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 ACCESSION NO.
LITERATURE
acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
coenzyme A transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobutyrate degradation V
-
acetyl-CoA fermentation to butyrate II
-
Aminobenzoate degradation
-
Butanoate metabolism
-
gallate degradation III (anaerobic)
-
glutamate degradation V (via hydroxyglutarate)
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Propanoate metabolism
-
succinate fermentation to butyrate
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetate CoA-transferase
Acts on butanoyl-CoA and pentanoyl-CoA.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AarC
B3EY95
-
acetate coenzyme A-transferase
-
-
-
-
acetate:succinate CoA-transferase
-
-
butyryl CoA:acetate CoA transferase
-
-
-
-
butyryl coenzyme A transferase
-
-
-
-
butyryl-CoA:acetate CoA-transferase
B0MC58
-
butyryl-CoA:acetate CoA-transferase
Anaerostipes caccae L1-92
B0MC58
-
-
butyryl-CoA:acetate CoA-transferase
D2WEY7
-
butyryl-CoA:acetate CoA-transferase
D2WEY7
-
-
butyryl-CoA:acetate CoA-transferase
D2WEY8
-
butyryl-CoA:acetate CoA-transferase
Eubacterium hallii M72/1
D2WEY8
-
-
butyryl-CoA:acetate CoA-transferase
D2WEY1
-
butyryl-CoA:acetate CoA-transferase
Eubacterium rectale A1-86
D2WEY1
-
-
butyryl-CoA:acetate CoA-transferase
A8SFP6, C7H5K4, D2WEZ2
-
butyryl-CoA:acetate CoA-transferase
C7H5K4
-
-
butyryl-CoA:acetate CoA-transferase
D2WEZ2
-
-
butyryl-CoA:acetate CoA-transferase
A8SFP6
-
-
butyryl-CoA:acetate CoA-transferase
C7GB37
-
butyryl-CoA:acetate CoA-transferase
C7GB37
-
-
butyryl-CoA:acetate CoA-transferase
D2WEY6
-
butyryl-CoA:acetate CoA-transferase
Roseburia inulinivorans A2-194
D2WEY6
-
-
butyryl-coenzyme A CoA transferase
Q2QB27
-
butyryl-coenzyme A CoA transferase
Q2QIH1
-
butyryl-coenzyme A CoA transferase
Q2QIH0
-
butyryl-coenzyme A CoA transferase
Q2TME9
-
coenzyme A-transferase, acetate
-
-
-
-
SCACT
B3EY95
-
succinyl-CoA:acetate CoA transferase
-
-
-
-
succinyl-CoA:acetate CoA-transferase
B3EY95
-
succinyl-coenzyme A:acetate CoA-transferase
B3EY95
-
CAS REGISTRY NUMBER
COMMENTARY
37278-35-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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
-
D2WEY8
UniProt
Manually annotated by BRENDA team
Eubacterium hallii M72/1
-
D2WEY8
UniProt
Manually annotated by BRENDA team
Eubacterium rectale A1-86
-
UniProt
Manually annotated by BRENDA team
formerly Fusobacterium, strain A2-165, exponential and stationary phase
-
-
Manually annotated by BRENDA team
-
Q2TME9
Uniprot
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 ACCESSION NO.
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
B3EY95
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
physiological function
B3EY95
the enzyme is an acetic acid resistance factor that is required for acetate resistance
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
B3EY95
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
B3EY95
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
?
-
B3EY95
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-, P76458
contains 3 Mg2+ ions, none of them located near the putative active site, functional relevance is not clear
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetate
B3EY95
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
110
-
acetate
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
290
-
acetate
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.029
-
acetate
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6109
0.16
-
acetate
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6109
0.6
-
acetate
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6109
3
-
acetate
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6109
2600
-
acetate
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6109
0.7
-
acetyl-CoA
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
6194
2.3
-
acetyl-CoA
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6194
3.4
-
acetyl-CoA
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6194
52
-
acetyl-CoA
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
6194
0.03
-
succinate
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16754
0.3
-
succinate
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16754
2.7
-
succinate
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16754
73
-
succinate
B3EY95
mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16754
79
-
succinate
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16754
0.074
-
succinyl-CoA
B3EY95
mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16798
0.13
-
succinyl-CoA
B3EY95
mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16798
0.39
-
succinyl-CoA
B3EY95
mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
16798
9
-
succinyl-CoA
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
16798
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1600
-
acetate
B3EY95
wild type enzyme, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-, P76458
alpha subunit assembles as a dimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
B3EY95
hanging drop vapor diffusion method, alpha subunit, native enzyme and SeMet-derivatized protein
-, P76458
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, dye-affinity chromatography, ion-exchange column chromatography, and gel filtration
B3EY95
98% pure, alpha subunit
-, P76458
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli C41(DE3) cells
B3EY95
alpha subunit
-, P76458
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E294A
B3EY95
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
E435A
B3EY95
insoluble mutant
E435D
B3EY95
the mutant shows almost wild type activity
E435Q
B3EY95
insoluble mutant
R228E
B3EY95
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
B3EY95
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
Q2QB27
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
Q2QIH1
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
Q2QIH0
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
Q2TME9
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