Activating Compound | Comment | Organism | Structure |
---|---|---|---|
S-(2-oxoheptadecyl)-CoA | binds to the smSPT-external aldimine complex and enhances the exchange rate of the alpha-proton of L-serine by smSPT | Sphingobacterium multivorum |
Cloned (Comment) | Organism |
---|---|
SPT expression in Escherichia coli strain BL21(DE3) | Sphingobacterium multivorum |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme complexed with L-serine, sitting drop vapor diffusion method, 0.002 ml of protein solution containing 20 mg/ml SPT, 20 mM potasium phosphate, pH 7.7, and 10 mM pyridoxal 5'-phosphate, is mixed with 0.004 ml of reservoir solution containing 100 mM Tris-HCl; pH 8.5, 200 mM sodium acetate, 21.6% w/v PEG 4000, equilibration against 0.5 ml reservoir solution at 20°C, 2 weeks, Schiff base formation between L-serine and pyridoxal 5'-phosphate in the crystal, X-ray diffraction structure determination and analysis at 2.3 A resolution, structural modelling | Sphingobacterium multivorum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
palmitoyl-CoA + L-serine | Sphingobacterium multivorum | - |
CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
palmitoyl-CoA + L-serine | Sphingobacterium multivorum GTC97 | - |
CoA + 3-dehydro-D-sphinganine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sphingobacterium multivorum | A7BFV6 | - |
- |
Sphingobacterium multivorum GTC97 | A7BFV6 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant SPT from Escherichia coli strain BL21(DE3) | Sphingobacterium multivorum |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 | via reaction intermediate pyridoxal 5'-phosphate-L-serine aldimine, His138 changes its hydrogen bond partner from the carboxyl group of L-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the L-serine CaH bond perpendicular to the pyridoxal 5'-phosphate-Schiff base plane, reaction mechanism with substrate synergism in the SPT reaction, overview. Modelling of reaction intermediates | Sphingobacterium multivorum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
palmitoyl-CoA + L-serine | - |
Sphingobacterium multivorum | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? | |
palmitoyl-CoA + L-serine | - |
Sphingobacterium multivorum GTC97 | CoA + 3-dehydro-D-sphinganine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
serine palmitoyltransferase | - |
Sphingobacterium multivorum |
SPT | - |
Sphingobacterium multivorum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Sphingobacterium multivorum |
General Information | Comment | Organism |
---|---|---|
metabolism | SPT is a key enzyme of sphingolipid biosynthesis and catalyses the pyridoxal 5'-phosphate-dependent decarboxylative condensation reaction of L-serine with palmitoyl-CoA to generate 3-ketodihydrosphingosine | Sphingobacterium multivorum |