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Information on EC 4.1.2.27 - sphinganine-1-phosphate aldolase
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4.1.2.27 sphinganine-1-phosphate aldolaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.2.27
- sphingolipids
- ceramide
-
sphingoid
-
egress
- lymphopenia
- dihydrosphingosine-1-phosphate
- medicine
- fingolimod
-
s1p-degrading
-
sphks
- 4-deoxypyridoxine
-
steroid-resistant
- analysis
-
lyase-deficient
-
s1p-dependent
-
spinster
-
s1p-induced
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
s1p lyase, sgpl1, sphingosine-1-phosphate lyase, s1p-lyase, sphingosine phosphate lyase, sphingosine 1-phosphate lyase, legs2, dpl1p, s1pl2021, sphingosine-phosphate lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldolase, dihydrosphingosine 1-phosphate
-
-
-
-
Dihydrosphingosine 1-phosphate aldolase
-
-
-
-
dihydrosphingosine phosphate lyase
Dpl1
Dpl1p
LegS2
S1P lyase
S1PL
S1PL2021
sphinganine 1-phosphate lyase
-
-
-
-
sphinganine-1-phosphate aldolase
sphinganine-1-phosphate-alkanal-lyase
-
-
-
-
sphingosine 1-phosphate lyase
sphingosine phosphate lyase
sphingosine-1-phosphate lyase
sphingosine-phosphate lyase
-
-
-
-
SPL
sphinganine-1-phosphate aldolase
-
-
-
-
sphingosine-1-phosphate lyase
-
-
-
-
sphingosine-1-phosphate lyase
-
-
SPL
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
possible reaction mechanism for the enzyme
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
irreversible reaction
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme is stereospecific for the D-erythro sphingoid base
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme-catalyzed conversion of (2S,3R)-sphinganine 1-phosphate to ethanolamine 1-phosphate involves the stereospecific incorporation of one atom of solvent hydrogen at carbon atom 2 of the latter compound
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
pyridoxal phosphate dependent catalysis
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
enzyme has been classified within the group of carbon-carbon lyases a subclass of aldehyde-lyases (Enzyme Nomenclature 1984)
-
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
of an aldehyde, C-C bond cleavage
-
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SYSTEMATIC NAME
IUBMB Comments
sphinganine-1-phosphate palmitaldehyde-lyase (phosphoethanolamine-forming)
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
37290-61-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3R,4E)-2-ammonio-3-hydroxy-7-((2-oxo-2H-chromen-7-yl)oxy)hept-4-en-1-yl hydrogenphosphate
?
i.e. RBM77
-
-
?
(2S,3R,5E)-2-ammonio-3-hydroxy-7-((2-oxo-2H-chromen-7-yl)oxy)hept-5-en-1-yl hydrogenphosphate
?
i.e. RBM148
-
-
?
4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled sphinganine 1-phosphate
phosphoethanolamine + 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled palmitaldehyde
-
i.e. BODIPY-label, allows fluorescent product detection by HPLC
major aldehyde product is confirmed by reaction with 2,4-dinitrophenylhydrazine
-
?
7-nitrobenz-2-oxa-1,3-diazole-sphingosine 1-phosphate
phosphoethanolamine + 7-nitrobenz-2-oxa-1,3-diazole-hexadec-2-enal
boron dipyrromethene difluoride-sphingosine 1-phosphate
phosphoethanolamine + boron dipyrromethene difluoride-hexadec-2-enal
eicosadihydrosphingosine 1-phosphate + H2O
hexadecanal + 2-(icosanoylamino)ethyl phosphate
-
-
-
?
omega-(7-nitro-2-1,3-benzoxadiazol-4-yl)-D-erythro-sphingosine 1-phosphate
phosphoethanolamine + omega-(7-nitro-2-1,3-benzoxadiazol-4-yl)-D-erythro-(2E)-hexadecenal
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + hexadecanal
-
-
?
umbelliferone-labled sphinganine 1-phosphate
phosphoethanolamine + 3-[(2-oxo-2H-chromen-7-yl)oxy]propanal
(2E)-hexadecenal + semicarbazide
(2E)-hexadecenal semicarbazone
-
-
-
?
