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Enzyme Nomenclature
Information on EC 2.8.3.8 - acetate CoA-transferase
Word Map on EC 2.8.3.8
- 2.8.3.8
- butyrate
-
butyrate-producing
-
faecalibacterium
- microbiota
- prausnitzii
-
faecal
- molecular biology
-
ascts
- vaginalis
- roseburia
- hydrogenosomal
-
trichomonas
-
pyrosequencing
- hepatica
- methylmalonyl-coa
-
fasciola
-
omnivores
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.8.3.8
-
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RECOMMENDED NAME
GeneOntology No.
acetate CoA-transferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
coenzyme A transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetate CoA-transferase
The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. Unlike EC 2.8.3.9, butyrate---acetoacetate CoA-transferase, this enzyme exhibits maximal activity using acetate as the CoA acceptor. Substrate range depends on the specific enzyme. Typical substrates include butanoyl-CoA and pentanoyl-CoA.
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CAS REGISTRY NUMBER
COMMENTARY
37278-35-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Fusobacterium, strain A2-165, exponential and stationary phase
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-
strain L1-82, L1-952, L1-8151, exponential and stationary phase
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
physiological function
metabolism
succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle
metabolism
-
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
-
the enzyme is an acetic acid resistance factor that is required for acetate resistance
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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
butanoyl-CoA + acetate
?
-
provides ability to grow on various fatty acids
-
-
r
acetate + succinyl-CoA
succinate + acetyl-CoA
5.1% activity compared to succinate
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-
r
acetate + succinyl-CoA
succinate + acetyl-CoA
-
5.1% activity compared to succinate
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-
r
acetoacetyl-CoA + acetate
acetoacetate + acetyl-CoA
-
-
-
-
?
acetoacetyl-CoA + acetate
acetoacetate + acetyl-CoA
-
-
-
-
?
butyryl-CoA + acetate
butanoate + acetyl-CoA
-
-
-
-
?
butyryl-CoA + acetate
butanoate + acetyl-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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-
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additional information
?
-
-
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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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
butanoyl-CoA + acetate
?
-
provides ability to grow on various fatty acids
-
-
r
acetoacetyl-CoA + acetate
acetoacetate + acetyl-CoA
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-
-
-
?
acetoacetyl-CoA + acetate
acetoacetate + acetyl-CoA
-
-
-
-
?
butyryl-CoA + acetate
butanoate + acetyl-CoA
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-
-
-
?
butyryl-CoA + acetate
butanoate + acetyl-CoA
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
contains 3 Mg2+ ions, none of them located near the putative active site, functional relevance is not clear
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110
acetate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
290
acetate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.029
acetate
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.16
acetate
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.6
acetate
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
3
acetate
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
2600
acetate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.7
acetyl-CoA
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
2.3
acetyl-CoA
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
3.4
acetyl-CoA
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
52
acetyl-CoA
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.03
succinate
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.3
succinate
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
2.7
succinate
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
73
succinate
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
79
succinate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.074
succinyl-CoA
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.13
succinyl-CoA
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
0.39
succinyl-CoA
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
9
succinyl-CoA
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1600
acetate
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.24
-
in crude cell extract, exponential growth phase, strain L1-8151
17.45
-
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
-
in crude cell extract, stationary growth phase, strain A2-165
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, dye-affinity chromatography, ion-exchange column chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Top10 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E294A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
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
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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LINKS TO OTHER DATABASES (specific for EC-Number 2.8.3.8)
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