01_9ARCH
255
0
28405
TrEMBL
-
A0A1V5CJS6_9DELT
226
0
24922
TrEMBL
-
A0A1V6HRJ6_9BACT
263
0
27535
TrEMBL
-
A0A1J5R2S3_9ZZZZ
257
0
27994
TrEMBL
other Location (Reliability: 2)
A0A1V5FAM9_9PROT
258
0
27696
TrEMBL
-
D3RXI0_FERPA
Ferroglobus placidus (strain DSM 10642 / AEDII12DO)
252
0
28129
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29900
-
4 * 30000, SDS-PAGE of purified His-tag labeled protein, 4 * 29900, calculated mass of the His-tag labeled protein, native mass by gel filtration
30000
30400
30000
-
2 * 30000, SDS-PAGE of purified His-tag labeled protein, 2 * 30400, calculated mass of the His-tag labeled protein, native mass by Ferguson blot analysis
30000
-
3 * 30000, SDS-PAGE of purified His-tag labeled protein, 3 * 30400, calculated mass of the His-tag labeled protein, native mass by gel filtration
30000
-
4 * 30000, SDS-PAGE of purified His-tag labeled protein, 4 * 29900, calculated mass of the His-tag labeled protein, native mass by gel filtration
30400
-
2 * 30000, SDS-PAGE of purified His-tag labeled protein, 2 * 30400, calculated mass of the His-tag labeled protein, native mass by Ferguson blot analysis
30400
-
3 * 30000, SDS-PAGE of purified His-tag labeled protein, 3 * 30400, calculated mass of the His-tag labeled protein, native mass by gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
-
4 * 30000, SDS-PAGE of purified His-tag labeled protein, 4 * 29900, calculated mass of the His-tag labeled protein, native mass by gel filtration
trimer
-
3 * 30000, SDS-PAGE of purified His-tag labeled protein, 3 * 30400, calculated mass of the His-tag labeled protein, native mass by gel filtration
dimer
-
2 * 30000, SDS-PAGE of purified His-tag labeled protein, 2 * 30400, calculated mass of the His-tag labeled protein, native mass by Ferguson blot analysis
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain MC4100 by nickel affinity chromatography and desalting gel filtration
recombinant protein using His-tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)pLysS cells
gene dch, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain MC4100
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)pLysS cells
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)pLysS cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harwood, C.S.; Gibson, J.
Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes?
J. Bacteriol.
179
301-309
1997
Aromatoleum evansii, Thauera aromatica
brenda
Koch, J.; Eisenreich, W.; Bacher, A.; Fuchs, G.
Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism
Eur. J. Biochem.
211
649-661
1993
Aromatoleum evansii
brenda
Boll, M.; Laempe, D.; Eisenreich, W.; Bachers, A.; Mittelberger, T.; Heinze, J.; Fuchs, G.
Nonaromatic products from anoxic conversion of benzoyl-CoA with benzoyl-CoA reductase and cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
J. Biol. Chem.
275
21889-21895
2000
Thauera aromatica
brenda
Lampe, D.; Eisenreich, W.; Bacher, A.; Fuchs, G.
Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, an enzyme involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica
Eur. J. Biochem.
255
618-627
1998
Thauera aromatica
brenda
Peters, F.; Shinoda, Y.; McInerney, M.J.; Boll, M.
Cyclohexa-1,5-diene-1-carbonyl-coenzyme A (CoA) hydratases of Geobacter metallireducens and Syntrophus aciditrophicus: Evidence for a common benzoyl-CoA degradation pathway in facultative and strict anaerobes
J. Bacteriol.
189
1055-1060
2007
Desulfococcus multivorans, Geobacter metallireducens, Syntrophus aciditrophicus
brenda
Thiele, B.; Rieder, O.; Golding, B.T.; Mueller, M.; Boll, M.
Mechanism of enzymatic Birch reduction: stereochemical course and exchange reactions of benzoyl-CoA reductase
J. Am. Chem. Soc.
130
14050-14051
2008
Thauera aromatica (o87873)
brenda
Schmid, G.; Rene, S.B.; Boll, M.
Enzymes of the benzoyl-coenzyme A degradation pathway in the hyperthermophilic archaeon Ferroglobus placidus
Environ. Microbiol.
17
3289-3300
2015
Ferroglobus placidus (D3RXI0), Ferroglobus placidus, Ferroglobus placidus DSM 10642 (D3RXI0)
brenda
Tiedt, O.; Mergelsberg, M.; Eisenreich, W.; Boll, M.
Promiscuous defluorinating enoyl-CoA hydratases/hydrolases allow for complete anaerobic degradation of 2-fluorobenzoate
Front. Microbiol.
8
2579
2017
Thauera aromatica (o87873), Thauera aromatica K172 (o87873)
brenda
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