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succinyl-CoA + 3-hydroxybutyrate
succinate + 3-hydroxybutyryl-CoA
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
succinyl-CoA + acetoacetate
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
succinyl-CoA + maleate
succinate + maleyl-CoA
-
-
-
-
?
additional information
?
-
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
r
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
ketone bodies, produced mainly in the liver, are an important source of energy for extrahepatic tissues
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
rate determining step of ketolysis in extrahepatic tissues
-
-
?
succinyl-CoA + acetoacetate
?
-
enzyme deficiency leads to ketoacidotic crises and persistent ketosis
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
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
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
key enzyme in ketone body metabolism
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
key enzyme for ketone body utilization, SCOT deficiency causes episodes of severe ketoacidosis
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
the activation of acetoacetate to acetoacetyl-CoA by SCOT is essential for use of ketone bodies as an energy source
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
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
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
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
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
via enzyme-coenzyme A covalent complex
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
ping-pong mechanism
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
SCOT transfers CoA from succinyl-CoA to acetoacetate via a thioester intermediate with its active site glutamate residue Glu305
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
essential enzyme in the metabolism of ketone bodies in higher animals, reaction via an enzyme-thioester intermediate
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
proposal of a new mechanism for catalysis by SCOT, the experiments contrasting the labeling of the C28S and C196S mutant proteins and wild-type SCOT clearly show that Cys 28 is the cysteine residue exposed on binding CoA in the enzyme-thioester intermediate
-
-
r
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
-
-
-
-
?
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
essential enzyme in the metabolism of ketone bodies in higher animals
-
-
?
additional information
?
-
-
no substrates are diacids with connecting chain lengths of 3 or more methylene groups
-
-
?
additional information
?
-
-
catalyzes exchange reactions in the absence of cosubstrates: succinate/succinyl-CoA and acetoacetate/acetoacetyl-CoA
-
-
?
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succinyl-CoA + 3-hydroxybutyrate
succinate + 3-hydroxybutyryl-CoA
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
succinyl-CoA + acetoacetate
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
r
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
ketone bodies, produced mainly in the liver, are an important source of energy for extrahepatic tissues
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
-
?
succinyl-CoA + a 3-oxo acid
succinate + a 3-oxoacyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
rate determining step of ketolysis in extrahepatic tissues
-
-
?
succinyl-CoA + acetoacetate
?
-
enzyme deficiency leads to ketoacidotic crises and persistent ketosis
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
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
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
liver enzyme: produces a substrate circle between acetoacetyl-CoA and acetoacetate
-
-
?
succinyl-CoA + acetoacetate
?
-
key enzyme in ketone body metabolism
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
key enzyme for ketone body utilization, SCOT deficiency causes episodes of severe ketoacidosis
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
the activation of acetoacetate to acetoacetyl-CoA by SCOT is essential for use of ketone bodies as an energy source
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
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
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
r
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
-
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
ping-pong mechanism
-
-
?
succinyl-CoA + acetoacetate
succinate + acetoacetyl-CoA
essential enzyme in the metabolism of ketone bodies in higher animals, reaction via an enzyme-thioester intermediate
-
-
r
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
-
-
-
-
?
succinyl-CoA + beta-hydroxybutyrate
succinate + beta-hydroxybutyryl-CoA
essential enzyme in the metabolism of ketone bodies in higher animals
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
acetylene dicarboxylate
-
weak
Acetylimidazole
-
equally efficient at pH 7 and 7.9
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
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
I-
lower inhibition than ClO4-, same inhibition as Br-, the kind of cation has no inhibitory effect
iodoacetamide
-
2.5fold increase at 2 mM
Maleamate
-
reversible, competitive
Maleimide
-
succinate or acetoacetate protects
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
Perfluorosuccinate
-
strong
Sodium borohydride
-
5 mM
streptozotocin
-
in vivo catalytic activity decreases after 4 and 8 weeks of treatment with streptozotocin
succinamate
-
competitive
acetoacetate
-
substrate inhibition above 1 mM
acetoacetate
-
kinetics; product inhibition
acetoacetate
product inhibition
acetoacetyl-CoA
-
product inhibition, kinetics
acetoacetyl-CoA
-
EDTA, trisodium citrate and diphosphate protect, too, addition of Cu2+, Mn2+, Ca2+ or Zn2+ (decreasing order) restores inactivating activity of acetoacetyl-CoA; in the absence of succinate, cysteine restores, succinate or 0.1 M NaCl protects
malonate
-
kinetics
SCN-
-
47% inhibition at 10 mM
SCN-
strongest inhibition, the kind of cation has no inhibitory effect
succinate
-
kinetics; product inhibition
succinate
-
product inhibition
succinate
-
kinetics; product inhibition
succinyl-CoA
-
product inhibition
succinyl-CoA
product inhibition
additional information
the DNA region between -2168 and -361 appears to inhibit the SCOT promoter activity in HepG2 cells
-
additional information
-
the DNA region between -2168 and -361 appears to inhibit the SCOT promoter activity in HepG2 cells
-
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
-
additional information
-
the DNA region between -2168 and -361 appears to inhibit the SCOT promoter activity in HepG2 cells
-
additional information
the DNA region between -2168 and -361 appears to inhibit the SCOT promoter activity in HepG2 cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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3-oxoacid coa-transferase deficiency
A Case of Succinyl-CoA:3-Oxoacid CoA Transferase Deficiency Presenting with Severe Acidosis in a 14-Month-Old Female: Evidence for Pathogenicity of a Point Mutation in the OXCT1 Gene.
