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Literature summary for 2.3.1.50 extracted from
- Modulating serine palmitoyl transferase (SPT) expression and activity unveils a crucial role in lipid-induced insulin resistance in rat skeletal muscle cells (2009), Biochem. J., 417, 791-801.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | SPT subunit LCB1 knockdown in L6 muscle cells by shRNA causes enzyme activity reduction by over 70%, silencing of LCB1 also leads to an attendant reduction in the expression of LCB2 | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | short-term inhibition of SPT ameliorates palmitate/ceramide-induced insulin resistance, sustained loss/reduction in SPT expression/activity promotes greater partitioning of palmitate towards diacylglycerol synthesis, which impacts negatively upon IRS1-directed insulin signalling | Rattus norvegicus | |
| myriocin | an SPT inhibitor | Rattus norvegicus |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| plasma membrane | - |
Rattus norvegicus | 5886 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| palmitoyl-CoA + L-serine | Rattus norvegicus | - |
CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| L-6 myoblast cell | - |
Rattus norvegicus | - |
| myotube | - |
Rattus norvegicus | - |
| skeletal muscle | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| palmitoyl-CoA + L-serine | - |
Rattus norvegicus | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | subunits LCB1 and LCB2 | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| serine palmitoyl transferase | - |
Rattus norvegicus |
| SPT | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Rattus norvegicus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | IRS1 serine phosphorylation and PKCtheta recruitment to the plasma membrane are increased in cells with reduced SPT expression and activity. Short-term inhibition of SPT ameliorates palmitate/ceramide-induced insulin resistance, sustained loss/reduction in SPT expression/activity promotes greater partitioning of palmitate towards diacylglycerol synthesis, which impacts negatively upon IRS1-directed insulin signalling | Rattus norvegicus |
| physiological function | SPT plays a crucial role in lipid-induced insulin resistance in skeletal muscle cells by desensitizing muscle cells to insulin in response to incubation with palmitate, overview. The effect is antagonized by inhibition of protein kinase C | Rattus norvegicus |
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Release 2023.1 (January 2023)
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