Information on EC 2.8.3.18 - succinyl-CoA:acetate CoA-transferase

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

EC NUMBER
COMMENTARY hide
2.8.3.18
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RECOMMENDED NAME
GeneOntology No.
succinyl-CoA:acetate CoA-transferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + acetate = acetyl-CoA + succinate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
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-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA III (succinate)
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-
anaerobic energy metabolism (invertebrates, mitochondrial)
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succinate fermentation to butanoate
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TCA cycle VII (acetate-producers)
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citric acid cycle
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Citrate cycle (TCA cycle)
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Pyruvate metabolism
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Butanoate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:acetate CoA-transferase
In acetic acid bacteria the enzyme, which is highly specific, catalyses the conversion of toxic acetate to acetyl-CoA [2,3]. In the hydrogenosomes of some trichomonads the enzyme catalyses the production of acetate [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
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
-
-
-
r
acetoacetate + succinyl-CoA
succinate + acetoacetyl-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetoacetate
acetoacetyl-CoA + acetate
show the reaction diagram
0.35% of the activity with succinate
-
-
r
acetyl-CoA + D-malate
D-malyl-CoA + acetate
show the reaction diagram
0.28% of the activity with succinate
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r
acetyl-CoA + fumarate
fumaryl-CoA + acetate
show the reaction diagram
0.20% of the activity with succinate
-
-
r
acetyl-CoA + propionate
propionyl-CoA + acetate
show the reaction diagram
0.34% of the activity with succinate
-
-
r
acetyl-CoA + succinate
succinyl-CoA + acetate
show the reaction diagram
succinate + acetyl-CoA
acetate + succinyl-CoA
show the reaction diagram
succinate + dethiaacetyl-CoA
?
show the reaction diagram
-
-
-
?
succinyl-CoA + acetate
acetyl-CoA + succinate
show the reaction diagram
succinyl-CoA + acetoacetate
acetoacetyl-CoA + succinate
show the reaction diagram
succinyl-CoA + D-malate
D-malyl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + DL-methylsuccinate
DL-methylsuccinyl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + formate
formyl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + fumarate
fumaryl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + glutarate
glutaryl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + L-malate
L-malyl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + oxaloacetate
oxaloacetyl-CoA + succinate
show the reaction diagram
-
-
-
?
succinyl-CoA + propionate
propionyl-CoA + succinate
show the reaction diagram
-
-
-
?
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
succinate + acetyl-CoA
acetate + succinyl-CoA
show the reaction diagram
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acetate producing pathway
-
-
?
succinyl-CoA + acetate
acetyl-CoA + succinate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
citrate
weak competitive inhibition against succinate
dethiaacetyl-CoA
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;
Sodium borohydride
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-
succinate
weak competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29 - 70
acetate
130
acetoacetate
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; pH 8.0, 25°C
0.022 - 0.0223
acetyl-CoA
0.045 - 0.9
succinate
0.0221
succinyl-CoA
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; pH 8.0, 25°C
additional information
additional information
steady-state kinetic analysis using a Michaelis-Menten model, a substrate inhibition model, or a competitive inhibition model, overview. Arg228 has an important kinetic role in carboxylate substrate binding
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49 - 280
acetate
36.5
acetoacetate
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; pH 8.0, 25°C
75.2
acetyl-CoA
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; pH 8.0, 25°C
70.9
succinate
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; pH 8.0, 25°C
201
succinyl-CoA
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; pH 8.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029 - 4
acetate
0.28
acetoacetate
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pH 8.0, 25°C
0.0007 - 3400
acetyl-CoA
0.03 - 79
succinate
0.000074 - 9000
succinyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
500 - 1600
acetate
150
citrate
pH 8.0, temperature not specified in the publication
0.016 - 0.0166
dethiaacetyl-CoA
150
succinate
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.007
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specific activity of recombinant TvASCT expressed in CHO cells
0.01
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knock out mutant
0.053
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strain 2002, reverse reaction, pH 8.0
0.058