3-oxoacid coa-transferase deficiency
A new Japanese case of succinyl-CoA: 3-ketoacid CoA-transferase deficiency.
3-oxoacid coa-transferase deficiency
A Rare Cause of Life-Threatening Ketoacidosis: Novel Compound Heterozygous OXCT1 Mutations Causing Succinyl-CoA:3-Ketoacid CoA Transferase Deficiency.
3-oxoacid coa-transferase deficiency
Heterozygous carriers of succinyl-CoA:3-oxoacid CoA transferase deficiency can develop severe ketoacidosis.
3-oxoacid coa-transferase deficiency
Management and communication problems in a patient with succinyl-CoA transferase deficiency in pregnancy and labour.
3-oxoacid coa-transferase deficiency
Neonatal hypoglycaemia in severe succinyl-CoA: 3-oxoacid CoA-transferase deficiency.
3-oxoacid coa-transferase deficiency
Rare cause of high anion gap metabolic acidosis in an infant: Succinyl-CoA:3-ketoacid transferase deficiency.
3-oxoacid coa-transferase deficiency
Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.
3-oxoacid coa-transferase deficiency
Succinyl-CoA: 3-ketoacid CoA-transferase deficiency. A cause for ketoacidosis in infancy.
3-oxoacid coa-transferase deficiency
Succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) deficiency: A rare and potentially fatal metabolic disease.
3-oxoacid coa-transferase deficiency
[Succinyl-CoA: 3-ketoacid CoA transferase deficiency]
acetyl-coa c-acetyltransferase deficiency
Influence of ketone bodies on oxidative stress parameters in brain of developing rats in vitro.
Acidosis
A Case of Succinyl-CoA:3-Oxoacid CoA Transferase Deficiency Presenting with Severe Acidosis in a 14-Month-Old Female: Evidence for Pathogenicity of a Point Mutation in the OXCT1 Gene.
Acidosis
Rare cause of high anion gap metabolic acidosis in an infant: Succinyl-CoA:3-ketoacid transferase deficiency.
Acidosis
Successful Management of Pregnancies in Patients with Inherited Disorders of Ketone Body Metabolism.
Brain Neoplasms
The calorically restricted ketogenic diet, an effective alternative therapy for malignant brain cancer.
Breast Neoplasms
?-hydroxybutyrate does not alter the effects of glucose deprivation on breast cancer cells.
Breast Neoplasms
Mitoketoscins: Novel mitochondrial inhibitors for targeting ketone metabolism in cancer stem cells (CSCs).
Carcinogenesis
Mitoketoscins: Novel mitochondrial inhibitors for targeting ketone metabolism in cancer stem cells (CSCs).
Carcinogenesis
The role of OXCT1 in the pathogenesis of cancer as a rate-limiting enzyme of ketone body metabolism.
Carcinoma, Hepatocellular
Acetoacetate coenzyme A transferase activity in rat hepatomas.
Carcinoma, Hepatocellular
Regulation of succinyl coenzyme A:acetoacetyl coenzyme A transferase in rat hepatoma cell lines.
Carcinosarcoma
Failure of systemic ketosis to control cachexia and the growth rate of the Walker 256 carcinosarcoma in rats.
Colitis
Physiological activity of E. coli engineered to produce butyric acid.
