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Information on EC 2.8.3.5 - 3-oxoacid CoA-transferase and Organism(s) Sus scrofa and UniProt Accession Q29551

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     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.3 CoA-transferases
                2.8.3.5 3-oxoacid CoA-transferase
IUBMB Comments
Acetoacetate and, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptors; malonyl-CoA can act instead of succinyl-CoA.
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This record set is specific for:
Sus scrofa
UNIPROT: Q29551
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
coa transferase, oxct1, 3-oxoacid coa-transferase, succinyl-coa:3-ketoacid coa transferase, 3-ketoacid coa-transferase, scot-t, succinyl-coa transferase, succinyl-coa:3-oxoacid coa transferase, succinyl-coa:3-oxoacid coa-transferase, succinyl-coa:3-ketoacid coenzyme a transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
succinyl-CoA:3-ketoacid coenzyme A transferase
-
succinyl-CoA:3-oxoacid CoA transferase
-
succinyl-CoA:3-oxoacid coenzyme A transferase
-
3-ketoacid CoA-transferase
-
-
-
-
3-ketoacid coenzyme A transferase
-
-
-
-
3-ketoacid coenzyme A-transferase
-
-
-
-
3-oxo-CoA transferase
-
-
-
-
3-oxoacid CoA dehydrogenase
-
-
-
-
3-oxoacid coenzyme A-transferase
-
-
-
-
acetoacetate succinyl-CoA transferase
-
-
-
-
acetoacetyl coenzyme A-succinic thiophorase
-
-
-
-
CoA transferase
-
-
coenzyme A-transferase, 3-oxoacid
-
-
-
-
SCOT-t
-
-
-
-
succinyl coenzyme A-acetoacetyl coenzyme A-transferase
-
-
-
-
succinyl-CoA transferase
-
-
-
-
succinyl-CoA:3-ketoacid CoA transferase
-
-
succinyl-CoA:3-ketoacid coenzyme A transferase
-
-
succinyl-CoA:acetoacetate CoA transferase
-
-
-
-
testis-specific succinyl-CoA:3-oxo-acid CoA-transferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A transfer
SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:3-oxo-acid CoA-transferase
Acetoacetate and, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptors; malonyl-CoA can act instead of succinyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-43-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
show the reaction diagram
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
show the reaction diagram
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
show the reaction diagram
essential enzyme in the metabolism of ketone bodies in higher animals
-
-
?
succinyl-CoA + acetoacetate
?
show the reaction diagram
-
key enzyme in ketone body metabolism
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
show the reaction diagram
additional information
?
-
-
catalyzes exchange reactions in the absence of cosubstrates: succinate/succinyl-CoA and acetoacetate/acetoacetyl-CoA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
show the reaction diagram
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
show the reaction diagram
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
show the reaction diagram
essential enzyme in the metabolism of ketone bodies in higher animals
-
-
?
succinyl-CoA + acetoacetate
?
show the reaction diagram
-
key enzyme in ketone body metabolism
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
four potassium ions are found in the crystal structure, they are actually two pairs with pair bound to each of the monomers
PO43-
-
one phosphate ion is found in the crystal structure, it is located in the same crevice as the pair of potassium ions that are bound to chain B
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
slow inactivation of the free enzyme by the thiol-modifying reagent DTNB, wild-type SCOT and C196S are both inactivated by DTNB with more rapid kinetics in the presence of succinyl- or acetoacetyl-CoA (about 70-80% inactivation in 25 min) than in the absence of acyl-CoA (only about 30% inactivation in 25 min and about 40-50% inactivation in 50 min), the rate of C28S inactivation by DTNB is accelerated to a much lesser extent by succinyl- or acetoacetyl-CoA, and C28S is inactivated less rapidly than wild-type SCOT or C196S, the inactivation with DNTB is reversible, the enzyme can be reactivated by adding dithiothreitol, kinetics of inactivation by DNTB
