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Information on EC 1.3.8.10 - cyclohex-1-ene-1-carbonyl-CoA dehydrogenase
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1.3.8.10 cyclohex-1-ene-1-carbonyl-CoA dehydrogenaseIUBMB Comments
Contains FAD. The enzyme, characterized from the strict anaerobic bacterium Syntrophus aciditrophicus, is involved in production of cyclohexane-1-carboxylate, a byproduct produced by that organism during fermentation of benzoate and crotonate to acetate.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
Ch1CoA dehydrogenase, cyclohex-1-ene-1-carboxyl-CoA dehydrogenase, cyclohexanecarboxyl-CoA dehydrogenase, Gmet_3306, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ch1CoA dehydrogenase
cyclohex-1-ene-1-carboxyl-CoA dehydrogenase
cyclohexanecarboxyl-CoA dehydrogenase
Gmet_3306
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclohex-1-ene-1-carbonyl-CoA + electron-transfer flavoprotein = cyclohex-1,5-diene-1-carbonyl-CoA + reduced electron-transfer flavoprotein
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
cyclohex-1-ene-1-carbonyl-CoA:electron transfer flavoprotein oxidoreductase
Contains FAD. The enzyme, characterized from the strict anaerobic bacterium Syntrophus aciditrophicus, is involved in production of cyclohexane-1-carboxylate, a byproduct produced by that organism during fermentation of benzoate and crotonate to acetate.
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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
cyclohex-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate
benzoyl-CoA + ferrocenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + Ti(III) citrate
cyclohex-1-ene-1-carbonyl-CoA + oxidized Ti(III) citrate
cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate
cyclohexa-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate
benzoyl-CoA + ferrocenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate
benzoyl-CoA + ferrocenium hexafluorophosphate
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-
-
?
cyclohex-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate
benzoyl-CoA + ferrocenium hexafluorophosphate
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-
-
?
cyclohex-1,5-diene-1-carbonyl-CoA + Ti(III) citrate
cyclohex-1-ene-1-carbonyl-CoA + oxidized Ti(III) citrate
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Ti(III) citrate (5mM) in the presence of methyl viologen (1 mM) serves as the electron donor
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-
r
cyclohex-1,5-diene-1-carbonyl-CoA + Ti(III) citrate
cyclohex-1-ene-1-carbonyl-CoA + oxidized Ti(III) citrate
-
Ti(III) citrate (5mM) in the presence of methyl viologen (1 mM) serves as the electron donor
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-
r
cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate
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-
-
?
cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate
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-
-
?
cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate
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-
-
-
r
cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate
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-
-
-
r
cyclohexa-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate
benzoyl-CoA + ferrocenium hexafluorophosphate
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-
-
-
ir
cyclohexa-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate
benzoyl-CoA + ferrocenium hexafluorophosphate
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-
-
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ir
additional information
?
-
no substrates: cyclohexanoyl-CoA, cyclohex-2-ene-1-carboxyl-CoA, cyclohex-3-ene-1-carboxyl-CoA, butanoyl-CoA, nor crotonyl-CoA
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-
?
additional information
?
-
no substrates: cyclohexanoyl-CoA, cyclohex-2-ene-1-carboxyl-CoA, cyclohex-3-ene-1-carboxyl-CoA, butanoyl-CoA, nor crotonyl-CoA
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-
?
additional information
?
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-
no activity with ChCoA, 6-hydroxycyclohex-1-en-1-carboxyl-CoA, butyryl-CoA, glutaryl-CoA, succinyl-CoA, or cyclohexane carboxylate
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?
additional information
?
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no activity with ChCoA, 6-hydroxycyclohex-1-en-1-carboxyl-CoA, butyryl-CoA, glutaryl-CoA, succinyl-CoA, or cyclohexane carboxylate
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
cyclohex-1-ene-1-carbonyl-CoA
-
Km less than 0.005 mM, at pH 7.0 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1
substrate cyclohex-1,5-diene-1-carbonyl-CoA, pH 6.8, 30°C
2.1
-
using (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA as substrate, at pH 7.0 and 30°C
9.5
-
using cyclohex-1-ene-1-carbonyl-CoA as substrate, at pH 7.0 and 30°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Geobacter metallireducens grows exponentially with cyclohexane carboxylic acid as the sole carbon source and nitrate as a terminal electron acceptor. Cyclohexane carboxylic acid degradation involves its activation by a succinyl-CoA-dependent CoA transferase followed by the oxidation to cyclohexadienoyl-CoA by cyclohexanoyl-CoA- and cyclohex-1-ene-1-carboxyl-CoA dehydrogenase activities
physiological function
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Geobacter metallireducens grows exponentially with cyclohexane carboxylic acid as the sole carbon source and nitrate as a terminal electron acceptor. Cyclohexane carboxylic acid degradation involves its activation by a succinyl-CoA-dependent CoA transferase followed by the oxidation to cyclohexadienoyl-CoA by cyclohexanoyl-CoA- and cyclohex-1-ene-1-carboxyl-CoA dehydrogenase activities
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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). CH1CO_SYNAS
Syntrophus aciditrophicus (strain SB)
414
0
45178
Swiss-Prot
-
A0A2S6QHV8_9PROT
393
0
43661
TrEMBL
-
A0A6L5C3G6_9PSED
387
0
42746
TrEMBL
-
A0A2S6UMF9_9PROT
393
0
43643
TrEMBL
-
A0A2S6REE8_9PROT
385
0
43358
TrEMBL
-
A0A6J5GMS1_9BURK
386
0
42978
TrEMBL
-
Q39QF5_GEOMG
Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)
380
0
40990
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kung, J.; Seifert, J.; von Bergen, M.; Bolla, M.
Cyclohexanecarboxyl-coenzyme a (CoA) and cyclohex-1-ene-1-carboxyl-CoA dehydrogenases, two enzymes involved in the fermentation of benzoate and crotonate in Syntrophus aciditrophicus
J. Bacteriol.
195
3193-3200
2013
Syntrophus aciditrophicus, Syntrophus aciditrophicus SB
brenda
Kung, J.W.; Meier, A.K.; Mergelsberg, M.; Boll, M.
Enzymes involved in a novel anaerobic cyclohexane carboxylic acid degradation pathway
J. Bacteriol.
196
3667-3674
2014
Geobacter metallireducens (Q39QF5), Geobacter metallireducens DSM 7210 (Q39QF5)
brenda
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