Dehydration
Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile.
Diabetes Mellitus
Increased Glucose Availability Attenuates Myocardial Ketone Body Utilization.
Diabetes Mellitus, Experimental
Physical training reverses defect in 3-ketoacid CoA-transferase activity in skeletal muscle of diabetic rats.
Diabetes Mellitus, Type 2
Increased Glucose Availability Attenuates Myocardial Ketone Body Utilization.
Diabetes Mellitus, Type 2
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.
Diabetic Ketoacidosis
Ketone body utilization and its metabolic effect in resting muscles of normal and streptozotocin-diabetic rats.
Genetic Diseases, Inborn
A 6-bp deletion at the splice donor site of the first intron resulted in aberrant splicing using a cryptic splice site within exon 1 in a patient with succinyl-CoA: 3-Ketoacid CoA transferase (SCOT) deficiency.
Glioma
Ketone-body metabolism in glioma and neuroblastoma cells.
Glioma
Novel LncRNA OXCT1-AS1 indicates poor prognosis and contributes to tumorigenesis by regulating miR-195/CDC25A axis in glioblastoma.
Glioma
Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells.
glycoprotein-fucosylgalactoside alpha-n-acetylgalactosaminyltransferase deficiency
Succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) deficiency: A rare and potentially fatal metabolic disease.
Heart Failure
Increased Glucose Availability Attenuates Myocardial Ketone Body Utilization.
Hyperthyroidism
Differential action of thyroid hormones on the activity of certain enzymes in rat kidney and brain.
Hyperthyroidism
Ketone-body metabolism in hyperthyroid rats: reduced activity of D-3-hydroxybutyrate dehydrogenase in both liver and heart and of succinyl-coenzyme A: 3-oxoacid coenzyme A-transferase in heart.
Hypoglycemia
Impact of peripheral ketolytic deficiency on hepatic ketogenesis and gluconeogenesis during the transition to birth.
Hypoglycemia
Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.
Hypoglycemia
Successful Management of Pregnancies in Patients with Inherited Disorders of Ketone Body Metabolism.
Infertility, Male
Ketone bodies could support the motility but not the acrosome reaction of mouse sperm.
Insulinoma
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.
Ketosis
A Rare Cause of Life-Threatening Ketoacidosis: Novel Compound Heterozygous OXCT1 Mutations Causing Succinyl-CoA:3-Ketoacid CoA Transferase Deficiency.
Ketosis
A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency.
Ketosis
Clinical and molecular characterization of five patients with succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency.
Ketosis
Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases.
Ketosis
Heterozygous carriers of succinyl-CoA:3-oxoacid CoA transferase deficiency can develop severe ketoacidosis.
Ketosis
Identification and characterization of a temperature-sensitive R268H mutation in the human succinyl-CoA:3-ketoacid CoA transferase (SCOT) gene.
Ketosis
Inborn errors of ketone body utilization.
Ketosis
Management and communication problems in a patient with succinyl-CoA transferase deficiency in pregnancy and labour.
Ketosis
Neonatal hypoglycaemia in severe succinyl-CoA: 3-oxoacid CoA-transferase deficiency.
Ketosis
Patients homozygous for the T435N mutation of succinyl-CoA:3-ketoacid CoA Transferase (SCOT) do not show permanent ketosis.
Ketosis
Structure of the mammalian CoA transferase from pig heart.
Ketosis
Succinyl-CoA: 3-ketoacid CoA-transferase deficiency. A cause for ketoacidosis in infancy.
Liver Neoplasms, Experimental
Subcellular localization of acetoacetate coenzyme A transferase in rat hepatomas.
Lymphoma
Signalling pathways identified in salivary glands from primary Sjögren's syndrome patients reveal enhanced adipose tissue development.
Metabolic Diseases
Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases.
Metabolic Diseases
Succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) deficiency: A rare and potentially fatal metabolic disease.
Neoplasm Metastasis
Mitoketoscins: Novel mitochondrial inhibitors for targeting ketone metabolism in cancer stem cells (CSCs).
Neoplasms
Acetoacetate coenzyme A transferase activity in rat hepatomas.
Neoplasms
Low ketolytic enzyme levels in tumors predict ketogenic diet responses in cancer cell lines in vitro and in vivo.
Neoplasms
Metabolic substrate utilization by a tumour cell line which induces cachexia in vivo.
