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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(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
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, BDH2, OXCT1 and ACAT1 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.
This protein has been found differentially expressed in the anterior cingulate cortex from patients with schizophrenia
Results demonstrate that h-Scot-t 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.
the R268H mutation is a ketoacidosis-causing one
liver-specific silencing of the SCOT gene expression may be mediated in part by its 5'-flanking sequence
The activities of pyruvate carboxylase (SCOT) were decreased by 65% in pancreatic islets of patients with type 2 diabetes.
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
, 3-oxoacid-CoA transferase 1
, somatic-type succinyl CoA:3-oxoacid CoA-transferase
, somatic-type succinyl-CoA:3-oxoacid CoA-transferase
, succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
, succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
, succinyl-CoA:alpha-ketoacid coenzyme A transferase
, 3-oxoacid CoA transferase 1
, succinyl-CoA:3-ketoacid CoA transferase
, somatic-type succinyl-CoA:3-oxoacid-CoA-transferase
, succinyl CoA:3-oxoacid CoA transferase
, succinyl-CoA:3-ketoacid-CoA transferase
, succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial-like