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3-oxoacid CoA transferase 1

3-oxoacid CoA-transferase, in 3-oxoacid CoA-transferase, SCOT-s, 2610008O03Rik
Top mentioned proteins: ACID, HAD, Hexokinase, CAN, FasT
Papers on 3-oxoacid CoA-transferase
Obligate role for ketone body oxidation in neonatal metabolic homeostasis.
Crawford et al., Saint Louis, United States. In J Biol Chem, 2011
Although Oxct1(-/-) mice exhibit normal prenatal development, all develop ketoacidosis, hypoglycemia, and reduced plasma lactate concentrations within the first 48 h of birth
The nitrated proteome in heart mitochondria of the db/db mouse model: characterization of nitrated tyrosine residues in SCOT.
Liu et al., Beijing, China. In J Proteome Res, 2010
Of the nitrated proteins, succinyl-CoA:3-oxoacid CoA-transferase (SCOT) is a key enzyme involved in ketolysis and has yet to be explored how its catalysis is affected by nitration.
Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum.
Messerschmidt et al., Martinsried, Germany. In Biol Chem, 2009
This site is also responsible for binding the acetyl group of acetyl-CoA or the succinyl group of succinyl-CoA in succinyl-CoA:3-oxoacid CoA-transferase from mammalian mitochondria.
Ketone body utilization is regulated by male-specific factors in rat subcutaneous adipocytes.
Fukui et al., Tokyo, Japan. In Exp Clin Endocrinol Diabetes, 2009
In contrast, expression of the other ketone body utilizing enzyme, succinyl-CoA: 3-oxoacid CoA-transferase (SCOT), did not change.
Genetic obesity affects neural ketone body utilization in the rat brain.
Fukui et al., Tokyo, Japan. In Obesity (silver Spring), 2009
Succinyl-CoA:3-oxoacid CoA-transferase (SCOT) mRNA level was decreased only in the PVT but not affected in the Arc and VMH.
Tamoxifen induces oxidative stress and mitochondrial apoptosis via stimulating mitochondrial nitric oxide synthase.
Ghafourifar et al., Columbus, United States. In Cancer Res, 2007
By stimulating mtNOS, tamoxifen hampers mitochondrial respiration, releases cytochrome c, elevates mitochondrial lipid peroxidation, increases protein tyrosine nitration of certain mitochondrial proteins, decreases the catalytic activity of succinyl-CoA:3-oxoacid CoA-transferase, and induces aggregation of mitochondria.
Transposon-mediated gene trapping in zebrafish.
Kawakami et al., Mishima, Japan. In Methods, 2006
In the SAGm18B line, GFP is expressed in the central nervous system, and the insertion captured a transcript of a gene for succinyl CoA:3-oxoacid CoA-transferase (SCOT).
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.
Fukui et al., Tokyo, Japan. In Biochim Biophys Acta, 2005
High labeling was observed in the midbrain, pons/medulla, cerebral cortex, hippocampus and cerebellum, and the localization profile of AACS mRNA was different from that of succinyl-CoA:3-oxoacid CoA-transferase (SCOT), a mitochondrial ketone body-activating enzyme.
Effect of enteral nutrition of monoacetoacetin on bacterial translocation in burned rats.
Hirakawa et al., Ōsaka, Japan. In Jpen J Parenter Enteral Nutr, 2004
To confirm the effectiveness of MA in the small intestine, we estimated succinyl-CoA:3-oxoacid CoA-transferase (SCOT) expression in the terminal ileum by immunohistochemical staining and Western blot analysis.
Growth-inhibitory effects of the ketone body, monoacetoacetin, on human gastric cancer cells with succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency.
Hirakawa et al., Ōsaka, Japan. In Anticancer Res, 2004
Succinyl-CoA: 3-oxoacid CoA transferase (SCOT) is a key enzyme in the metabolism of MAA.
Altered expression of hypothetical proteins in hippocampus of transgenic mice overexpressing human Cu/Zn-superoxide dismutase 1.
Lubec et al., Vienna, Austria. In Proteome Sci, 2004
Of these, expression levels of 2610008O03Rik protein (Q9D0K2) and 4632432E04Rik protein (Q9D358) were significantly decreased (P < 0.05 and 0.001) and hypothetical protein (Q99KP6) was significantly increased (P < 0.05) in hippocampus of SOD1-TGs as compared with non-transgenic mice.
Differential expression of succinyl CoA transferase (SCOT) genes in somatic and germline cells of the mouse testis.
Nishimune et al., Suita, Japan. In Int J Androl, 2003
We then isolated a mouse orthologue of the SCOT/OXCT cDNA (SCOT-s) and determined the expression of the two types of SCOT in the testis.
Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase.
Murad et al., Houston, United States. In Am J Physiol Heart Circ Physiol, 2001
In the present study, we have demonstrated that succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC is susceptible to tyrosine nitration in hearts from streptozotocin-treated rats.
Neonatal hypoglycaemia in severe succinyl-CoA: 3-oxoacid CoA-transferase deficiency.
Palmieri et al., Philadelphia, United States. In J Inherit Metab Dis, 2001
Succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency is an inborn error of ketone body utilization, characterized by intermittent ketoacidotic crises and persistent ketosis.
Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration.
Murad et al., Houston, United States. In Proc Natl Acad Sci U S A, 2001
The 52-kDa protein was purified and identified with partial sequence as succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC ).
Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases.
Messerschmidt et al., Martinsried, Germany. In Structure, 1997
A defect in the human gene encoding succinyl-CoA: 3-oxoacid CoA-transferase causes a metabolic disease which leads to severe ketoacidosis, thus reflecting the importance of this family of enzymes.
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