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D ‐Serine inhibits serine palmitoyltransferase, the enzyme catalyzing the initial step of sphingolipid biosynthesis
Author(s) -
Hanada Kentaro,
Hara Tomoko,
Nishijima Masahiro
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01579-9
Subject(s) - serine , biosynthesis , biochemistry , threonine , enzyme , chemistry , sphingolipid , alanine , incubation , amino acid , biology
Serine palmitoyltransferase (SPT), responsible for the initial step of sphingolipid biosynthesis, catalyzes condensation of palmitoyl coenzyme A and L ‐serine to produce 3‐ketodihydrosphingosine (KDS). For determination of the stereochemical specificity of the amino acid substrate, a competition analysis of the production of [ 3 H]KDS from L ‐[ 3 H]serine was performed using purified SPT. D ‐Serine inhibited [ 3 H]KDS production as effectively as non‐radioactive L ‐serine, whereas neither D ‐alanine nor D ‐threonine showed any significant effect. Incubation of purified SPT with [palmitoyl 1‐ 14 C]palmitoyl coenzyme A and D ‐serine did not produce [ 14 C]KDS, while the control incubation with L ‐serine did. These results suggest that D ‐serine competes with L ‐serine for the amino acid recognition site of SPT, but that D ‐serine is not utilized by this enzyme to produce KDS.