Information on EC 2.8.3.5 - 3-oxoacid CoA-transferase

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

EC NUMBER
COMMENTARY hide
2.8.3.5
-
RECOMMENDED NAME
GeneOntology No.
3-oxoacid 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
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
-
-
citric acid cycle
-
-
ketolysis
-
-
Synthesis and degradation of ketone bodies
-
-
TCA cycle VIII (helicobacter)
-
-
Valine, leucine and isoleucine degradation
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes scoA and scoB encode subunits of the heteromeric enzyme ScoAB
-
-
Manually annotated by BRENDA team
herring
-
-
Manually annotated by BRENDA team
domestic pigeon
-
-
Manually annotated by BRENDA team
bass
-
-
Manually annotated by BRENDA team
domestic fowl
-
-
Manually annotated by BRENDA team
strain 69A
-
-
Manually annotated by BRENDA team
strain 69A
-
-
Manually annotated by BRENDA team
green lizard
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
plaice
-
-
Manually annotated by BRENDA team
ray
-
-
Manually annotated by BRENDA team
mackerel
-
-
Manually annotated by BRENDA team
dogfish
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
-
low enzyme expression is correlated with diabetis type 2
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 + 3-hydroxybutyrate
succinate + 3-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
show the reaction diagram
succinyl-CoA + acetoacetate
?
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
succinyl-CoA + maleate
succinate + maleyl-CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
succinyl-CoA + 3-hydroxybutyrate
succinate + 3-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
show the reaction diagram
succinyl-CoA + acetoacetate
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
succinyl-CoA
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
Mg2+
-
-
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2-Difluorosuccinate
-
strong
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
3-Sulfopropanoate
-
-
4-nitrophenylacetate
-
at pH 7.9, less inactivating activity at pH 7
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
Acetic anhydride
-
-
acetoacetate
acetoacetyl-CoA
acetylene dicarboxylate
-
weak
Acetylimidazole
-
equally efficient at pH 7 and 7.9
ADP
-
-
Blue MY-2G
-
-
-
Br-
-
same inhibition as I-, stronger inhibition than Cl-, the kind of cation has no inhibitory effect
citrate
-
0.167 M, weak
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
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
F-
-
lowest inhibition, the kind of cation has no inhibitory effect
Glutarate
-
0.1 M, weak
HPO42-
-
0.1 M, weak
I-
-
lower inhibition than ClO4-, same inhibition as Br-, the kind of cation has no inhibitory effect
iodoacetamide
-
2.5fold increase at 2 mM
malate
-
0.1 M, weak
Maleamate
-
reversible, competitive
Maleimide
-
succinate or acetoacetate protects
malonate
Monomethylsuccinate
-
competitive
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
N-ethylmaleamate
-
reversible, competitive
N-ethylmaleimide
-
succinate or acetoacetate protects
NaCl
-
kinetics, 24% inhibition at 10 mM
NaI
-
57% inhibition at 10 mM
oxalate
-
kinetics
pantothenol
-
-
Perfluorosuccinate
-
strong
SO42-
-
0.1 M, weak
Sodium borohydride
-
5 mM
streptozotocin
-
in vivo catalytic activity decreases after 4 and 8 weeks of treatment with streptozotocin
succinamate
-
competitive
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
0.0002 - 0.44
acetoacetate
0.006 - 0.72
acetoacetyl-CoA
35
Maleate
-
cosusbstrate: acetoacetyl-CoA, pH 8.1, 25C
0.025 - 39
succinate
0.156 - 8
succinyl-CoA
additional information
additional information
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
Sus scrofa
-
pH 8.1
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.4
2,2-Difluorosuccinate
-
pH 8.1, 25C
0.78 - 3.7
acetoacetate
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
21
malonate
-
pH 8.1, 25C
15
oxalate
-
pH 8.1, 25C
120
pantothenol
-
pH 8.1, 25
18
Perfluorosuccinate
-
pH 8.1, 25C
0.72 - 1
succinate
1.9
succinyl-CoA
-
pH 8.1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
-
diabetic pancreatic islets
0.0005
-
fibroblast extract, patient with enzyme deficiency
0.0038
-
nondiabetic pancreatic islets
3.9 - 4.5
-
-
6
-
C28A mutant, similar to C28S mutant
7.1
-
C28S mutant, 3.6times lower than wild-type enzyme; purified recombinant mutant C28S
10.9
-
heart
15.6
-
brain
19.5
-
skeletal muscle
22.4
-
C196S mutant; purified recombinant mutant C196S
24.1
-
kidney
25.2
-
purified recombinant wild-type enzyme; wild-type SCOT
145
-
-
180
-
-
200
-
-
225.8
-
-
280
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
8
-
assay at
8 - 8.7
-
-
8.1
-
assay at
8.1 - 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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
100% SCOT activity of wild-type enzyme
30
-
