Information on EC 2.8.3.8 - acetate CoA-transferase
New: Word Map on EC 2.8.3.8
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
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coenzyme A transfer
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4-aminobutanoate degradation V
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acetyl-CoA fermentation to butanoate II
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Aminobenzoate degradation
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butanoate fermentation
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gallate degradation III (anaerobic)
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glutamate and glutamine metabolism
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L-glutamate degradation V (via hydroxyglutarate)
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Microbial metabolism in diverse environments
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Propanoate metabolism
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succinate fermentation to butanoate
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acyl-CoA:acetate CoA-transferase
Acts on butanoyl-CoA and pentanoyl-CoA.
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acetate coenzyme A-transferase
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acetate:succinate CoA-transferase
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butyryl CoA:acetate CoA transferase
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butyryl coenzyme A transferase
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butyryl-CoA:acetate CoA-transferase
butyryl-coenzyme A CoA transferase
coenzyme A-transferase, acetate
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succinyl-CoA:acetate CoA transferase
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succinyl-CoA:acetate CoA-transferase
succinyl-coenzyme A:acetate CoA-transferase
AarC
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
DSM 17629
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-CoA:acetate CoA-transferase
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butyryl-coenzyme A CoA transferase
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butyryl-coenzyme A CoA transferase
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butyryl-coenzyme A CoA transferase
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butyryl-coenzyme A CoA transferase
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SCACT
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succinyl-CoA:acetate CoA-transferase
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succinyl-CoA:acetate CoA-transferase
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succinyl-coenzyme A:acetate CoA-transferase
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succinyl-coenzyme A:acetate CoA-transferase
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UniProt
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DSM 17629
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UniProt
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UniProt
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UniProt
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UniProt
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UniProt
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Coprococcus sp.
strain L2-50, exponential and stationary phase
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Coprococcus sp. L2-50
strain L2-50, exponential and stationary phase
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UniProt
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UniProt
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UniProt
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UniProt
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Uniprot
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UniProt
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UniProt
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Roseburia sp.
strain A2-181, A2-183, exponential and stationary phase
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Roseburia sp. A2-181
strain A2-181, A2-183, exponential and stationary phase
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Uniprot
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UniProt
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Uniprot
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K12, constitutive mutant strain V10 and strain D5H3G7
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Uniprot
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UniProt
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Uniprot
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UniProt
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formerly Fusobacterium, strain A2-165, exponential and stationary phase
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UniProt
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strain L1-82, L1-952, L1-8151, exponential and stationary phase
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UniProt
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strain L1-82, L1-952, L1-8151, exponential and stationary phase
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malfunction
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the acetate:succinate CoA-transferase null mutant is about 1000times more sensitive to oligomycin, a specific inhibitor of the mitochondrial F0/F1-ATP synthase, than wild type cells
metabolism
succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle
metabolism
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the enzyme is involved in ATP production in the mitochondrion
metabolism
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succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle
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physiological function
the enzyme is an acetic acid resistance factor that is required for acetate resistance
physiological function
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the enzyme is an acetic acid resistance factor that is required for acetate resistance
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acetate + succinyl-CoA
succinate + acetyl-CoA
butanoyl-CoA + acetate
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provides ability to grow on various fatty acids
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
pentanoyl-CoA + acetate
pentanoate + acetyl-CoA
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succinate + acetyl-CoA
acetate + succinyl-CoA
valeryl-CoA + acetate
valerate + acetyl-CoA
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r
additional information
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acetate + succinyl-CoA
succinate + acetyl-CoA
5.1% activity compared to succinate
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acetate + succinyl-CoA
succinate + acetyl-CoA
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5.1% activity compared to succinate
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
Coprococcus sp.
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
Coprococcus sp. L2-50
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
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best substrate
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r
butanoyl-CoA + acetate
butanoate + acetyl-CoA
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
Roseburia sp.
