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Human Polyclonal OXCT1 Primary Antibody für ICC, IF - ABIN4342095
Chang, Olson, Schwartz: Ketolytic and glycolytic enzymatic expression profiles in malignant gliomas: implication for ketogenic diet therapy. in Nutrition & metabolism 2013
Crystal structure of human SCOT, providing a molecular understanding of the reported mutations based on their potential structural effects.
Case Report: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency causes episodic ketoacidotic crises and no apparent symptoms between them.
Data show that the ketone body metabolizing enzymes BDH1 (zeige BDH1 Antikörper), BDH2 (zeige BDH2 Antikörper), OXCT1 and ACAT1 (zeige ACAT1 Antikörper) were expressed at the mRNA and protein level in all glioma cell lines.
Missense Mutations in succinyl-CoA:3-ketoacid CoA transferase is associated with Ketoacidosis.
Results demonstrate that h-Scot-t (zeige OXCT2 Antikörper) is a single intronless gene specifically expressed in the testis.
In SCOT-deficient patients retaining some residual activity, permanent ketosis may be absent.
A 6-bp deletion at the splice donor site of intron 1 resulted in the absence of a full-length mature SCOT mRNA with faint amounts of aberrantly spliced transcripts using a cryptic splice donor site within exon 1.
liver-specific silencing of the SCOT gene expression may be mediated in part by its 5'-flanking sequence
The activities of pyruvate carboxylase (zeige PC Antikörper) (SCOT) were decreased by 65% in pancreatic islets of patients with type 2 diabetes.
mechanism of SCOT catalysis
Structure of the CoA transferase from pig heart to 1.7 A resolution
On the basis of these results the conformational change in SCOT was deduced to be a domain rotation of 17 degrees coupled with movement of two loops: res. 321-329 that interact with succinate or acetoacetate and res. 374-386 that interact with CoA.
These results suggest that MT prevention of diabetes-induced pathological changes in cardiac tissues is most likely mediated by suppression of SCOT nitration at Trp (zeige TYRP1 Antikörper)(374).
Data suggest that to sustain survival and euglycemia during moderate-duration starvation, ketone body oxidation via Oxct1 is not required for energy transfer in three cell types: neurons, skeletal myocytes, and cardiomyocytes.
Although Oxct1(-/-) mice exhibit normal prenatal development, all develop ketoacidosis, hypoglycemia, and reduced plasma lactate concentrations within the first 48 h of birth
This gene encodes a member of the 3-oxoacid CoA-transferase gene family. The encoded protein is a homodimeric mitochondrial matrix enzyme that plays a central role in extrahepatic ketone body catabolism by catalyzing the reversible transfer of coenzyme A from succinyl-CoA to acetoacetate. Mutations in this gene are associated with succinyl CoA:3-oxoacid CoA transferase deficiency.
3-oxoacid CoA transferase 1
, succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
, succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial-like
, 3-oxoacid CoA-transferase 1
, 3-oxoacid-CoA transferase 1
, somatic-type succinyl CoA:3-oxoacid CoA-transferase
, somatic-type succinyl-CoA:3-oxoacid CoA-transferase
, somatic-type succinyl-CoA:3-oxoacid-CoA-transferase
, succinyl CoA:3-oxoacid CoA transferase
, succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
, succinyl-CoA:3-ketoacid-CoA transferase
, succinyl-CoA:alpha-ketoacid coenzyme A transferase
, succinyl-CoA:3-ketoacid CoA transferase