acetoacetate
product inhibition
Br-
same inhibition as I-, stronger inhibition than Cl-, the kind of cation has no inhibitory effect
Cl-
lower inhibition than Br-, stronger inhibition than F-, the kind of cation has no inhibitory effect
ClO4-
lower inhibition than SCN-, stronger inhibition than I-, the kind of cation has no inhibitory effect
F-
lowest inhibition, the kind of cation has no inhibitory effect
I-
lower inhibition than ClO4-, same inhibition as Br-, the kind of cation has no inhibitory effect
SCN-
strongest inhibition, the kind of cation has no inhibitory effect
succinyl-CoA
product inhibition
2,4-Dinitrophenylacetate
-
at pH 7.9, less inactivating activity at pH 7, acetoacetyl-CoA protects
2-Nitro-5-(thiocyanato)benzoate
-
kinetics, methyl methanethiosulfonate and 5,5'-dithiobis(2-nitro-benzoate) protect, DTT removes this protection
4-nitrophenylacetate
-
at pH 7.9, less inactivating activity at pH 7
Acetic anhydride
-
-
acetoacetate
acetoacetyl-CoA
Acetylimidazole
-
equally efficient at pH 7 and 7.9
ADP
-
-
Blue MY-2G
-
-
-
citrate
-
0.167 M, weak
coenzyme A
-
-
desulfo-CoA
-
competitive inhibition with respect to acetoacetyl-CoA
desulfopantetheine
-
competitive inhibition with respect to acetoacetyl-CoA
DTNB
rapid inactivation of wild-type enzyme and mutant C196S, less rapid inactivation of mutant C28S, CoA, linked to the enzyme, allows the rapid modification of Cys28 by 5,5'-dithiobis(2-nitrobenzoicacid), reflecting a conformational change of SCOT upon formation of the thioester, overview
Glutarate
-
0.1 M, weak
HPO42-
-
0.1 M, weak
malate
-
0.1 M, weak
malonate
-
0.1 M, weak
Monovalent anions
-
decreasing order of effectiveness: SCN-, ClO4-, I-, Br-, Cl-, not F-
-
N-acetylaletheine
-
reacts with the enzyme thiol ester E-CoA to form a catalytically inactive enzyme
N-acetylcysteamine
-
reacts with the enzyme thiol ester E-CoA to form a catalytically inactive enzyme
NaCl
-
kinetics, 24% inhibition at 10 mM
NaI
-
57% inhibition at 10 mM
pantothenol
-
-
SCN-
-
47% inhibition at 10 mM
SO42-
-
0.1 M, weak
Sodium borohydride
-
5 mM
succinate
succinyl-CoA
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sodium sulfate
-
increases the activity at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.1
acetoacetate
0.06 - 0.2
acetoacetyl-CoA
13 - 39
succinate
1.7 - 8
succinyl-CoA
0.0002 - 0.2
acetoacetate
0.006 - 0.72
acetoacetyl-CoA
13 - 39
succinate
1.7 - 8
succinyl-CoA
additional information
additional information
-
kinetic study
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.17 - 98.3
acetoacetate
58.3 - 1250
acetoacetyl-CoA
37.3
succinyl-CoA
-
pH 8.1
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
acetoacetate
-
pH 8.1
0.13
acetoacetyl CoA
-
pH 8.1
45
ADP
-
pH 8.1, 25°
1.7
CoA
-
pH 8.1, 25°
2.7
desulfo-CoA
-
pH 8.1, 25°
110
desulfopoantetheine
-
pH 8.1, 25°
120
pantothenol
-
pH 8.1, 25°
1
succinate
-
pH 8.1
1.9
succinyl-CoA
-
pH 8.1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22.4
C196S mutant
25.2
wild-type SCOT
6
C28A mutant, similar to C28S mutant
7.1
C28S mutant, 3.6times lower than wild-type enzyme
145
-
-
22.4
purified recombinant mutant C196S
225.8
-
-
25.2
purified recombinant wild-type enzyme
280
-
-
3.9 - 4.5
-
-
7.1
purified recombinant mutant C28S
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.7
-
-
8.1 - 9.1
assay at
8.5
-
assay at
9.1
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 8.7
-
about 50% of activity at pH 7.1, optimum at pH 8-8.7
7.5 - 8.8
-
decreasing activity with increasing pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21 - 22
assay at
22
-
assay at
25
-
assay at
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, brain enzyme
5.5
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, heart and kidney enzyme
5.7
-
4 isozymes with pI: 5.7, 5.9, 6.2 and 6.5
5.9
-
4 isozymes with pI: 5.7, 5.9, 6.2 and 6.5
6.2
-
4 isozymes with pI: 5.7, 5.9, 6.2 and 6.5
6.5
-
4 isozymes with pI: 5.7, 5.9, 6.2 and 6.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCOT1_PIG
520
0
56338
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52230
4 * 52230, calculated from amino acid sequence
