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Information on EC 2.8.3.5 - 3-oxoacid CoA-transferase and Organism(s) Rattus norvegicus and UniProt Accession B2GV06
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2.8.3.5 3-oxoacid CoA-transferaseIUBMB 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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Word Map
- 2.8.3.5
- ketone
- acetoacetyl-coa
-
thiolase
- 3-hydroxybutyrate
-
ketolytic
-
ketogenic
- ketosis
- butyryl-coa
-
ketoacidotic
- acetobutylicum
-
butyrate-producing
-
butyryl-coa:acetate
-
ketone-body
- tyrobutyricum
- medicine
-
hydrogenosomes
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, succinyl-coa transferase, scot-t, succinyl-coa:3-oxoacid coa transferase, succinyl-coa:3-oxoacid coa-transferase, succinyl-coa:3-ketoacid coenzyme a transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacid CoA-transferase
3-ketoacid coenzyme A transferase
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-
-
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3-ketoacid coenzyme A-transferase
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-
-
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3-oxo-CoA transferase
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-
-
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3-oxoacid CoA dehydrogenase
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-
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3-oxoacid coenzyme A-transferase
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-
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acetoacetate succinyl-CoA transferase
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-
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acetoacetyl coenzyme A-succinic thiophorase
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-
-
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coenzyme A-transferase, 3-oxoacid
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-
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SCOT
SCOT-t
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-
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succinyl coenzyme A-acetoacetyl coenzyme A-transferase
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-
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succinyl-CoA transferase
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succinyl-CoA:acetoacetate CoA transferase
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-
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testis-specific succinyl-CoA:3-oxo-acid CoA-transferase
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-
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3-ketoacid CoA-transferase
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-
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SCOT
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
coenzyme A transfer
coenzyme A transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
9027-43-4
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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
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
-
-
-
-
?
additional information
?
-
-
no substrates are diacids with connecting chain lengths of 3 or more methylene groups
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-
?
succinyl-CoA + acetoacetate
?
-
ketolytic enzyme, uniquely involved in complete oxidation of ketone bodies
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-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
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-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
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-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
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involved in the breakdown of ketone bodies in the extrahepatic tissues, mainly heart and skeletal muscle, SCOT catalyzes the conversion of the main ketone body, acetoacetate, into acetoacetyl-CoA, which is subsequently metabolized via citric acid cycle for energy production
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-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
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here we report the novel finding that tryptophan 372, located in close vicinity of the enzyme active site, is a specific in vivo target of nitration/oxidation, and that the amount of SCOT nitration and activity increase with age
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-
r
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
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
?
-
ketolytic enzyme, uniquely involved in complete oxidation of ketone bodies
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
involved in the breakdown of ketone bodies in the extrahepatic tissues, mainly heart and skeletal muscle, SCOT catalyzes the conversion of the main ketone body, acetoacetate, into acetoacetyl-CoA, which is subsequently metabolized via citric acid cycle for energy production
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
streptozotocin
-
in vivo catalytic activity decreases after 4 and 8 weeks of treatment with streptozotocin
additional information
-
no inhibition by glutarate, adipate, cis- or trans-cyclobutane-1,2-dicarboxylate, cis- or trans-cyclohexane-1,2-dicarboxylate, methylsuccinate, mercaptosuccinate, malate, aspartate, succinimide or iodoacetamide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
when expressed per gram of gastrocnemius muscle, activity is decreased by 32% in sedentary diabetic rats compared with their sedentary counterparts, physical training increases the activity by 88% in nondiabetic rats and by 148% in diabetic rats, when expressed per total gastrocnemius muscle, activity is decreased by 61% in sedentary diabetic rats compared with their sedentary counterparts, physical training increases the activity by 66% in nondiabetic rats and by 150% in diabetic rats
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
thalamus, hypothalamus and pons, mRNA expression in the subiculum, the pyramidal cell layer of cornus ammonis and the granular cell layer of dentate gyrus, mRNA expression is discretely focussed in a cortex-side layer of Purkinje cells, streptozotocin-induced diabetes does not change the localization profile of SCOT mRNA
age-related decreases in SCOT protein amount and catalytic activity: between 4 and 24 months of age, the amounts of SCOT protein and catalytic activity decrease by 55 and 45%, respectively
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
rat heart mitochondria at 4, 13, 19, and 24 months of age
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
SCOT is a rate-limiting enzyme in the degradation of ketone bodies
physiological function
loss of SCOT protein in the aged rats may attenuate the capacity of kidney mitochondria to utilize ketone bodies for energy production
malfunction
insulinoma cell lines with more than 70% knockdown of enzyme activity shows more than 70% reduction in glucose- or methyl succinate-plus-beta-hydroxybutyrate-stimulated insulin release
malfunction
loss of succinyl-CoA:3-ketoacid CoA transferase protein in aged rats may attenuate the capacity of kidney mitochondria to utilize ketone bodies for energy production
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SCOT1_RAT
520
0
56204
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
58000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
nitrification of tyrosine residues leads to inhibition of enzyme activity in inflammatory conditions
additional information
-
basal nitration only detectable in heart and kidney, nitration in heart occurs after streptozotocin-treatment
additional information
-
the enzyme is a target for nitration, tryptophan 372, rather than a tyrosine residue, is the actual site of simultaneous additions of nitro and hydroxy groups, impact on enzyme activity, mass spectrometric analysis, overview
additional information
the enzyme is a target for nitration, tryptophan 372, rather than a tyrosine residue, is the actual site of simultaneous additions of nitro and hydroxy groups, impact on enzyme activity, mass spectrometric analysis, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
degradation of 3-oxo acid CoA-transferase in glioma and neuroblastoma cells
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen, partially purified preparation in phosphate solution, less than 10% loss of activity within 1-2 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from mitochondria by chromatofocusing and gel filtration to over 75% purity
native enzyme from mitochondria by chromatofocusing and gel filtration to over 85% purity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zammit, V.A.; Beis, A.; Newsholme, E.A.