Neoplasms
Role of acetoacetyl-CoA synthetase in acetoacetate utilization by tumor cells.
Neoplasms
The calorically restricted ketogenic diet, an effective alternative therapy for malignant brain cancer.
Neoplasms
The role of OXCT1 in the pathogenesis of cancer as a rate-limiting enzyme of ketone body metabolism.
Neoplasms
Treatment of glioma patients with ketogenic diets: report of two cases treated with an IRB-approved energy-restricted ketogenic diet protocol and review of the literature.
Neuroblastoma
Ketone-body metabolism in glioma and neuroblastoma cells.
Neuroblastoma
Turnover of succinyl-CoA:3-oxoacid CoA-transferase in glioma and neuroblastoma cells. Specific influence of acetoacetate in neuroblastoma cells.
Ovarian Neoplasms
3-Oxoacid CoA transferase 1 as a therapeutic target gene for cisplatin-resistant ovarian cancer.
Phenylketonurias
When one disease is not enough: succinyl-CoA: 3-oxoacid coenzyme A transferase (SCOT) deficiency due to a novel mutation in OXCT1 in an infant with known phenylketonuria.
Sleep Deprivation
Ketone body metabolism and sleep homeostasis in mice.
Starvation
Activities of some key enzymes of carbohydrate, ketone body, adenosine and glutamine metabolism in liver, and brown and white adipose tissues of the rat.
Stomach Neoplasms
Growth-inhibitory effects of the ketone body, monoacetoacetin, on human gastric cancer cells with succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency.
Thymoma
[Analysis of Gene Variation in Thymoma by Microarray].
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G219E
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
G324E
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
L429F
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
M388V
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
P262R
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
R217X
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
R268C
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
R38C
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
S283X
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
T58M
-
missense mutation derived from a SCOT-deficient patient, enzyme is functional
V112D
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
V221M
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
C129S
like wild-type SCOT rapid modification in the presence of acyl-CoA substrates
C28A
specific activity similar to C28S mutant
DELTA249-254
-
delta-SCOT, deletion mutant, residues 249-254 are removed
A215V
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
A215V
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains 3.5% residual activity
C456F
-
no activity
C456F
-
missense mutation derived from a SCOT-deficient patient, no enzyme activity
C456F
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
E273X
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
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
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
R268H
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
R468C
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
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 30°C, respectively
S226N
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
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
S405P
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains no residual activity
T435N
-
retains significant residual SCOT activities
T435N
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
V133E
-
no activity
V133E
-
missense mutation derived from a SCOT-deficient patient, no enzyme activity
V133E
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
V404F
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency
V404F
-
the mutation is associated with succinyl-CoA:3-ketoacid CoA transferase deficiency and retains some residual activity
C196S
site-directed mutagenesis, the mutant protein is modified rapidly in the presence of acyl-CoA substrates in analogy to the wild-type enzyme
C196S
specific activity similar to wild-type SCOT
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
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
additional information
-
identification of point mutation leading to enzyme inactivation, and deficiency causing severe ketoacidosis in vivo, some mutations lead to highly reduced mRNA and enzyme levels, overview
additional information
sensitization of cells to cisplatin following overexpression of OXCT1 , overexpression of OXCT1 enhances sensitivity to cisplatin, one of the most effective broad-spectrum anticancer drugs, in the SK-OV-3 OC ovarian cancer cell line. Overexpression of OXCT1 significantly decreases the IC50 for cisplatin by about 21% compared with EGFP-transfected control cells
additional information
-
sensitization of cells to cisplatin following overexpression of OXCT1 , overexpression of OXCT1 enhances sensitivity to cisplatin, one of the most effective broad-spectrum anticancer drugs, in the SK-OV-3 OC ovarian cancer cell line. Overexpression of OXCT1 significantly decreases the IC50 for cisplatin by about 21% compared with EGFP-transfected control cells
additional information
-
mutant with deletion of amino acid residues 249-254 shows no altered kinetic values
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1975
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1981
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1984
Mus musculus, Rattus norvegicus
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13
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1974
Rattus norvegicus
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Ovis aries, Sus scrofa
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Ovis aries
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Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family
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Helicobacter pylori, Helicobacter pylori 69A
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Homo sapiens
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Mus musculus, Mus musculus (Q9JJN4)
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dimeric pig heart succinate-coenzyme A transferase zses only one subunit to support catalysis
Biochemistry
40
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Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration
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Sus scrofa
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Pig heart CoA transferase exists as two oligomeric forms separated by a large kinetic barrier
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Rattus norvegicus
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Patients homozygous for the T435N mutation of succinyl-CoA:3-ketoacid CoA Transferase (SCOT) do not show permanent ketosis
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Homo sapiens
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46
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2007
Sus scrofa, Sus scrofa (Q29551)
brenda
Yamada, K.; Fukao, T.; Zhang, G.; Sakurai, S.; Ruiter, J.P.; Wanders, R.J.; Kondo, N.
