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Literature summary for 2.3.1.50 extracted from
- Is the mammalian serine-palmitoyltransferase a high molecular weight complex? (2007), Biochem. J., 405, 157-164.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed as a His-tagged fusion protein in Escherichia coli | Homo sapiens |
| individual overexpression of subunits SPTLC1, SPTLC2, and SPTLC3, fused to a C-terminal V5-his tag, in HEK-293 cells | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| myrocin | - |
Homo sapiens |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum membrane | the enzyme is a transmembrane protein | Homo sapiens | 5789 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 480000 | - |
holoenzyme, gel filtration | Homo sapiens |
| 480000 | - |
molecular mass of SPT complex determined by gel filtration | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| palmitoyl-CoA + L-serine | Homo sapiens | the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids, the dynamic composition of the SPT complex could provide a cellular mechanism to adjust SPT activity to tissue specific requirements in sphingolipid synthesis | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| reconstitution of the holoenzyme from subunits SPTLC1 and SPLC2, isolated from placenta extract, and recombinant subunit SPTLC3 forming a single multisubunit SPT complex, overview | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HEK-293 cell | - |
Homo sapiens | - |
| placenta | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| palmitoyl-CoA + L-serine | - |
Homo sapiens | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
| palmitoyl-CoA + L-serine | the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids, the dynamic composition of the SPT complex could provide a cellular mechanism to adjust SPT activity to tissue specific requirements in sphingolipid synthesis | Homo sapiens | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | reconstitution of the holoenzyme from subunits SPTLC1 and SPLC2, isolated from placenta extract, and recombinant subunit SPTLC3 forming a single multisubunit SPT complex, overview | Homo sapiens |
| octamer | results show that functional SPT is not a dimer, but a higher organized complex, composed of three distinct subunits (SPTLC1, SPTLC2 and SPTLC3) with a molecular mass of 480 kDa (gel filtration). The stoichiometry of SPTLC2 and SPTLC3 in this complex is not to be fixed and is changed dynamically in dependence of the tissue specific SPTLC2 and SPTLC3 expression levels. A model of an octameric SPT structure is proposed. By Blue-native-PAGE experiments it is shown that all three SPT subunits (SPTLC1-3) are co-localized within a single SPT complex | Homo sapiens |
| oligomer | the enzyme is composed of three different types of subunits, the stoichiometry of SPTLC2 and SPTLC3 in this complex seems not to be fixed and is probably changed dynamically in dependence of the tissue specific SPTLC2 and SPTLC3 expression levels, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| serine palmitoyltransferase | - |
Homo sapiens |
| serine-palmitoyltransferase | - |
Homo sapiens |
| SPT | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Homo sapiens | |
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