(2E)-hexadecenal + semicarbazide
(2E)-hexadecenal semicarbazone
-
-
-
?
4D-Hydroxysphinganine 1-phosphate
Phosphoethanolamine + 2-hydroxyhexadecanal
-
-
-
?
4D-Hydroxysphinganine 1-phosphate
Phosphoethanolamine + 2-hydroxyhexadecanal
-
-
-
?
4D-Hydroxysphinganine 1-phosphate
Phosphoethanolamine + 2-hydroxyhexadecanal
-
-
-
?
7-nitrobenz-2-oxa-1,3-diazole-sphingosine 1-phosphate
phosphoethanolamine + 7-nitrobenz-2-oxa-1,3-diazole-hexadec-2-enal
-
-
-
-
?
7-nitrobenz-2-oxa-1,3-diazole-sphingosine 1-phosphate
phosphoethanolamine + 7-nitrobenz-2-oxa-1,3-diazole-hexadec-2-enal
-
-
-
?
7-nitrobenz-2-oxa-1,3-diazole-sphingosine 1-phosphate
phosphoethanolamine + 7-nitrobenz-2-oxa-1,3-diazole-hexadec-2-enal
-
-
-
-
?
boron dipyrromethene difluoride-sphingosine 1-phosphate
phosphoethanolamine + boron dipyrromethene difluoride-hexadec-2-enal
-
-
-
-
?
boron dipyrromethene difluoride-sphingosine 1-phosphate
phosphoethanolamine + boron dipyrromethene difluoride-hexadec-2-enal
-
-
-
?
boron dipyrromethene difluoride-sphingosine 1-phosphate
phosphoethanolamine + boron dipyrromethene difluoride-hexadec-2-enal
-
-
-
-
?
D-(+)-erythro-sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
-
ir
D-(+)-erythro-sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
ir
D-(+)-erythro-sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
-
ir
D-erythrosphingosine
?
8% activity compared to sphinganine 1-phosphate
-
-
?
D-erythrosphingosine
?
8% activity compared to sphinganine 1-phosphate
-
-
?
Dihydrosphingosine 1-phosphonate
Aminoethylphosphonate + palmidaldehyde
-
-
-
-
?
Dihydrosphingosine 1-phosphonate
Aminoethylphosphonate + palmidaldehyde
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-
-
-
?
Dihydrosphingosine 1-phosphonate
Aminoethylphosphonate + palmidaldehyde
-
-
-
-
?
Dihydrosphingosine 1-phosphonate
Aminoethylphosphonate + palmidaldehyde
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1-deoxysphinganine 1-phosphonate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
dihydrosphingosine-1-phosphate
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?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
dihydrosphingosine-1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
D-erythro-(2S,3R)-sphinganine 1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
D-erythro-(2S,3R)-sphinganine 1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
D(+)-erythro-dihydrosphingosine-1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
dihydrosphingosine-1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
dihydrosphingosine-1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
erythro-DL-dihydrosphingosine 1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
erythro-sphinganine 1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
threo-dihydrosphingosine 1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
D(+)-erythro-dihydrosphingosine-1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
dihydrosphingosine-1-phosphate
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
dihydrosphingosine-1-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
-
SPL from Symbiobacterium thermophilum degrades extracellular sphingosine 1-phosphate in vitro and in blood
-
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
pathway of sphingomyelin degradation, sphingosine 1-phosphate is an important element of signal transduction pathways that regulate cell proliferation and cell death
-
ir
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
ir
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
4t-sphingosine 1-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
sphingenine-phosphate
-
?
umbelliferone-labled sphinganine 1-phosphate
phosphoethanolamine + 3-[(2-oxo-2H-chromen-7-yl)oxy]propanal
-
-
-
-
?
umbelliferone-labled sphinganine 1-phosphate
phosphoethanolamine + 3-[(2-oxo-2H-chromen-7-yl)oxy]propanal
-
-
-
?
umbelliferone-labled sphinganine 1-phosphate
phosphoethanolamine + 3-[(2-oxo-2H-chromen-7-yl)oxy]propanal
-
-
-
-
?
additional information
?