59.7% residual SCOT activity of R268H mutant enzyme
37
-
34% residual SCOT activity of R268H mutant enzyme
40
-
4% residual SCOT activity of R268H mutant enzyme, the R268H mutant protein has temperature-sensitive instability and dramatically reduces residual SCOT activity to 4% wild-type in 40C expression so that the R268H mutation is a disease-causing mutation in GS10 and GS11 a SCOT-deficient sibling case from South Africa
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
6.3 - 6.8
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, brain enzyme
6.5
-
4 isozymes with pI: 5.7, 5.9, 6.2 and 6.5
6.8
-
heart enzyme, pH gradient 7-9
7
-
isoelectric focusing; isoelectric focusing
7.6
-
kidney, brain, muscle and liver enzyme, pH gradient 7-9
8.2
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, heart enzyme
8.4
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, purified kidney enzyme
8.7
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, purified kidney enzyme
9
-
pH gradient pH 3.5-10 or pH 7-10 in glycerol gradient, enzyme in kidney extract
9.24
calculated from nucleotide sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
glioma C6 cell line
Manually annotated by BRENDA team
H1e human hepatoma cell line, but no detection in normal hepatocytes, HepG2 hepatoma cells and liver tissues
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
duodenum, jejunum, ileum, caecum, colon, muscle
Manually annotated by BRENDA team
-
neuroblastoma N2a cell line
Manually annotated by BRENDA team
-
decreased expression of SCOT protein, neuroblastoma cells are unable to use ketone bodies as an energy source
Manually annotated by BRENDA team
-
decreased expression of SCOT protein, neuroblastoma cells are unable to use ketone bodies as an energy source
Manually annotated by BRENDA team
midpiece of ejaculated spermatozoa where mitochondria exist
Manually annotated by BRENDA team
-
glandular mucosa
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular distribution
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52200
-
calculated from nucleotide sequence
53200
-
C-terminal domain, sedimentation equilibrium experiments; N-terminal domain, sedimentation equilibrium experiments
55000
-
two species with molecular masses close to 55000 Da, both species are enzymatically active, SDS-PAGE
56530
calculated from nucleotide sequence
58000
-
subunits 2 * 58000, SDS-PAGE, immunostaining and Coomassie Blue
80000
-
gel filtration
90000
-
gel filtration
92000
-
sedimentation equilibrium centrifugation
100000
-
gel filtration
101000
-
dimeric form, sedimentation equilibrium experiments
102000
-
analytical ultracentrifugation
105000
-
SDS-PAGE after cross-linking with dimethyl dodecanediimidate
110000
-
gel filtration
113000
-
gel filtration
120000
218000
-
tetrameric form, sedimentation equilibrium experiments
915000
-
sedimentation equilibrium experiments
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
tetramer
additional information
-
ScoAB subunits, separately expressed and mixed, do not interact effectively resulting in an inactive protein, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
contains galactose, glucose, total sugar content: 1.6%
proteolytic modification
-
SCOT autolytic fragmentation, autocatalytic cleavage of the protein at its active site, glutamate 303, under specific conditions
side-chain modification
-
structural modification, involving the addition of nitro and hydroxy groups to tryptophan, of the mitochondrial protein, mass spectrometric analysis, overview
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant ScoA and ScoB, sitting drop vapour diffusion method, 69 mg/ml protein in 20 mM Hepes, pH 8.0, 200 mM NaCl and 1 mM DTT, mixing with reservoir solution containing 100 mM Tris, pH 8.5, 200 mM MgCl2, and 20% PEG 8000, at 16C, X-ray diffraction structure determination and analysis at 2.89 A resolution
-
14C, hanging drop vapor diffusion, structure determination with X-ray crystallography; 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
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.1
-
below, 1 min at 25C, inactivation
645967
5
-
slow loss of activity at 25C
645967
10.7
-
slow loss of activity at 25C
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
42
-
incubation of wild type at 42C for 10 min does not affect enzyme activity, incubation of mutant T435N at 42C for 10 min reduces enzyme activity to 50%
55
-
incubation of wild type at 55C for 10 min reduces enzyme activity to 20%, incubation of T435N at 55C results in more rapid inactivation of enzyme activity (below 10% in a 4-min incubation)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
An analysis of the three-dimensional structure of SCOT shows that the R268H mutation is expected to break a conserved salt bridge between R268 and D52, which would be expected to lead to decreased stability of the protein.