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wildtype
0.083
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strain 1023, reverse reaction, pH 8.0
0.114
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strain 2002, forward reaction, pH 8.0
0.157
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rescued clone, i.e. knock out mutant transfected with the vector pTSArib.ASCT, resulting in overexpression
0.17
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strain 1023, forward reaction, pH 8.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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procyclic cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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SDS-PAGE
55847
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3 * 55847, ESI-MS, 3 * 55847, calculated, His-tagged recombinant protein
57000
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predicted from cDNA
160000
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gel filtration, His-tagged recombinant protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
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3 * 55847, ESI-MS, 3 * 55847, calculated, His-tagged recombinant protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of a C-terminally His6-tagged form of several wild-type and mutant complexes, including freeze-trapped acetylglutamyl anhydride and glutamyl-CoA thioester adducts. The latter shows the acetate product bound to an auxiliary site that is required for efficient carboxylate substrate recognition. Mutant E294A crystallizes in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation. A model of the acetyl-CoA Michaelis complex reveals that the nucleophilic glutamate is held at a near-ideal angle for attack as the thioester oxygen is forced into an oxyanion hole composed of Gly388 NH and CoA N2'' CoA is nearly immobile along its entire length during all stages of the enzyme reaction; native and C-terminally His6-tagged wild-type enzymes in complexes including freeze-trapped acetylglutamyl anhydride and glutamyl-CoA thioester adducts, hanging drop vapor diffusion method, mixing of 0.002 ml of protein solution containing 5.6 mg/ml AarC in 45 mM potassium phosphate, pH 8.0, 90 mM potassium chloride, and 2 mM CoA or 6.0 mg/ml His6-tagged AarC in 45 mM Tris-HCl, pH 8.0, 90 mM potassium chloride, and 2 mM CoA, with 0.002 ml of reservoir solution containing 0.8-1.0 M sodium citrate, 0.1 M imidazole, pH 8.2, and 25 mM 2-mercaptoethanol for orthorhombic crystals or 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 for hexagonal crystals, room temperature of about 22°C, X-ray diffraction structure determination and analysis
enzyme bound to dethiaacetyl-CoA and acetate, hanging drop vapor diffusion method, using 0.9 M sodium citrate, 0.1 M imidazole-HCl, pH 8.2, and 25 mM 2-mercaptoethanol
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 6.8
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721675
3.8
unstable below
721675
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using an ammonium sulfate fractionation procedure and an immobilized-metal affinity step. An 8-liter culture yields 9.5 mg of purified protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells
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expressed in Escherichia coli as a C-terminal hexahistidine-containing fusion peptide; expression in Escherichia coli
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expressed in Escherichia coli C41(DE3) cells
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expression in Escherichia coli; gene aarC, sequence comparisons and phylogenetic analysis, expression of C-terminally His6-tagged wild-type and mutant enzymes
overexpression in Trypanosoma brucei
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E294A
complete loss of activity; site-directed mutagenesis, the mutant specific catalytic activity is 10000fold reduced compared to the wild-type enzyme, ligand bound crystal structure modeling
E435A
mutant protein is completely insoluble; site-directed mutagenesis, the mutant is completely insoluble, ligand bound crystal structure determination and analysis, the mutant crystallizes in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation
E435D
activity similar to wild-type; site-directed mutagenesis, the mutant catalytic properties are nearly equivalent to those of the His6-tagged wild-type enzyme, ligand bound crystal structure modeling
E435Q
mutant protein is completely insoluble; site-directed mutagenesis, the mutant is completely insoluble, ligand bound crystal structure modeling
R228E
large decrease in catalytic activity; site-directed mutagenesis, the mutant has a specific defect in its ability to bind both carboxylate substrates, ligand bound crystal structure modeling
S71A
large decrease in catalytic activity; site-directed mutagenesis, the mutant shows impaired catalytic activity associated with lower kcat values, ligand bound crystal structure modeling
N347A
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the mutant retains about 15% of wild type specific activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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the enzyme seems to be a logical target for broad-spectrum anti-parasitic drugs