-
-
critical role in maintenance of intestinal integrity and normal reproduction
-
?
additional information
?
-
-
metabolic pathways of the enzyme substrates
-
-
?
additional information
?
-
-
acts on 1-phosphorylated derivatives of sphingoid bases, products are an aliphatic fatty aldehyde and phosphoethanolamine
-
?
additional information
?
-
role in ceramide metabolism and cell fate
-
?
additional information
?
-
-
role in ceramide metabolism and cell fate
-
?
additional information
?
-
-
acts on 1-phosphorylated derivatives of sphingoid bases, products are an aliphatic fatty aldehyde and phosphoethanolamine
-
?
additional information
?
-
-
acts on 1-phosphorylated derivatives of sphingoid bases, products are an aliphatic fatty aldehyde and phosphoethanolamine
-
?
additional information
?
-
-
phosphoethanolamine is characterized by various forms of chromatography
-
-
?
additional information
?
-
-
metabolic pathways of the enzyme substrates
-
-
?
additional information
?
-
-
enzyme is responsible for the ultimate step in sphingolipid breakdown, converting phosphorylated long chain bases into ethanolamine phosphate and fatty aldehyde
-
-
?
additional information
?
-
-
metabolic relationship between substrates and products of biosynthesis and degradation of sphingosine bases
-
-
?
additional information
?
-
-
enzyme catalyzes a rate-limiting step in sphingolipid catabolism
-
-
?
additional information
?
-
-
metabolic pathways of the enzyme substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sphingosine 1-phosphate
phosphoethanolamine + palmitaldehyde
pathway of sphingomyelin degradation, sphingosine 1-phosphate is an important element of signal transduction pathways that regulate cell proliferation and cell death
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
?
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
-
-
-
-
ir
additional information
?
-
-
critical role in maintenance of intestinal integrity and normal reproduction
-
?
additional information
?
-
-
metabolic pathways of the enzyme substrates
-
-
?
additional information
?
-
role in ceramide metabolism and cell fate
-
?
additional information
?
-
-
role in ceramide metabolism and cell fate
-
?
additional information
?
-
-
acts on 1-phosphorylated derivatives of sphingoid bases, products are an aliphatic fatty aldehyde and phosphoethanolamine
-
?
additional information
?
-
-
metabolic pathways of the enzyme substrates
-
-
?
additional information
?
-
-
enzyme is responsible for the ultimate step in sphingolipid breakdown, converting phosphorylated long chain bases into ethanolamine phosphate and fatty aldehyde
-
-
?
additional information
?
-
-
metabolic relationship between substrates and products of biosynthesis and degradation of sphingosine bases
-
-
?
additional information
?
-
-
enzyme catalyzes a rate-limiting step in sphingolipid catabolism
-
-
?
additional information
?