The role of 3-oxo acid-CoA transferase in the regulation of ketogenesis in the liver
FEBS Lett.
103
212-215
1979
Gallus gallus, Clupea harengus, Columba livia, Oryctolagus cuniculus, Dicentrarchus labrax, Lacerta viridis, Mus musculus, Oncorhynchus mykiss, Pleuronectes platessa, Raja clavata, Rattus norvegicus, Scomber scombrus, Scyliorhinus canicula
Fenselau, A.; Wallis, K.
Comparative studies on 3-oxo acid coenzyme A transferase from various rat tissues
Biochem. J.
142
619-627
1974
Rattus norvegicus
Russell, J.J.; Patel, M.S.
Purification and properties of succinyl-CoA:3-oxo-acid CoA-transferase from rat brain
J. Neurochem.
38
1446-1452
1982
Rattus norvegicus
Fenselau, A.; Wallis, K.
Ketone body usage by mammals. Acetoacetate substrate inhibition of CoA transferase from various rat tissues
Life Sci.
15
811-818
1974
Rattus norvegicus
Fenselau, A.; Wallis, K.
Ping-pong chromatography. A novel purification of CoA-transferase
Biochem. Biophys. Res. Commun.
62
350-356
1975
Rattus norvegicus
Hanson, P.J.; Carrington, J.M.
Activity of 3-oxo acid CoA-transferase, D-3-hydroxybutyrate dehydrogenase, hexokinase and carnitine palmitoyltransferase in the stomach and small and large intestine of the rat
Biochem. J.
200
349-355
1981
Rattus norvegicus
Haney, P.M.; Bolinger, L.; Raefsky, C.; Patel, M.S.
Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells
Biochem. J.
224
67-74
1984
Mus musculus, Rattus norvegicus
Fenselau, A.; Wallis, K.
Substrate specificity and mechanism of action of acetoacetate coenzyme A transferase from rat heart
Biochemistry
13
3884-3889
1974
Rattus norvegicus
Marcondes, S.; Turko, I.V.; Murad, F.
Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration
Proc. Natl. Acad. Sci. USA
98
7146-7151
2001
Rattus norvegicus
Turko, I.V.; Marcondes, S.; Murad, F.
Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase
Am. J. Physiol.
281
H2289-H2294
2001
Rattus norvegicus
El Midaoui, A.; Chiasson, J.L.; Tancrede, G.; Nadeau, A.
Physical training reverses defect in 3-ketoacid CoA-transferase activity in skeletal muscle of diabetic rats
Am. J. Physiol.
288
E748-752
2005
Rattus norvegicus
Ohnuki, M.; Takahashi, N.; Yamasaki, M.; Fukui, T.
Different localization in rat brain of the novel cytosolic ketone body-utilizing enzyme, acetoacetyl-CoA synthetase, as compared to succinyl-CoA:3-oxoacid CoA-transferase
Biochim. Biophys. Acta
1729
147-153
2005
Rattus norvegicus
Rebrin, I.; Bregere, C.; Kamzalov, S.; Gallaher, T.K.; Sohal, R.S.
Nitration of tryptophan 372 in succinyl-CoA:3-ketoacid CoA transferase during aging in rat heart mitochondria
Biochemistry
46
10130-10144
2007
Rattus norvegicus
Bregere, C.; Rebrin, I.; Gallaher, T.K.; Sohal, R.S.
Effects of age and calorie restriction on tryptophan nitration, protein content, and activity of succinyl-CoA:3-ketoacid CoA transferase in rat kidney mitochondria
Free Radic. Biol. Med.
48
609-618
2009
Rattus norvegicus, Rattus norvegicus (B2GV06)
Bregere, C.; Rebrin, I.; Sohal, R.S.
Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins
Methods Enzymol.
441
339-349
2008
Rattus norvegicus
Hasan, N.M.; Longacre, M.J.; Seed Ahmed, M.; Kendrick, M.A.; Gu, H.; Ostenson, C.G.; Fukao, T.; MacDonald, M.J.
Lower succinyl-CoA:3-ketoacid-CoA transferase (SCOT) and ATP citrate lyase in pancreatic islets of a rat model of type 2 diabetes: knockdown of SCOT inhibits insulin release in rat insulinoma cells
Arch. Biochem. Biophys.
499
62-68
2010
Rattus norvegicus (B2GV06)
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