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butanoyl-CoA + acetate
butanoate + acetyl-CoA
Roseburia sp. A2-181
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succinate + acetyl-CoA
acetate + succinyl-CoA
100% activity
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succinate + acetyl-CoA
acetate + succinyl-CoA
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100% activity
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succinate + acetyl-CoA
acetate + succinyl-CoA
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additional information
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less than 1% activity with acetoacetate, propionate, D-malate, fumarate, L-malate, formate, oxaloacetate, DL-methylsuccinate, and glutarate. No activity is detected with dethiaacetyl-CoA, glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, alpha-ketoglutarate, citrate, or DL-isocitrate
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additional information
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less than 1% activity with acetoacetate, propionate, D-malate, fumarate, L-malate, formate, oxaloacetate, DL-methylsuccinate, and glutarate. No activity is detected with dethiaacetyl-CoA, glycolate, glyoxylate, oxalate, trifluoroacetate, DL-lactate, L-lactate, malonate, pyruvate, maleate, butyrate, D-tartrate, L-tartrate, alpha-ketoglutarate, citrate, or DL-isocitrate
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butanoyl-CoA + acetate
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provides ability to grow on various fatty acids
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Mg2+
contains 3 Mg2+ ions, none of them located near the putative active site, functional relevance is not clear
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110
acetate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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290
acetate
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.029
acetate
Acetobacter aceti
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.16
acetate
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.6
acetate
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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3
acetate
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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2600
acetate
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.7
acetyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C; mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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2.3
acetyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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3.4
acetyl-CoA
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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52
acetyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.03
succinate
Acetobacter aceti
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.3
succinate
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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2.7
succinate
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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73
succinate
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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79
succinate
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.074
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
224
0.13
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
224
0.39
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
224
9
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C; wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
224
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1600
acetate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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0.1 - 1
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in crude cell extract
1.32
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in crude cell extract, stationary growth phase, strain L1-952
2.05
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in crude cell extract, stationary growth phase, strain L1-8151
2.79
Roseburia sp.
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in crude cell extract, stationary growth phase, strain A2-181
8.9
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in crude cell extract, stationary growth phase, strain L1-82
9.1
Roseburia sp.
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in crude cell extract, stationary growth phase, strain A2-183
9.24
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in crude cell extract, exponential growth phase, strain L1-8151
10.8
Coprococcus sp.
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in crude cell extract, stationary growth phase, strain L2-50
15.58
Roseburia sp.
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in crude cell extract, exponential growth phase, strain A2-181
17.45
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in crude cell extract, exponential growth phase, strain L1-952
18.64
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in crude cell extract, exponential growth phase, strain A2-165
19
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in crude cell extract, stationary growth phase, strain A2-165
25.5
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in crude cell extract, exponential growth phase, strain L1-82
38.95
Roseburia sp.
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in crude cell extract, exponential growth phase, strain A2-183
118.4
Coprococcus sp.
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in crude cell extract, exponential growth phase, strain L2-50
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Escherichia coli (strain K12)
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dimer
alpha subunit assembles as a dimer
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hanging drop vapor diffusion method, using 1.7-2.0 M ammonium sulfate, 0.2 M sodium chloride, 0.1 M sodium cacodylate (pH 6.5), and 25 mM 2-mercaptoethanol
hanging drop vapor diffusion method, alpha subunit, native enzyme and SeMet-derivatized protein
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ammonium sulfate precipitation, dye-affinity chromatography, ion-exchange column chromatography, and gel filtration
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expressed in Escherichia coli C41(DE3) cells
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E294A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
E435D
the mutant shows almost wild type activity
R228E
the mutant has a specific defect in its ability to bind both carboxylate substrates succinyl-CoA and acetyl-CoA and does not use 4-aminobutyrate as substrate
S71A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
E294A
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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E435A
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insoluble mutant
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E435Q
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insoluble mutant
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R228E
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the mutant has a specific defect in its ability to bind both carboxylate substrates succinyl-CoA and acetyl-CoA and does not use 4-aminobutyrate as substrate
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S71A
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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molecular biology
a new degenerated real-time PCR approach to simultaneously quantify phylogenetically different butyrate-producing bacteria based on the detection of butyryl-coenzyme A (CoA) CoA transferase genes is described
molecular biology
a new degenerated real-time PCR approach to simultaneously quantify phylogenetically different butyrate-producing bacteria based on the detection of butyryl-coenzyme A (CoA) CoA transferase genes is described
molecular biology
a new degenerated real-time PCR approach to simultaneously quantify phylogenetically different butyrate-producing bacteria based on the detection of butyryl-coenzyme A (CoA) CoA transferase genes is described
molecular biology
a new degenerated real-time PCR approach to simultaneously quantify phylogenetically different butyrate-producing bacteria based on the detection of butyryl-coenzyme A (CoA) CoA transferase genes is described
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Vanderwinkel, E.; Furmanski, P.; Reeves, H.C.; Ajl, S.J.