-
-
metabolic pathways of the enzyme substrates
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F-
F-
-
NaF required to inhibit phosphatases which rapidly hydrolyse the substrate sphinganine 1-phosphate and the coenzyme pyridoxal phosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S,3R)-1-(1H,1'H-2,2'-biimidazol-4-yl)butane-1,2,3,4-tetraol
-
inhibitory to sphinganine 1-phosphate lyase. 53% decrease in circulating lymphocytes after 30 mg/kg oral dose
(1R,2S,3R)-1-(2-(1-benzyl-1H-1,2,4-triazol-3-yl)-1H-imidazol-4-yl)butane-1,2,3,4-tetraol
-
inhibitory to sphinganine 1-phosphate lyase. 41% decrease in circulating lymphocytes after 30 mg/kg oral dose
(1R,2S,3R)-1-(2-(thiazol-4-yl)-1H-imidazol-4-yl)butane-1,2,3,4-tetraol
-
inhibitory to sphinganine 1-phosphate lyase. 33% decrease in circulating lymphocytes after 30 mg/kg oral dose
(R)-1-benzyl-4-(3-methyl-4-(5-(trifluoromethyl)pyridin-2-yl)-piperazin-1-yl)phthalazine
-
-
(R)-1-benzyl-4-(3-methyl-4-(5-nitropyridin-2-yl)piperazin-1-yl)-phthalazine
-
-
(R)-1-benzyl-4-(4-(5-cyanopyridin-2-yl)-3-methylpiperazin-1-yl)phthalazine-6-carbonitrile
-
-
(R)-4-benzyl-1-(4-(5-cyanopyridin-2-yl)-3-methylpiperazin-1-yl)phthalazine-6-carbonitrile
-
-
(R)-6-(2-methyl-4-(4-phenethylphthalazin-1-yl)piperazin-1-yl)nicotinonitrile
-
-
(R)-6-(2-methyl-4-(4-phenylphthalazin-1-yl)piperazin-1-yl)-nicotinonitrile
-
-
(R)-6-(4-(4-benzyl-6-(trifluoromethyl)phthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
-
-
(R)-6-(4-(4-benzyl-6-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
-
-
(R)-6-(4-(4-benzyl-7-(trifluoromethyl)phthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
-
-
(R)-6-(4-(4-benzyl-7-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
-
-
(R)-6-(4-(4-benzylphthalazin-1-yl)-2-ethylpiperazin-1-yl)nicotinonitrile
-
-
(R)-6-(4-(4-benzylphthalazin-1-yl)-2-isopropylpiperazin-1-yl)-nicotinonitrile
-
-
(R)-6-(4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl)-nicotinic acid
-
-
(R)-6-(4-(4-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)-nicotinonitrile
-
-
(S)-6-(4-(4-benzylphthalazin-1-yl)-2-(hydroxymethyl)piperazin-1-yl)nicotinonitrile
-
-
1-(4-((1R,2S,3R)-1,2,3,4-tetrahydroxybutyl)-1H-imidazol-2-yl)ethanone
-
inhibitory to sphinganine 1-phosphate lyase. 25% decrease in circulating lymphocytes after 30 mg/kg oral dose
1-benzyl-4-[(3R)-4-(5-cyanopyridin-2-yl)-3-methylpiperazin-1-yl]phthalazine-6-carbonitrile
-
-
1-{5-[(1R,2S,3R)-1,2,3,4-tetrahydroxybutyl]-1H-imidazol-2-yl}ethanone
-
when given overnight at 25 mg/l in drinking water, tetrahydroxybutylimidazole raises sphingosine 1-phosphate levels and reduces SPL activity
2-acetyl-4(5)-tetrahydroxybutyl imidazole
-
inhibitory. Following the oral administration of 10 and 100 mg/kg 2-acetyl-4(5)-tetrahydroxybutyl imidazole to male rats, 2-acetyl-4(5)-tetrahydroxybutyl imidazole is rapidly absorbed and reaches a plasma peak level at 1 h post-dosing. Splenic S1P increases and reaches the peak level at 24 h. Blood lymphocyte count decreases as the splenic S1P level increases. 2-Acetyl-4(5)-tetrahydroxybutyl imidazole plasma concentration is linked to splenic S1P concentration using an indirect model incorporated with a four-step signal transduction model. In turn, the S1P level is directly coupled with blood lymphocyte number
2-acetyl-4-(tetrahydroxybutyl)imidazole
-
the enzyme is inhibited indirectly by 2-acetyl-4-(tetrahydroxybutyl)imidazole under conditions of vitamin B6 deficiency
4-amino-N-[4-(1H-imidazol-1-yl)benzyl]-5-oxo-2-(piperidin-1-yl)-8-(tetrahydrofuran-2-ylmethyl)-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxamide
-
-
5-cyclopropyl-N-[2-[(4-ethoxy-2,5-dimethylbenzyl)amino]-1-(4-fluorophenyl)ethyl]-1,2-oxazole-3-carboxamide
-
-
5-cyclopropyl-N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-1,2-oxazole-3-carboxamide
-
-
5-methoxy-N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-1,2-oxazole-3-carboxamide
