Information on EC 2.8.3.8 - acetate CoA-transferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.8.3.8
-
RECOMMENDED NAME
GeneOntology No.
acetate CoA-transferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
coenzyme A transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation V
-
-
acetyl-CoA fermentation to butanoate II
-
-
gallate degradation III (anaerobic)
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
succinate fermentation to butanoate
-
-
butanoate fermentation
-
-
glutamate and glutamine metabolism
-
-
propanol degradation
-
-
Aminobenzoate degradation
-
-
Propanoate metabolism
-
-
Butanoate metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetate CoA-transferase
Acts on butanoyl-CoA and pentanoyl-CoA.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetate coenzyme A-transferase
-
-
-
-
acetate:succinate CoA-transferase
-
-
butyryl CoA:acetate CoA transferase
-
-
-
-
butyryl coenzyme A transferase
-
-
-
-
butyryl-CoA:acetate CoA-transferase
-
-
butyryl-CoA:acetate CoA-transferase
DSM 17629
-
-
butyryl-CoA:acetate CoA-transferase
-
butyryl-CoA:acetate CoA-transferase
Anaerostipes caccae L1-92
-
-
butyryl-CoA:acetate CoA-transferase
-
butyryl-CoA:acetate CoA-transferase
-
-
butyryl-CoA:acetate CoA-transferase
-
butyryl-CoA:acetate CoA-transferase
Eubacterium hallii M72/1
-
-
butyryl-CoA:acetate CoA-transferase
-
butyryl-CoA:acetate CoA-transferase
-
-
butyryl-CoA:acetate CoA-transferase
-
-
butyryl-CoA:acetate CoA-transferase
-
-
butyryl-CoA:acetate CoA-transferase
-
butyryl-CoA:acetate CoA-transferase
-
-
butyryl-CoA:acetate CoA-transferase
-
butyryl-CoA:acetate CoA-transferase
Roseburia inulinivorans A2-194
-
-
butyryl-coenzyme A CoA transferase
-
butyryl-coenzyme A CoA transferase
-
butyryl-coenzyme A CoA transferase
-
butyryl-coenzyme A CoA transferase
-
coenzyme A-transferase, acetate
-
-
-
-
succinyl-CoA:acetate CoA transferase
-
-
-
-
succinyl-CoA:acetate CoA-transferase
-
succinyl-CoA:acetate CoA-transferase
-
-
succinyl-coenzyme A:acetate CoA-transferase
-
succinyl-coenzyme A:acetate CoA-transferase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37278-35-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
UniProt
Manually annotated by BRENDA team
DSM 17629
-
UniProt
Manually annotated by BRENDA team
Anaerostipes caccae L1-92
-
UniProt
Manually annotated by BRENDA team
Coprococcus sp.
strain L2-50, exponential and stationary phase
-
-
Manually annotated by BRENDA team
Coprococcus sp. L2-50
strain L2-50, exponential and stationary phase
-
-
Manually annotated by BRENDA team
K12, constitutive mutant strain V10 and strain D5H3G7
-
-
Manually annotated by BRENDA team
Eubacterium hallii M72/1
-
UniProt
Manually annotated by BRENDA team
formerly Fusobacterium, strain A2-165, exponential and stationary phase
-
-
Manually annotated by BRENDA team
strain L1-82, L1-952, L1-8151, exponential and stationary phase
-
-
Manually annotated by BRENDA team
strain L1-82, L1-952, L1-8151, exponential and stationary phase
-
-
Manually annotated by BRENDA team
Roseburia inulinivorans A2-194
-
UniProt
Manually annotated by BRENDA team
Roseburia sp.
strain A2-181, A2-183, exponential and stationary phase
-
-
Manually annotated by BRENDA team
Roseburia sp. A2-181
strain A2-181, A2-183, exponential and stationary phase
-
-
Manually annotated by BRENDA team
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
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
-
succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + succinyl-CoA
succinate + acetyl-CoA
show the reaction diagram
5.1% activity compared to succinate
-
r
acetate + succinyl-CoA
succinate + acetyl-CoA
show the reaction diagram
-
5.1% activity compared to succinate
-
r
butanoyl-CoA + acetate
butanoate + acetyl-CoA
show the reaction diagram
Coprococcus sp., Roseburia sp., Faecalibacterium prausnitzii, Roseburia intestinalis
-
-
-
?
butanoyl-CoA + acetate
butanoate + acetyl-CoA
show the reaction diagram
-
best substrate
-
r
butanoyl-CoA + acetate
butanoate + acetyl-CoA
show the reaction diagram
Roseburia intestinalis L1-82, Roseburia sp. A2-181, Coprococcus sp. L2-50
-
-
-
?
pentanoyl-CoA + acetate
pentanoate + acetyl-CoA
show the reaction diagram
-
-
-
r
succinate + acetyl-CoA
acetate + succinyl-CoA
show the reaction diagram
-
-
-
?
succinate + acetyl-CoA
acetate + succinyl-CoA
show the reaction diagram
100% activity
-
r
succinate + acetyl-CoA
acetate + succinyl-CoA
show the reaction diagram
-
100% activity
-
r
valeryl-CoA + acetate
valerate + acetyl-CoA
show the reaction diagram
-
-
-
r
butanoyl-CoA + acetate
?
show the reaction diagram
-
provides ability to grow on various fatty acids
-
-
r
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
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
butanoyl-CoA + acetate
?
show the reaction diagram
-
provides ability to grow on various fatty acids
-
-
r
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
290
acetate
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.029
acetate
Acetobacter aceti
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
47
0.16
acetate
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
47
0.6
acetate
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
47
3
acetate
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
47
2600
acetate
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
47
0.7
acetyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C; mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
29
2.3
acetyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
29
3.4
acetyl-CoA
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
29
52
acetyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
29
0.03
succinate
Acetobacter aceti
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
58
0.3
succinate
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
58
2.7
succinate
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
58
73
succinate
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
58
79
succinate
Acetobacter aceti
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
58
0.074
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
224
0.13
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
224
0.39
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
224
9
succinyl-CoA
Acetobacter aceti
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C; wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
224
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 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1 - 1
-
in crude cell extract
1.32
-
in crude cell extract, stationary growth phase, strain L1-952
2.05
-
in crude cell extract, stationary growth phase, strain L1-8151
2.79
Roseburia sp.
-
in crude cell extract, stationary growth phase, strain A2-181
8.9
-
in crude cell extract, stationary growth phase, strain L1-82
9.1
Roseburia sp.
-
in crude cell extract, stationary growth phase, strain A2-183
9.24
-
in crude cell extract, exponential growth phase, strain L1-8151
10.8
Coprococcus sp.
-
in crude cell extract, stationary growth phase, strain L2-50
15.58
Roseburia sp.
-
in crude cell extract, exponential growth phase, strain A2-181
17.45
-
in crude cell extract, exponential growth phase, strain L1-952
18.64
-
in crude cell extract, exponential growth phase, strain A2-165
19
-
in crude cell extract, stationary growth phase, strain A2-165
25.5
-
in crude cell extract, exponential growth phase, strain L1-82
38.95
Roseburia sp.
-
in crude cell extract, exponential growth phase, strain A2-183
118.4
Coprococcus sp.
-
in crude cell extract, exponential growth phase, strain L2-50
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
alpha subunit assembles as a dimer
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, dye-affinity chromatography, ion-exchange column chromatography, and gel filtration
98% pure, alpha subunit
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E294A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
E435A
insoluble mutant
E435D
the mutant shows almost wild type activity
E435Q
insoluble mutant
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
-
E435A
-
insoluble mutant
-
E435Q
-
insoluble mutant
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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