Growth of Escherichia coli on fatty acids: requirement for coenzyme A transferase activity
Biochem. Biophys. Res. Commun.
33
902-908
1968
Escherichia coli
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Duncan, S.H.; Barcenilla, A.; Stewart, C.S.; Pryde, S.E.; Flint, H.J.
Acetate utilization and butyryl coenzyme A (CoA):acetate-CoA transferase in butyrate-producing bacteria from the human large intestine
Appl. Environ. Microbiol.
68
5186-5190
2002
Coprococcus sp., Coprococcus sp. L2-50, Faecalibacterium prausnitzii, Roseburia intestinalis, Roseburia intestinalis L1-82, Roseburia sp., Roseburia sp. A2-181
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Korolev, S.; Koroleva, O.; Petterson, K.; Gu, M.; Collart, F.; Dementieva, I.; Joachimiak, A.
Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data
Acta Crystallogr. Sect. D
58
2116-2121
2002
Escherichia coli, Escherichia coli (P76458)
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Louis, P.; Flint, H.J.
Development of a semiquantitative degenerate real-time PCR-based assay for estimation of numbers of butyryl-coenzyme A (CoA) CoA transferase genes in complex bacterial samples
Appl. Environ. Microbiol.
73
2009-2012
2007
Anaerostipes caccae (Q2QB27), Eubacterium hallii (Q2QIH1), Faecalibacterium prausnitzii (Q2QIH0), Roseburia hominis (Q2TME9)
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Mullins, E.A.; Kappock, T.J.
Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases
Biochemistry
51
8422-8434
2012
Acetobacter aceti (B3EY95)
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Louis, P.; Young, P.; Holtrop, G.; Flint, H.
Diversity of human colonic butyrate-producing bacteria revealed by analysis of the butyryl-CoA:acetate CoA-transferase gene
Environ. Microbiol.
12
304-314
2010
(D2WEY1), Anaerostipes caccae (B0MC58), Anaerostipes caccae L1-92 (B0MC58), Butyrivibrio fibrisolvens 16/4 (D2WEY7), Butyrivibrio fibrisolvens (D2WEY7), DSM 17629 (D2WEY1), Eubacterium hallii (D2WEY8), Eubacterium hallii, Eubacterium hallii M72/1 (D2WEY8), Faecalibacterium prausnitzii (A8SFP6), Faecalibacterium prausnitzii (C7H5K4), Faecalibacterium prausnitzii (D2WEZ2), Faecalibacterium prausnitzii, Faecalibacterium prausnitzii A2-165 (C7H5K4), Faecalibacterium prausnitzii L2-6 (D2WEZ2), Faecalibacterium prausnitzii M21/2 (A8SFP6), Roseburia intestinalis (C7GB37), Roseburia intestinalis L1-82 (C7GB37), Roseburia inulinivorans (D2WEY6), Roseburia inulinivorans A2-194 (D2WEY6)
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Millerioux, Y.; Morand, P.; Biran, M.; Mazet, M.; Moreau, P.; Wargnies, M.; Ebikeme, C.; Deramchia, K.; Gales, L.; Portais, J.C.; Boshart, M.; Franconi, J.M.; Bringaud, F.
ATP synthesis-coupled and -uncoupled acetate production from acetyl-CoA by mitochondrial acetate:succinate CoA-transferase and acetyl-CoA thioesterase in Trypanosoma
J. Biol. Chem.
287
17186-17197
2012
Trypanosoma brucei
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Enzyme Nomenclature
COMMENTARY
2.8.3.8-RECOMMENDED NAME
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