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 hide
2.8.3.8
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RECOMMENDED NAME
GeneOntology No.
acetate CoA-transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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Butanoate metabolism
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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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Metabolic pathways
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Microbial metabolism in diverse environments
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Propanoate metabolism
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propanol degradation
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succinate fermentation to butanoate
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetate CoA-transferase
Acts on butanoyl-CoA and pentanoyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-35-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
DSM 17629
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Coprococcus sp.
strain L2-50, exponential and stationary phase
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Manually annotated by BRENDA team
Coprococcus sp. L2-50
strain L2-50, exponential and stationary phase
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Roseburia sp.
strain A2-181, A2-183, exponential and stationary phase
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Manually annotated by BRENDA team
Roseburia sp. A2-181
strain A2-181, A2-183, exponential and stationary phase
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetate + succinyl-CoA
succinate + acetyl-CoA
show the reaction diagram
butanoyl-CoA + acetate
?
show the reaction diagram
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provides ability to grow on various fatty acids
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r
butanoyl-CoA + acetate
butanoate + acetyl-CoA
show the reaction diagram
pentanoyl-CoA + acetate
pentanoate + acetyl-CoA
show the reaction diagram
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r
succinate + acetyl-CoA
acetate + succinyl-CoA
show the reaction diagram
valeryl-CoA + acetate
valerate + acetyl-CoA
show the reaction diagram
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r
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
butanoyl-CoA + acetate
?
show the reaction diagram
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provides ability to grow on various fatty acids
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r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
contains 3 Mg2+ ions, none of them located near the putative active site, functional relevance is not clear
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
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 hide
LITERATURE
IMAGE
0.029 - 2600
acetate
0.7 - 52
acetyl-CoA
0.03 - 79
succinate
0.074 - 9
succinyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
98% pure, alpha subunit
ammonium sulfate precipitation, dye-affinity chromatography, ion-exchange column chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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