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Information on EC 2.8.3.9 - butyrate-acetoacetate CoA-transferase
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2.8.3.9 butyrate-acetoacetate CoA-transferaseIUBMB Comments
Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C2 to C6 monocarboxylic acids.
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Word Map
- 2.8.3.9
- clostridium
- acetobutylicum
- butanol
- acetone
-
thiolase
- atcc824
- beijerinckii
- acetoacetyl-coa
-
acetone-butanol-ethanol
-
re-assimilate
-
solventogenesis
-
facultative
-
biofuel
-
megaplasmid
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ctfab, butyrate-acetoacetate coa-transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
butyryl coenzyme A-acetoacetate coenzyme A-transferase
-
-
-
-
butyryl-CoA-acetoacetate CoA-transferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA
butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C2 to C6 monocarboxylic acids
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
coenzyme A transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
butanoyl-CoA:acetoacetate CoA-transferase
Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C2 to C6 monocarboxylic acids.
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CAS REGISTRY NUMBER
COMMENTARY
66231-37-6
-
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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
3-hydroxypropanoate + acetoacetyl-CoA
3-hydroxypropanoyl-CoA + acetoacetate
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reaction at 8.6% the rate of butyrate
-
-
r
3-mercaptopropionate + acetoacetyl-CoA
3-mercaptopropionyl-CoA + acetoacetate
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reaction at 71% the rate of butyrate
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-
r
3-methylvinylacetate + acetoacetyl-CoA
3-methylvinylacetyl-CoA + acetoacetate
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reaction at 44% the rate of butyrate
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-
r
4-hydroxybutyrate + acetoacetyl-CoA
4-hydroxybutanoyl-CoA + acetoacetate
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reaction at 14% the rate of butyrate
-
-
r
4-pentenoate + acetoacetyl-CoA
4-pentenoyl-CoA + acetoacetate
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reaction at 21% the rate of acetate
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-
r
acrylate + acetoacetyl-CoA
acrylyl-CoA + acetoacetate
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reaction at 10% the rate of butyrate
-
-
r
butanoyl-CoA + 2-methylacetoacetate
butanoate + 2-methylacetoacetyl-CoA
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used 12% as fast as acetoacetate
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r
butanoyl-CoA + 3-oxohexanoate
butanoate + 3-oxohexanoyl-CoA
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used 21% as fast as acetoacetate
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r
butanoyl-CoA + 3-oxopentanoate
butanoate + 3-oxopentanoyl-CoA
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used 60% as fast as acetoacetate
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r
butyrate + acetyl-CoA
butyryl-CoA + acetate
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reaction at 56% the rate of acetoacetate, reverse reaction at 86% the rate of acetoacetyl-CoA
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r
crotonate + acetoacetyl-CoA
crotonyl-CoA + acetoacetate
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reaction at 16% the rate of butyrate
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r
crotonyl-CoA + acetate
crotonate + acetyl-CoA
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reaction at 4% the rate of acetoacetylCoA
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r
DL-2-hydroxybutyrate + acetoacetyl-CoA
2-hydroxybutyryl-CoA + acetoacetate
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reaction at 19% the rate of butyrate
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-
r
DL-2-hydroxypentanoate + acetoacetyl-CoA
2-hydroxypentanoyl-CoA + acetoacetate
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reaction at 7.9% the rate of butyrate
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-
r
DL-3-hydroxybutyrate + acetoacetyl-CoA
3-hydroxybutyryl-CoA + acetoacetate
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reaction at 30% the rate of butyrate
-
-
r
DL-3-hydroxybutyrate + acetyl-CoA
3-hydroxybutyryl-CoA + acetate
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reaction at 9% the rate of acetoacetate
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-
r
epsilon-acetyl-CoA + acetoacetate
acetate + acetoacetyl-CoA
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reaction at 1% the rate of acetylCoA
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r
formate + acetoacetyl-CoA
formyl-CoA + acetoacetate
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reaction at 7% the rate of acetate
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-
r
isobutyrate + acetoacetyl-CoA
isobutyryl-CoA + acetoacetate
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reaction at 19% the rate of butyrate
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-
r
isopentanoate + acetoacetyl-CoA
isopentanoyl-CoA + acetoacetate
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reaction at 8.3% the rate of butyrate
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-
r
monochloroacetate + acetoacetyl-CoA
monochloroacetyl-CoA + acetoacetate
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reaction at 5.4% the rate of butyrate
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-
r
octanoate + acetoacetyl-CoA
octanoyl-CoA + acetoacetate
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reaction at 3% the rate of acetate
-
-
r
pentanoate + acetoacetyl-CoA
pentanoyl-CoA + acetoacetate
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reaction at 19% the rate of butyrate
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r
vinylacetate + acetoacetyl-CoA
vinylacetyl-CoA + acetoacetate
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best substrate
-
-
r
acetate + acetoacetyl-CoA
acetyl-CoA + acetoacetate
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reaction at 24% the rate of butyrate
-
r
acetate + acetoacetyl-CoA
acetyl-CoA + acetoacetate
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reaction at 24% the rate of butyrate
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r
acetate + acetoacetyl-CoA
acetyl-CoA + acetoacetate
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best substrates
-
r
acetate + acetoacetyl-CoA
acetyl-CoA + acetoacetate
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best substrates
-
r
acetyl-CoA + acetoacetate
acetate + acetoacetyl-CoA
-
best substrates
-
r
acetyl-CoA + acetoacetate
acetate + acetoacetyl-CoA
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best substrates
-
r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
-
-
-
r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
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lysine degradation pathway
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r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
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lysine degradation pathway
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r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
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reaction at 68% the rate of acetate
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r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
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reaction at 68% the rate of acetate
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r
propionate + acetoacetyl-CoA
propionyl-CoA + acetoacetate
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reaction at 21% the rate of butyrate
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r
additional information
?
