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Literature summary extracted from

  • Don, A.S.; Rosen, H.
    A lipid binding domain in sphingosine kinase 2 (2009), Biochem. Biophys. Res. Commun., 380, 87-92.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.91 cholesterol 0.01 mM, isoform SphK2, 107% of initial activity Homo sapiens
2.7.1.91 galactosylceramide 0.01 mM, isoform SphK2, 84% of initial activity, isoform SphK1, 109% of initial activity Homo sapiens
2.7.1.91 galactosylceramide 3-sulfate 0.01 mM, isoform SphK2, 37% of initial activity, isoform SphK1, 156% of initial activity Homo sapiens
2.7.1.91 phosphatidic acid 0.01 mM, isoform SphK2, 102% of initial activity, isoform SphK1, 265% of initial activity Homo sapiens
2.7.1.91 phosphatidylinositol 0.01 mM, isoform SphK2,187% of initial activity Homo sapiens
2.7.1.91 phosphatidylinositol 4-phosphate 0.01 mM, isoform SphK2, 89% of initial activity, isoform SphK1, 175% of initial activity Homo sapiens
2.7.1.91 phosphatidylserine 0.01 mM, isoform SphK2, 203% of initial activity Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.91
-
 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.91 additional information isoform SphK2 contains a lipid binding domain at the N-terminal residues 1-175, a region of sequence that is absent in Sphk1. Deleting the N-terminal domain reduces Sphk2 membrane localisation in cells Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.91 3-O-sulfogalactosylceramide endogenous glycolipid sulfatide, binds to and inhibits the activity of isoform Sphk2 and the closely related ceramide kinase Cerk, but not isoform Sphk1. The lipid binding domain is mapped to the N-terminus of Sphk2, residues 1-175, a region of sequence that is absent in Sphk1, but aligns with a pleckstrin homology domain in Cerk Homo sapiens
2.7.1.91 galactosylceramide 0.01 mM, isoform SphK2, 84% of initial activity, isoform SphK1, 109% of initial activity Homo sapiens
2.7.1.91 galactosylceramide 3-sulphate 0.01 mM, isoform SphK2, 37% of initial activity, isoform SphK1, 156% of initial activity Homo sapiens
2.7.1.91 additional information isoform Sphk2 binds to phosphatidylinositol monophosphates but not to abundant cellular phospholipids Homo sapiens
2.7.1.91 phosphatidylinositol 4,5-bisphosphate 0.01 mM, isoform SphK2, 60% of initial activity, isoform SphK1, 90% of initial activity Homo sapiens
2.7.1.91 phosphatidylinositol 4-phosphate 0.01 mM, isoform SphK2, 89% of initial activity, isoform SphK1, 175% of initial activity Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.91 1
-
 nitrobenzoxadiazole-labeled sphingosine pH 7.4, 35°C, presence of 10 microM 3-O-sulfogalactosylceramide Homo sapiens
2.7.1.91 1.7
-
 nitrobenzoxadiazole-labeled sphingosine pH 7.4, 35°C Homo sapiens
2.7.1.91 1.7
-
 nitrobenzoxadiazole-labeled sphingosine pH 7.4, 35°C, presence of 25 microM 3-O-sulfogalactosylceramide Homo sapiens
2.7.1.91 3.6
-
 nitrobenzoxadiazole-labeled sphingosine pH 7.4, 35°C, presence of 4 microM 3-O-sulfogalactosylceramide Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.91 membrane deleting the N-terminal domain with residues 1-175 reduces Sphk2 membrane localisation in cells Homo sapiens 16020
-

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.91 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.91 ATP + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine
-
 Homo sapiens ADP + N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-D-erythro-sphingosine 1-phosphate
-
 ?