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Literature summary for 2.8.3.5 extracted from
- Identification and characterization of a temperature-sensitive R268H mutation in the human succinyl-CoA:3-ketoacid CoA transferase (SCOT) gene (2007), Mol. Genet. Metab., 92, 216-221.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | Succinyl-CoA:3-ketoacid CoA transferase deficiency causes episodic ketoacidosis | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R268H | DNA mutation in a south african human with SCOT deficiency, detected in fibroblasts | Homo sapiens |
General Stability
| General Stability | Organism |
|---|---|
| An analysis of the three-dimensional structure of SCOT shows that the R268H mutation is expected to break a conserved salt bridge between R268 and D52, which would be expected to lead to decreased stability of the protein. | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | the enzyme is a mitochondrial homodimer | Homo sapiens | 5739 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinyl-CoA + 3-hydroxybutyrate | Homo sapiens | - |
succinate + 3-hydroxybutyryl-CoA | - |
? |  |
| succinyl-CoA + a 3-oxo acid | Homo sapiens | ketone bodies, produced mainly in the liver, are an important source of energy for extrahepatic tissues | succinate + a 3-oxoacyl-CoA | - |
? | |
| succinyl-CoA + acetoacetate | Homo sapiens | - |
succinate + acetoacetyl-CoA | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fibroblast | of mutant enzyme R268H | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinyl-CoA + 3-hydroxybutyrate | - |
Homo sapiens | succinate + 3-hydroxybutyryl-CoA | - |
? | |
| succinyl-CoA + a 3-oxo acid | - |
Homo sapiens | succinate + a 3-oxoacyl-CoA | - |
? | |
| succinyl-CoA + a 3-oxo acid | ketone bodies, produced mainly in the liver, are an important source of energy for extrahepatic tissues | Homo sapiens | succinate + a 3-oxoacyl-CoA | - |
? | |
| succinyl-CoA + acetoacetate | - |
Homo sapiens | succinate + acetoacetyl-CoA | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SCOT | - |
Homo sapiens |
| succinyl-CoA:3-ketoacid coenzyme A transferase | - |
Homo sapiens |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 40 | 100% SCOT activity of wild-type enzyme | Homo sapiens |
| 30 | - |
59.7% residual SCOT activity of R268H mutant enzyme | Homo sapiens |
| 37 | - |
34% residual SCOT activity of R268H mutant enzyme | Homo sapiens |
| 40 | - |
4% residual SCOT activity of R268H mutant enzyme, the R268H mutant protein has temperature-sensitive instability and dramatically reduces residual SCOT activity to 4% wild-type in 40°C expression so that the R268H mutation is a disease-causing mutation in GS10 and GS11 a SCOT-deficient sibling case from South Africa | Homo sapiens |
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