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IUBMB Comments The enzyme, characterized from the bacterium Geobacter metallireducens , participates in an anaerobic degradation pathway for cyclohexane-1-carboxylate. In vitro , the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA.
Synonyms
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CHC-activating CoA transferase
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Gmet_3304
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locus name
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succinyl-CoA + cyclohexane-1-carboxylate = succinate + cyclohexane-1-carbonyl-CoA
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succinyl-CoA---cyclohexane-1-carboxylate CoA-transferase
The enzyme, characterized from the bacterium Geobacter metallireducens, participates in an anaerobic degradation pathway for cyclohexane-1-carboxylate. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA.
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acetoacetyl-CoA + cyclohexane-1-carboxylate
acetoacetate + cyclohexane-1-carbonyl-CoA
Substrates: 5% activity compared to succinyl-CoA
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acetyl-CoA + cyclohexane-1-carboxylate
acetate + cyclohexane-1-carbonyl-CoA
Substrates: 31% activity compared to succinyl-CoA
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butyryl-CoA + benzoate
butyrate + benzoyl-CoA
Substrates: 42% activity compared to cyclohexane-1-carbonyl-CoA
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butyryl-CoA + cyclohex-1-ene-1-carboxylate
butyrate + cyclohex-1-ene-1-carboxyl-CoA
Substrates: 140% activity compared to cyclohexane-1-carbonyl-CoA
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butyryl-CoA + cyclohexane-1-carboxylate
butyrate + cyclohexane-1-carbonyl-CoA
Substrates: 135% activity compared to succinyl-CoA
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CH1ene-CoA + cyclohexane-1-carboxylate
CH1ene + cyclohexane-1-carbonyl-CoA
Substrates: 22% activity compared to succinyl-CoA
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crotonyl-CoA + cyclohexane-1-carboxylate
crotonate + cyclohexane-1-carbonyl-CoA
Substrates: 50% activity compared to succinyl-CoA
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glutaryl-CoA + cyclohexane-1-carboxylate
glutarate + cyclohexane-1-carbonyl-CoA
Substrates: 28% activity compared to succinyl-CoA
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propionyl-CoA + cyclohexane-1-carboxylate
propionate + cyclohexane-1-carbonyl-CoA
Substrates: 9% activity compared to succinyl-CoA
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succinyl-CoA + benzoate
succinate + benzoyl-CoA
Substrates: 15% activity compared to cyclohexane-1-carbonyl-CoA
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succinyl-CoA + cyclohex-1-ene-1-carboxylate
succinate + cyclohex-1-ene-1-carboxyl-CoA
Substrates: 40% activity compared to cyclohexane-1-carbonyl-CoA
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succinyl-CoA + cyclohexane-1-carboxylate
succinate + cyclohexane-1-carbonyl-CoA
Substrates: 100% activity
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0.5
acetyl-CoA
Km above 0.5 mM, with cyclohexane-1-carboxylate as cosubstrate, at pH 6.8 and 30°C
0.014 - 0.125
butyryl-CoA
0.2
cyclohex-1-ene-1-carboxyl-CoA
Km above 0.2 mM, with cyclohexane-1-carboxylate as cosubstrate, at pH 6.8 and 30°C
0.056 - 0.416
succinyl-CoA
0.014
butyryl-CoA
with cyclohexane-1-carboxylate as cosubstrate, at pH 6.8 and 30°C
0.052
butyryl-CoA
with cyclohex-1-ene-1-carboxyate as cosubstrate, at pH 6.8 and 30°C
0.125
butyryl-CoA
with benzoate as cosubstrate, at pH 6.8 and 30°C
0.056
succinyl-CoA
with cyclohexane-1-carboxylate as cosubstrate, at pH 6.8 and 30°C
0.158
succinyl-CoA
with cyclohex-1-ene-1-carboxylate as cosubstrate, at pH 6.8 and 30°C
0.416
succinyl-CoA
with benzoate as cosubstrate, at pH 6.8 and 30°C
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UniProt
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Highest Expressing Human Cell Lines
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SCHCT_GEOMG
Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)
437
0
47911
Swiss-Prot
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homodimer
2 * 47800, calculated from amino acid sequence
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Ni-chelating affinity chromatography
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expressed in Escherichia coli BL21 Star cells
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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 (Q39QF7)
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