Single-base substitution at the last nucleotide of exon 6 (c.671G>A), resulting in the skipping of exon 6, and exons 6 and 7 in human succinyl-CoA:3-ketoacid CoA transferase (SCOT) gene
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Homo sapiens
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Bacillus subtilis
brenda
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
brenda
Fukao, T.; Kursula, P.; Owen, E.P.; Kondo, N.
Identification and characterization of a temperature-sensitive R268H mutation in the human succinyl-CoA:3-ketoacid CoA transferase (SCOT) gene
Mol. Genet. Metab.
92
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2007
Homo sapiens
brenda
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Liver-specific silencing of the human gene encoding succinyl-CoA: 3-ketoacid CoA transferase
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Homo sapiens (P55809), Homo sapiens
brenda
MacDonald, M.J.; Longacre, M.J.; Langberg, E.C.; Tibell, A.; Kendrick, M.A.; Fukao, T.; Ostenson, C.G.
Decreased levels of metabolic enzymes in pancreatic islets of patients with type 2 diabetes
Diabetologia
52
1087-1091
2009
Homo sapiens
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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
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48
609-618
2009
Rattus norvegicus, Rattus norvegicus (B2GV06)
brenda
Skinner, R.; Trujillo, A.; Ma, X.; Beierle, E.
Ketone bodies inhibit the viability of human neuroblastoma cells
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2009
Homo sapiens
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Bregere, C.; Rebrin, I.; Sohal, R.S.
Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins
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441
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2008
Rattus norvegicus
brenda
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
brenda
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
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499
62-68
2010
Rattus norvegicus (B2GV06)
brenda
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
brenda
Fukao, T.; Sass, J.O.; Kursula, P.; Thimm, E.; Wendel, U.; Ficicioglu, C.; Monastiri, K.; Guffon, N.; Bari?, I.; Zabot, M.T.; Kondo, N.
Clinical and molecular characterization of five patients with succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
Biochim. Biophys. Acta
1812
619-624
2011
Homo sapiens
brenda
Zhang, M.; Xu, H.Y.; Wang, Y.C.; Shi, Z.B.; Zhang, N.N.
Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster
Acta Crystallogr. Sect. F
69
1089-1093
2013
Drosophila melanogaster (Q9W058), Drosophila melanogaster
brenda
Cong, W.; Ma, W.; Zhao, T.; Zhu, Z.; Wang, Y.; Tan, Y.; Li, X.; Jin, L.; Cai, L.
Metallothionein prevents diabetes-induced cardiac pathological changes, likely via the inhibition of succinyl-CoA:3-ketoacid coenzyme A transferase-1 nitration at Trp(374)
Am. J. Physiol. Endocrinol. Metab.
304
E826-E835
2013
Mus musculus (Q9D0K2)
brenda
Shafqat, N.; Kavanagh, K.L.; Sass, J.O.; Christensen, E.; Fukao, T.; Lee, W.H.; Oppermann, U.; Yue, W.W.
A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
J. Inherit. Metab. Dis.
36
983-987
2013
Homo sapiens (P55809), Homo sapiens
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Chutoam, P.; Charoensawan, V.; Wongtrakoongate, P.; Kum-Arth, A.; Buphamalai, P.; Tungpradabkul, S.
RpoS and oxidative stress conditions regulate succinyl-CoA: 3-ketoacid-coenzyme A transferase (SCOT) expression in Burkholderia pseudomallei
Microbiol. Immunol.
57
605-615
2013
Burkholderia pseudomallei (Q63TL3), Burkholderia pseudomallei, Burkholderia pseudomallei K96243 (Q63TL3)
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Yang, S.D.; Ahn, S.H.; Kim, J.I.
3-Oxoacid CoA transferase 1 as a therapeutic target gene for cisplatin-resistant ovarian cancer
Oncol. Lett.
15
2611-2618
2018
Homo sapiens (P55809), Homo sapiens
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