-
-
6-[(2R)-4-(4-benzyl-7-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile
-
-
cisplatin
-
cells overexpressing enzyme show increased sensitivity, mediated by death kinase p38
ethyl 6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carboxylate
-
fumonisin B1
-
10 mg/kg inhibits the expression of sphingosine 1-phosphate lyase
N-(2-[[2,5-dimethyl-4-(2,2,2-trifluoroethoxy)benzyl]amino]-1-phenylethyl)-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-(2-[[2,5-dimethyl-4-(pyridin-4-ylmethoxy)benzyl]amino]-1-phenylethyl)-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-(2-[[4-methoxy-2-methyl-5-(trifluoromethyl)benzyl]amino]-1-phenylethyl)-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[1-(4-fluorophenyl)-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[1-[3-(4-amino-4-oxobutyl)phenyl]-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[1-[4-(3-hydroxyprop-1-yn-1-yl)phenyl]-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[1-[4-(4-amino-4-oxobutyl)phenyl]-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-butoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-ethoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-(2-methoxyphenyl)ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-(3-methoxyphenyl)ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-(4-methoxyphenyl)ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-3-methyl-1,2-oxazole-5-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-[4-(pyridin-4-yl)phenyl]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[2-[(4-methoxybenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
sphinganine phosphate
-
2D,3L-isomer is a competitive inhibitor, but 2L,3L-isomer does not influence the enzyme
6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile
-
-
6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile
-
FTY720
-
in vitro inhibition of enzyme, effects occurring from 300 nM concentrations on, maximal effects at 0.03 mM
FTY720
-
in vivo enzyme inhibition concommitantly with lymphopenia, neither enzyme gene expression nor tissue enzyme protein expression is affected by inhibior
FTY720
-
produces an 82% inhibition at equimolar concentration with C17-sphinganine-1-phosphate
N-[(1R,2S)-2-hydroxy-1-hydroxymethyl-2-(2-tridecyl-1-cyclopentenyl)ethyl]octanamide
-
-
N-[(1R,2S)-2-hydroxy-1-hydroxymethyl-2-(2-tridecyl-1-cyclopentenyl)ethyl]octanamide
-
N-[(1R,2S)-2-hydroxy-1-hydroxymethyl-2-(2-tridecyl-1-cyclopentenyl)ethyl]octanamide
-
-
Semicarbazide
-
nonspecific SPL inhibitor, reduces SPL activity in vitro by about 70% at 2 mM
[2-amino-2[2-(4-octylphenyl)ethyl]-3-hydroxypropyl]dihydrogen phosphate
-
[2-amino-2[2-(4-octylphenyl)ethyl]-3-hydroxypropyl]dihydrogen phosphate
-
-
additional information
-
overexpression of enzyme, no change in sensitivity to vincristine, chlorambucil
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled sphinganine 1-phosphate
-
37°C
0.0201
Dihydrosphingosine 1-phosphonate
-
in 0.6 mM EDTA, 0.4 mM pyridoxal 5'-phosphate, 3 mM dithiothreitol mM sucrose, 36 mM potassium phosphate buffer, and 36 mM NaF containing 0.08% Triton X-100
0.0057
sphingosine 1-phosphate
-
in 35 mM potassium phosphate buffer (pH 7.4), 0.6 mM EDTA, 70 mM sucrose, 36 mM sodium fluoride, 0.57 mM pyridoxal 5'-phosphate, at 37°C
0.0146
sphingosine 1-phosphate
-
in 0.6 mM EDTA, 0.4 mM pyridoxal 5'-phosphate, 3 mM dithiothreitol mM sucrose, 36 mM potassium phosphate buffer, and 36 mM NaF containing 0.08% Triton X-100
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0175
(2R,3R,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
-
at pH 10.6 and 37°C
0.0056
(2R,3S,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
-
at pH 10.6 and 37°C
0.0091
(2S,3R,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
-
at pH 10.6 and 37°C
0.0204
(2S,3S,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
-
at pH 10.6 and 37°C