101000
-
dimeric form, sedimentation equilibrium experiments
105000
-
SDS-PAGE after cross-linking with dimethyl dodecanediimidate
113000
-
gel filtration
218000
-
tetrameric form, sedimentation equilibrium experiments
45600
-
2 * 45600, sedimentation equilibrium in 6 M guanidine chloride
52000
-
SDS-PAGE
52197
-
2 * 52197, deduced from amino acid sequence
52200
-
calculated from nucleotide sequence
53200
55000
78000
80000
-
gel filtration
915000
-
sedimentation equilibrium experiments
92000
-
sedimentation equilibrium centrifugation
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
homodimer
extracted from literature
homotetramer
dimer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
contains galactose, glucose, total sugar content: 1.6%
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
14°C, hanging drop vapor diffusion, structure determination with X-ray crystallography
hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 100 mM Tris-HCl (pH8.5)
hanging drop vapor diffusion method, using 75 mM Tris-HCl pH 8.0, 20% (w/v) PEG 3350 or PEG 4000
orthothrombic crystal form
-
purified recombinant C28S and C28A mutants, hanging drop vapour diffusion method, enzyme in 0.125-0.5 M KCl, 0.5 mM benzamidine, 0.2 mM EDTA, 20 mM 2-mercaptoethanol, and 5 mM Tris-HCl, pH 8.0, the precipitant solution contains 14-22% polyethylene glycol 2000, 0.1 M Tris-HCl, pH 8.0, and 10-15% glycerol, X-ray diffraction structure determination and analysis at 2.0-2.05 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C129S
like wild-type SCOT rapid modification in the presence of acyl-CoA substrates
C196S
specific activity similar to wild-type SCOT
C28A
specific activity similar to C28S mutant
C28S
slow modification in the presence of acyl-CoA substrates, a chloride ion is bound to one of four active sites in the crystal structure of the C28S mutant protein, mimicking substrate, interacting with Lys329, Asn51, and Asn52
C196S
site-directed mutagenesis, the mutant protein is modified rapidly in the presence of acyl-CoA substrates in analogy to the wild-type enzyme
C28S
site-directed mutagenesis, the mutant protein is modified much more slowly than the wild-type enzyme, indicating that Cys28 is the residue exposed on binding CoA, the specific activity of the C28S mutant protein is unexpectedly lower than that of wild-type SCOT
DELTA249-254
-
delta-SCOT, deletion mutant, residues 249-254 are removed
additional information
-
mutant with deletion of amino acid residues 249-254 shows no altered kinetic values
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.7
-
slow loss of activity at 25°C
645967
3.1
-
below, 1 min at 25°C, inactivation
645967
5
-
slow loss of activity at 25°C
645967
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
1 min, inactivation at pH-values below pH 3.1 or in 0.1 M NaOH, slow loss of activity at pH 5 and pH 10.7
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is susceptible to proteolytic cleavage to produce a nicked but active enzyme, PMSF and EDTA protect
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1.4 mg protein/ml, 0.02 M potassium phosphate buffer, pH 7.4, t1/2: 9 months
-
-20°C, at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
as described in literature
Ni-NTA agarose column chromatography and Ultrogel AcA 44 column chromatography
4 isozymes, separable by isoelectric focusing
-
N-terminal and C-terminal domain, a mixture of the domains is only active when domains are isolated in the presence of 2-mercaptoethanol
-
partial
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli BL21-DE3
cDNA clone of mature mitochondrial and cytoplasmic precursor to mitochondrial enzyme
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
N-terminal and C-terminal domain
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
intact hydrophilic peptide which links the 2 domains is essential for the recovery of activity observed upon refolding of the denatured enzyme in vitro
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
hereditary SCOT deficiency is one cause of ketoacidosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hersh, L.B.; Jencks, W.P.