-
degradation of 3-oxo acid CoA-transferase in glioma and neuroblastoma cells
deoxycholate does not stabilize
-
enzyme is only soluble under denaturating conditions
-
enzyme is susceptible to proteolytic cleavage to produce a nicked but active enzyme, PMSF and EDTA protect
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1.4 mg protein/ml, 0.02 M potassium phosphate buffer, pH 7.4, t1/2: 9 months
-
-20C, at least 1 month
frozen, less than 10% loss of activity within 2 months
-
frozen, partially purified preparation in phosphate solution, less than 10% loss of activity within 1-2 weeks
-
storage as ammonium sulfate suspension leads to rapid loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 isozymes, separable by isoelectric focusing
-
as described in literature; recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) to homogeneity
-
BioSep-SEC-S 3000 gel filtration; native enzyme from mitochondria by chromatofocusing and gel filtration to over 75% purity
-
gel filtration
-
homogeneity
-
N-terminal and C-terminal domain, a mixture of the domains is only active when domains are isolated in the presence of 2-mercaptoethanol
-
native enzyme from mitochondria by chromatofocusing and gel filtration to over 85% purity
-
Ni-NTA agarose column chromatography and Ultrogel AcA 44 column chromatography
-
partial
recombinant ScoA and ScoB by metal affinity chromatography and gel filtration
-
two subunits A and B, both subunits are necessary for enzyme activity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA clone of mature mitochondrial and cytoplasmic precursor to mitochondrial enzyme
-
cDNA from patient with SCOT deficiency
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in INS-1832/13 cells
-
expressed in SCOT-deficient fibroblasts of GS01
-
expression in Escherichia coli BL21-DE3; expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression in SCOT-deficient SV 40-transformed fibroblasts
-
gene SCOT, DNA and amino acid sequence determination and analysis, mutant sequence analysis, overview
-
genes scoA and scoB, encoding subunits of the heteromeric enzyme ScoAB, separate expression of the ScoAB subunits His-tagged ScoA and S-tagged ScoB
-
N-terminal and C-terminal domain
-
two subunits A and B, both subunits are necessary for enzyme activity
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
between 4 and 24 months of age, the amount of the enzyme protein and catalytic activity decrease by 55% and 45%, respectively
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A215V
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains 3.5% residual activity
E273X
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
L327P
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains 4.7% residual activity
R268H
-
DNA mutation in a south african human with SCOT deficiency, detected in fibroblasts
R468C
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains 12% and 51% of wild type residual activities at 37 and 30C, respectively
S226N
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency showing no residual activity
S405P
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains no residual activity
T435N
-
retains significant residual SCOT activities
T58M
-
missense mutation derived from a SCOT-deficient patient, enzyme is functional
V404F
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains some residual activity
C129S
-
like wild-type SCOT rapid modification in the presence of acyl-CoA substrates
C196S
-
site-directed mutagenesis, the mutant protein is modified rapidly in the presence of acyl-CoA substrates in analogy to the wild-type enzyme; specific activity similar to wild-type SCOT
C28A
-
specific activity similar to C28S mutant
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; 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
DELTA249-254
-
delta-SCOT, deletion mutant, residues 249-254 are removed
additional information
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
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