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Sphingosine 1-phosphate lyase (SPL)
- Target
- SPL
- Molecular classification
- Enzyme, Lyase, Pyridoxal 5'-phosphate-dependent enzyme
01
Overview
Sphingosine 1-phosphate lyase (SPL, EC 4.1.2.27) is a membrane-bound, pyridoxal 5′-phosphate-dependent enzyme that catalyzes the irreversible cleavage of sphingosine-1-phosphate (S1P), a bioactive lipid mediator, as the final step in the sphingolipid degradative pathway. This reaction produces hexadecenal and ethanolamine phosphate. SPL regulates intracellular levels of S1P, which is crucial for controlling immune cell trafficking, angiogenesis, cell transformation, neuronal autophagy, and other fundamental physiological processes. SPL inactivation leads to accumulation of S1P and related metabolites, making it a potential drug target for immunosuppressive therapies and diseases involving aberrant sphingolipid signaling.
- Other names
- SGPL1
02
Mechanism of action
Catalyzes the irreversible cleavage of sphingosine-1-phosphate (S1P) into hexadecenal and ethanolamine phosphate.
03
Biological functions
Regulation of sphingolipid metabolismRegulation of S1P levelsImmune cell trafficking regulationAngiogenesis regulationPhospholipid biosynthesisRegulation of apoptosisNeuronal autophagy
04
Disease associations
Autoimmune disordersCancerMetabolic disordersInflammatory diseases
05
Safety considerations
Potential for broad immunosuppressionOff-target effects on sphingolipid metabolismDevelopment of resistanceAccumulation of upstream intermediates
06
Interacting drugs
Fingolimod (indirectly through S1P receptor modulation)
1 more in the full profile.
07
Biomarkers
S1P levelsSGPL1 expression levels
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