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Information on EC 1.3.8.10 - cyclohex-1-ene-1-carbonyl-CoA dehydrogenase for references in articles please use BRENDA:EC1.3.8.10
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IUBMB 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.
The enzyme appears in viruses and cellular organisms
Synonyms
ch1coa dehydrogenase, cyclohexanecarboxyl-coa dehydrogenase,
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cyclohex-1-ene-1-carboxyl-CoA dehydrogenase
cyclohexanecarboxyl-CoA dehydrogenase
Ch1CoA dehydrogenase
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Ch1CoA dehydrogenase
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cyclohex-1-ene-1-carboxyl-CoA dehydrogenase
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cyclohex-1-ene-1-carboxyl-CoA dehydrogenase
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cyclohexanecarboxyl-CoA dehydrogenase
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cyclohexanecarboxyl-CoA dehydrogenase
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Gmet_3306
gene name
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cyclohex-1-ene-1-carbonyl-CoA + electron-transfer flavoprotein = cyclohex-1,5-diene-1-carbonyl-CoA + reduced electron-transfer flavoprotein
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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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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
additional information
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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 + 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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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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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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cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate
cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate
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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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ir
additional information
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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 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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0.019 - 0.085
cyclohex-1,5-diene-1-carbonyl-CoA
0.005 - 0.031
cyclohex-1-ene-1-carbonyl-CoA
0.019
cyclohex-1,5-diene-1-carbonyl-CoA
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at pH 7.0 and 30°C
0.085
cyclohex-1,5-diene-1-carbonyl-CoA
pH 6.8, 30°C
0.005
cyclohex-1-ene-1-carbonyl-CoA
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Km less than 0.005 mM, at pH 7.0 and 30°C
0.031
cyclohex-1-ene-1-carbonyl-CoA
pH 6.8, 30°C
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1
substrate cyclohex-1,5-diene-1-carbonyl-CoA, pH 6.8, 30°C
2.1
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using (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA as substrate, at pH 7.0 and 30°C
2.3
substrate cyclohex-1-ene-1-carbonyl-CoA, pH 6.8, 30°C
9.5
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using cyclohex-1-ene-1-carbonyl-CoA as substrate, at pH 7.0 and 30°C
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UniProt
brenda
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UniProt
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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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CH1CO_SYNAS
Syntrophus aciditrophicus (strain SB)
414
0
45178
Swiss-Prot
A0A143QLD1_9NOCA
385
0
40874
TrEMBL
A0A143QBZ3_9NOCA
390
0
40911
TrEMBL
A0A0B8NA42_9NOCA
385
0
41765
TrEMBL
A0A3P5BND0_PSEAI
386
0
42854
TrEMBL
A0A383RZP4_9PSED
387
0
42903
TrEMBL
A0A2J7V4X6_9BURK
298
0
31195
TrEMBL
A0A2S6REE8_9PROT
385
0
43358
TrEMBL
A0A2J7W7E1_9BURK
371
0
39304
TrEMBL
A0A2R8BR89_9RHOB
373
0
40308
TrEMBL
A0A3P4MQY6_ACIBA
597
0
66340
TrEMBL
Q39QF5_GEOMG
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
380
0
40990
TrEMBL
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x * 40900,SDS-PAGE, recombinant protein with His-tag
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x * 40900,SDS-PAGE, recombinant protein with His-tag
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homotetramer
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4 * 40000-45000, SDS-PAGE
homotetramer
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4 * 40000-45000, SDS-PAGE
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Ni-chelating affinity column chromatography
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expressed in Escherichia coli BL 21 Star(DE3) OneShot cells
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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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1.3.8.10 cyclohex-1-ene-1-carbonyl-CoA dehydrogenase
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