0.005
1-deoxydihydrosphingosine 1-phosphonate
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
(R)-1-benzyl-4-(3-methyl-4-(5-(trifluoromethyl)pyridin-2-yl)-piperazin-1-yl)phthalazine
Homo sapiens
at pH 7.4 and 25°C
-
0.00074
(R)-1-benzyl-4-(3-methyl-4-(5-nitropyridin-2-yl)piperazin-1-yl)-phthalazine
Homo sapiens
at pH 7.4 and 25°C
-
0.000024
(R)-1-benzyl-4-(4-(5-cyanopyridin-2-yl)-3-methylpiperazin-1-yl)phthalazine-6-carbonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.0013
(R)-4-benzyl-1-(4-(5-cyanopyridin-2-yl)-3-methylpiperazin-1-yl)phthalazine-6-carbonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.03
(R)-6-(2-methyl-4-(4-phenethylphthalazin-1-yl)piperazin-1-yl)nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.03
(R)-6-(2-methyl-4-(4-phenylphthalazin-1-yl)piperazin-1-yl)-nicotinonitrile
Homo sapiens
IC50 above 0.03 mM, at pH 7.4 and 25°C
-
0.012
(R)-6-(4-(4-benzyl-6-(trifluoromethyl)phthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.0023
(R)-6-(4-(4-benzyl-6-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.0001
(R)-6-(4-(4-benzyl-7-(trifluoromethyl)phthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.00021
(R)-6-(4-(4-benzyl-7-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.0017
(R)-6-(4-(4-benzylphthalazin-1-yl)-2-ethylpiperazin-1-yl)nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.0025
(R)-6-(4-(4-benzylphthalazin-1-yl)-2-isopropylpiperazin-1-yl)-nicotinonitrile
Homo sapiens
at pH 7.4 and 25°C
-
0.03
(R)-6-(4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl)-nicotinic acid, (R)-6-(4-(4-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)-nicotinonitrile
Homo sapiens
IC50 above 0.03 mM, at pH 7.4 and 25°C
-
0.03
(R)-6-(4-(4-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)-nicotinonitrile
Homo sapiens
-
IC50 above 0.03 mM, at pH 7.4 and 25°C
-
0.03
(S)-6-(4-(4-benzylphthalazin-1-yl)-2-(hydroxymethyl)piperazin-1-yl)nicotinonitrile
Homo sapiens
IC50 above 0.03 mM, at pH 7.4 and 25°C
-
0.0024
2-vinylsphinganine 1-phosphate
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
5-cyclopropyl-N-[2-[(4-ethoxy-2,5-dimethylbenzyl)amino]-1-(4-fluorophenyl)ethyl]-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00073
5-cyclopropyl-N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0092
5-methoxy-N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0024 - 0.03
6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile
0.03
6-[4-(4-benzylphthalazin-1-yl)piperazin-1-yl]pyridine-3-carbonitrile
Homo sapiens
IC50 above 0.03 mM, at pH 7.4 and 25°C
0.0034
ethyl 6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carboxylate
Homo sapiens
at pH 7.4 and 25°C
0.00059
N-(2-[[2,5-dimethyl-4-(2,2,2-trifluoroethoxy)benzyl]amino]-1-phenylethyl)-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
N-(2-[[2,5-dimethyl-4-(pyridin-4-ylmethoxy)benzyl]amino]-1-phenylethyl)-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
N-(2-[[4-methoxy-2-methyl-5-(trifluoromethyl)benzyl]amino]-1-phenylethyl)-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00072
N-[1-(4-fluorophenyl)-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0096
N-[1-[3-(4-amino-4-oxobutyl)phenyl]-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
N-[1-[4-(3-hydroxyprop-1-yn-1-yl)phenyl]-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
N-[1-[4-(4-amino-4-oxobutyl)phenyl]-2-[(4-methoxy-2,5-dimethylbenzyl)amino]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
N-[2-[(4-butoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
N-[2-[(4-ethoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.05
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-(2-methoxyphenyl)ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
IC50 above 0.05 mM, pH and temperature not specified in the publication
0.0073
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-(3-methoxyphenyl)ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.005