Coenzyme A transferase. Kinetics and exchange reactions
J. Biol. Chem.
242
3468-3480
1967
Sus scrofa
-
Manually annotated by BRENDA team
Edwards, M.R.; Singh, M.; Tubbs, P.K.
A simple purification of acetoacetate-succinate CoA-transferase using substrate elution chromatography
FEBS Lett.
37
155-158
1973
Sus scrofa
Manually annotated by BRENDA team
White, H.; Jencks, W.P.
Properties of succinyl-CoA:3-ketoacid coenzyme A transferase
J. Biol. Chem.
251
1708-1711
1976
Sus scrofa
Manually annotated by BRENDA team
Kindman, L.A.; Jencks, W.P.
Modification and inactivation of CoA transferase by 2-nitro-5-(thiocyanato)benzoate
Biochemistry
20
5183-5187
1981
Sus scrofa
Manually annotated by BRENDA team
Lin, T.; Bridger, W.A.
Sequence of a cDNA clone encoding pig heart mitochondrial CoA transferase
J. Biol. Chem.
267
975-978
1992
Sus scrofa
Manually annotated by BRENDA team
Sharp, J.A.; Edwards, M.R.
Purification and properties of succinyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney
Biochem. J.
173
759-765
1978
Ovis aries, Sus scrofa
Manually annotated by BRENDA team
Lloyd, A.J.; Shoolingin-Jordan, P.M.
dimeric pig heart succinate-coenzyme A transferase zses only one subunit to support catalysis
Biochemistry
40
2455-2467
2001
Sus scrofa
Manually annotated by BRENDA team
Rochet, J.C.; Bridger, W.A.
Identification of glutamate 344 as the catalytic residue in the active site of pig heart CoA transferase
Protein Sci.
3
975-981
1994
Sus scrofa
Manually annotated by BRENDA team
Rochet, J.C.; Brownie, E.R.; Oikawa, K.; Hicks, L.D.; Fraser, M.E.; James, M.N.; Kay, C.M.; Bridger, W.A.; Wolodko, W.T.
Pig heart CoA transferase exists as two oligomeric forms separated by a large kinetic barrier
Biochemistry
39
11291-11302
2000
Sus scrofa
Manually annotated by BRENDA team
Rochet, J.C.; Oikawa, K.; Hicks, L.D.; Kay, C.M.; Bridger, W.A.; Wolodko, W.T.
Productive interactions between the two domains of pig heart CoA transferase during folding and assembly
Biochemistry
36
8807-8820
1997
Sus scrofa
Manually annotated by BRENDA team
Whitty, A.; Fierke, C.A.; Jencks, W.P.
Role of binding energy with coenzyme A in catalysis by 3-oxoacid coenzyme A transferase
Biochemistry
34
11678-11689
1995
Sus scrofa
Manually annotated by BRENDA team
Coros, A.M.; Swenson, L.; Wolodko, W.T.; Fraser, M.E.
Structure of the CoA transferase from pig heart to 1.7 A resolution
ACTA CRYSTALLOGR. SECT. D
60
1717-1725
2004
Sus scrofa
Manually annotated by BRENDA team
Tammam, S.D.; Rochet, J.C.; Fraser, M.E.
Identification of the cysteine residue exposed by the conformational change in pig heart succinyl-CoA:3-ketoacid coenzyme A transferase on binding coenzyme A
Biochemistry
46
10852-10863
2007
Sus scrofa, Sus scrofa (Q29551)
Manually annotated by BRENDA team
Coker, S.F.; Lloyd, A.J.; Mitchell, E.; Lewis, G.R.; Coker, A.R.; Shoolingin-Jordan, P.M.
The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase
Acta Crystallogr. Sect. D
66
797-805
2010
Sus scrofa (Q29551), Sus scrofa
Manually annotated by BRENDA team
Fraser, M.E.; Hayakawa, K.; Brown, W.D.
Catalytic role of the conformational change in succinyl-CoA:3-oxoacid CoA transferase on binding CoA
Biochemistry
49
10319-10328
2010
Sus scrofa (Q29551), Sus scrofa
Manually annotated by BRENDA team