-
-
monofluoroacetate and hexanoate are no substrates, compounds found to be unreactive or less than 0.1% as reactive as butyrate are formate, cyanoacetate, n-heptanoate, tiglate, oxalate, malonate, succinate, citramalate, DL-alpha-hydroxyisobutyrate, 3,4-dihydroxybutyrate, alpha-ketobutyrate, 2-oxoglutarate, DL-3-aminobutyrate and 4-aminobutyrate, 3-oxo-5-aminohexanoate and triacetate are unreactive
-
-
?
additional information
?
-
-
monofluoroacetate and hexanoate are no substrates, compounds found to be unreactive or less than 0.1% as reactive as butyrate are formate, cyanoacetate, n-heptanoate, tiglate, oxalate, malonate, succinate, citramalate, DL-alpha-hydroxyisobutyrate, 3,4-dihydroxybutyrate, alpha-ketobutyrate, 2-oxoglutarate, DL-3-aminobutyrate and 4-aminobutyrate, 3-oxo-5-aminohexanoate and triacetate are unreactive
-
-
?
additional information
?
-
-
decanoyl-CoA and succinyl-CoA cannot replace acetoacetyl-CoA, succinate, malonate and 2,3-butandienoate cannot replace acetate, 3-carbon dicarboxylic and 4-carbon dicarboxylic acids are completely inactive as substrates
-
-
?
additional information
?
-
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decanoyl-CoA and succinyl-CoA cannot replace acetoacetyl-CoA, succinate, malonate and 2,3-butandienoate cannot replace acetate, 3-carbon dicarboxylic and 4-carbon dicarboxylic acids are completely inactive as substrates
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-
?
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NATURAL SUBSTRATE
NATURAL 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
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
-
-
-
r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
-
lysine degradation pathway
-
r
butanoate + acetoacetyl-CoA
butanoyl-CoA + acetoacetate
-
lysine degradation pathway
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r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activation at 6 mM CaCl2, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
K+
-
activation at 0.08 M KCl, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
Li+
-
activation at 0.2 M LiCl, inhibitions at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
Mg2+
-
activation at 12 mM MgCl2, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
Mn2+
-
activation at 1.2 mM MnCl2, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
Na+
-
activation at 0.17 M NaCl, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
NH4+
-
activation at 0.08 M NH4Cl, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
partially inactivated by acyl-CoA substrates in absence of carboxylic acid substrates
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tris-HCl
-
activation at 0.25 M, inhibition at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.054
butyryl-CoA
-
pH 8.1, 25°C, cosubstrate acetoacetate 1.0 mM, 20 mM MgCl2
0.073
butyryl-CoA
-
pH 8.1, 25°C, cosubstrate acetoacetate 2.0 mM, 20 mM MgCl2
0.083
butyryl-CoA
-
pH 8.1, 25°C, cosubstrate acetoacetate 3.0 mM, 20 mM MgCl2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (671 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
-
2 * 23000 + 2 * 26000, 2 alpha and 2 beta subunits, SDS-PAGE
26000
-
2 * 23000 + 2 * 26000, 2 alpha and 2 beta subunits, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
2 * 23000 + 2 * 26000, 2 alpha and 2 beta subunits, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
-
1 h, at 30°C, most stable, about 20% loss of activity at pH 6.0 and 8.0
643838
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
1 h, in potassium phosphate buffer, pH 6.5-7.0, most stable, about 20% loss of activity at pH 6.0 and 8.0
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is very stable, considerably less stable in Tris-HCl than in phosphate buffer
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C 0.0062 mg/ml protein, 10 mM phosphate buffer, pH 7.0, half-life of 12 days when thawed and refrozen 5 times
-
-15°C, 3.1 mg protein/ml, 20 mM potassium phosphate, pH 7.0, retains full activity during storage for 1 year
-
4°C, 0.0062 mg/ml protein, 10 mM phosphate buffer, pH 7.0, half-life of about 7 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sramek, S.J.; Frerman, F.E.
Escherichia coli coenzyme A-transferase: kinetics, catalytic pathway and structure
Arch. Biochem. Biophys.
171
27-35
1975
Escherichia coli, Escherichia coli C22
brenda
Sramek, S.J.; Frerman, F.E.
Purification and properties of Escherichia coli coenzyme A-transferase
Arch. Biochem. Biophys.
171
14-26
1975
Escherichia coli, Escherichia coli C22
brenda
Barker, H.A.; Jemg, I.M.; Neff, N.; Robertson, J.M.; Tam, F.K.; Hosaka, S.
Butyryl-CoA:acetoacetate CoA-transferase from a lysine-fermenting Clostridium
J. Biol. Chem.
253
1219-1225
1978
Acetoanaerobium sticklandii, Clostridium sp., Clostridium sp. SB4
brenda
Emmanuel, B.; Milligan, L.P.
Butyrate:acetoacetyl-CoA transferase activity in bovine rumen epithelium
Can. J. Anim. Sci.
63
355-360
1983
Bos taurus
-
brenda
Yu, L.; Zhao, J.; Xu, M.; Dong, J.; Varghese, S.; Yu, M.; Tang, I.; Yang, S.
Metabolic engineering of Clostridium tyrobutyricum for n-butanol production: effects of CoA transferase
Appl. Microbiol. Biotechnol.
99
4917-4930
2015
Clostridium tyrobutyricum
brenda
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