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-(4-methoxyphenyl)ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0064
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0038
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-3-methyl-1,2-oxazole-5-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00085
N-[2-[(4-methoxy-2,5-dimethylbenzyl)amino]-1-[4-(pyridin-4-yl)phenyl]ethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.05
N-[2-[(4-methoxybenzyl)amino]-1-phenylethyl]-5-methyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
IC50 above 0.05 mM, pH and temperature not specified in the publication
0.0243
(2R,3R)-2-azido-3-hydroxyoctadecyl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0117
(2R,3R,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0229
(2R,3R,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Homo sapiens
-
at pH 10.6 and 37°C
0.025
(2R,3S)-2-azido-3-hydroxyoctadecyl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0052
(2R,3S,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Homo sapiens
-
at pH 10.6 and 37°C
0.0138
(2R,3S,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0257
(2S,3R)-2-azido-3-hydroxyoctadecyl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0101
(2S,3R,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Homo sapiens
-
at pH 10.6 and 37°C
0.0129
(2S,3R,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0272
(2S,3S)-2-azido-3-hydroxyoctadecyl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.016
(2S,3S,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0288
(2S,3S,4E)-2-azido-3-hydroxyoctadec-4-en-1-yl phosphate
Homo sapiens
-
at pH 10.6 and 37°C
0.0024
2-vinyldihydrosphingosine 1-phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0024
6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile
Homo sapiens
at pH 7.4 and 25°C
0.03
6-[(2R)-4-(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile
Homo sapiens
IC50 above 0.03 mM, at pH 7.4 and 25°C
0.0524
FTY720
Mus musculus
-
in 35 mM potassium phosphate buffer (pH 7.4), 0.6 mM EDTA, 70 mM sucrose, 36 mM sodium fluoride, 0.57 mM pyridoxal 5'-phosphate, at 37°C
0.047
phosphopyridoxyl sphinganine 1-phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
0.0534
phosphopyridoxyl sphingosine 1-phosphate
Symbiobacterium thermophilum
-
at pH 10.6 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the cells expressing sphingosine-1-phosphate lyase in the parenchyma o lymph nodes are CD68+ antigen-presenting cells. CD68+ antigen-presenting cells generated from human monocytes are able to internalize and irreversibly degrade sphingosine 1-phosphate
brenda
-
inhibition of sphingosine-1-phosphate lyase activity rendes sphingosine 1-phosphate an efficient S1P1 receptor internalizing compound and abrogated sphingosine-1-phosphate-mediated sustained signaling, suggesting that sphingosine-1-phosphate lyase by facilitating S1P1 receptor recycling is essential for sphingosine-1-phosphate-mediated sustained signaling, and that synthetic agonists are functional antagonists because they are not sphingosine-1-phosphate lyase substrates
brenda
-
silencing of sphingosine 1-phosphate lyase enhances survival after irradiation or chemotherapy by decreasing expression of proteins involved in sensing and repairing DNA damage or apoptosis, respectively. Enforced expression of sphingosine 1-phosphate lyase sensitizes cancer cells to irradiation or docetaxel by tilting the ceramide/sphingosine 1-phosphate balance toward cell death
brenda
-
sphingosine-1-phosphate lyase expression is almost exclusively restricted to cells on the parenchymal side of marginal reticular cells, consistent with a role in maintaining the S1P gradient between the sinuses and the parenchyma
brenda
sphingosine-1-phosphate lyase is induced during myoblast differentiation
brenda
-
of the olfactory bulb, cerebral cortex, midbrain, hindbrain, and cerebellum, high expression rate
