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Literature summary for 2.3.1.50 extracted from

  • Shiraiwa, Y.; Ikushiro, H.; Hayashi, H.
    Multifunctional role of His159in the catalytic reaction of serine palmitoyltransferase (2009), J. Biol. Chem., 284, 15487-15495.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics analysis, detailed overview Sphingomonas paucimobilis

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Sphingomonas paucimobilis
-
-
-

Reaction

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 Dunathan’s 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 and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Sphingomonas paucimobilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Sphingomonas paucimobilis

Cofactor

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

General Information Comment Organism
metabolism SPT catalyzes the first and rate-limiting step of the sphingolipid biosynthetic pathway Sphingomonas paucimobilis