Protein Variants | Comment | Organism |
---|---|---|
H159A | site-directed mutagenesis, the mutant shows reduced activity and still forms the pyridoxal 5'-phosphate-L-serine-aldimine reaction intermediate | Sphingomonas paucimobilis |
H159F | site-directed mutagenesis, inactive mutant | Sphingomonas paucimobilis |
H159W | site-directed mutagenesis, inactive mutant | Sphingomonas paucimobilis |
H159Y | site-directed mutagenesis, inactive mutant | Sphingomonas paucimobilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics analysis, detailed overview | Sphingomonas paucimobilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
palmitoyl-CoA + L-serine | Sphingomonas paucimobilis | - |
CoA + 3-dehydro-D-sphinganine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sphingomonas paucimobilis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 | the enzyme forms a pyridoxal 5'-phosphate-L-serine-aldimine intermediate during the reaction, His159 plays multiple roles in the reaction mechanism by exploiting the stereochemistry of Dunathans conjecture. His159 promotes both the Claisen-type condensation as an acid catalyst and the protonation at Calpha of the second quinonoid to form the pyridoxal 5'-phosphate-KDS aldimine, spectral analysis, overview | Sphingomonas paucimobilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
palmitoyl-CoA + L-serine | - |
Sphingomonas paucimobilis | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
palmitoyl-CoA + L-serine | His159 is the anchoring site for L-serine and regulates the alpha-deprotonation of L-serine by fixing the conformation of the pyridoxal 5'-phosphate-L-serine aldimine to prevent unwanted side reactions | Sphingomonas paucimobilis | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | SPT belongs to the fold type I family of the pyridoxal 5'-phosphate-dependent enzymes, and the alpha-oxamine synthase subfamily enzymes | Sphingomonas paucimobilis |
serine palmitoyltransferase | - |
Sphingomonas paucimobilis |
SPT | - |
Sphingomonas paucimobilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Sphingomonas paucimobilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Sphingomonas paucimobilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on, the re face of SPT of the pyridoxal 5'-phosphate-Lys aldimine is occupied by a His159 residue instead of an aromatic amino acid residue as in the other type I enzymes | Sphingomonas paucimobilis |
General Information | Comment | Organism |
---|---|---|
metabolism | SPT catalyzes the first and rate-limiting step of the sphingolipid biosynthetic pathway | Sphingomonas paucimobilis |