brenda
the enzyme is highly enriched in olfactory mucosal epithelium
brenda
-
silencing of sphingosine 1-phosphate lyase enhances survival after irradiation or chemotherapy by decreasing expression of proteins involved in sensing and repairing DNA damage or apoptosis, respectively. Enforced expression of sphingosine 1-phosphate lyase sensitizes cancer cells to irradiation or docetaxel by tilting the ceramide/sphingosine 1-phosphate balance toward cell death
brenda
-
in fresh human prostatectomy specimens, a remarkable decrease in sphingosine 1-phosphate lyase enzymatic activity is found in tumor samples, as compared with normal adjacent tissues. A significant relationship between loss of sphingosine 1-phosphate lyase expression and higher Gleason score is confirmed. Sphingosine 1-phosphate lyase protein expression and activity are inversely correlated with those of sphingosine kinase-1, the enzyme producing sphingosine 1-phosphate. Sphingosine 1-phosphate lyase and sphingosine kinase expressions are independently predictive of aggressive cancer on tissue microarray
brenda
-
spingosine 1-phosphate lyase is modestly expressed at day 20 of pregnancy antd then decreases. In contrast, sphingosine 1-phosphate receptor mRNA increases in endometrium and caruncular stroma of the gravid uterine horn
brenda
additional information
-
mRNA expression is temporally regulated during embryonal development
brenda
-
mRNA expression is temporally regulated during embryonal development
brenda
-
-
brenda
additional information
-
no expression in gonad, body wall muscle, pharynx, vulva and epidermis
brenda
additional information
-
the human SGPL1 gene is ubiquitously expressed with the exception of erythrocytes and platelets and its expression is linked to tissues undergoing rapid cell turnover
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the large hydrophilic domain containing the active site is facing the cytosol
brenda
-
inner mitochondrial membrane possesses the highest activity
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
downregulation/inhibition of SPL prevents premature cell cycle progression and mitotic death. Oral administration of an SPL inhibitor to mice prolonges their survival after exposure to a lethal dose (10Gy) of total body ionizing radiation
malfunction
-
hearts of heterozygous SPL knockout mice exhibit reduced SPL activity, elevated sphingosine 1-phosphate levels, smaller infarct size, and increased functional recovery after ischemia-reperfusion injury compared with littermate controls
malfunction
-
inhibition of S1PL with 4-deoxypyridoxine or knockdown of S1PL with siRNA increases intracellular sphingosine-1-phosphate 3fold, potentiates motility of HPAEC cells to extracellular sphingosine-1-phosphate or serum, and augments activated Rac1 as well as stimulates Rac1 and IQGAP1 translocation to the cell periphery
malfunction
-
enzyme inhibition causes protein-losing glomerulopathy due to podocyte dysfunction, skin irritation, and platelet activation and may also be associated with pathological alterations in other tissues such as lung, liver, thymus, and the red blood cell system
malfunction
-
enzyme inhibition causes protein-losing glomerulopathy due to podocyte dysfunction, skin irritation, and platelet activation and may also be associated with pathological alterations in other tissues such as lung, liver, thymus, and the red blood cell system
malfunction
-
enzyme-deficient mutants display impaired intracellular replication in murine macrophages (associated with an inability to evade the maturing phagosome)
malfunction
-
enzyme-deficient mutants display impaired intracellular replication in murine macrophages (associated with an inability to evade the maturing phagosome)
malfunction
-
the absence of the enzyme is associated with reduced NF-kappaB activation and atypical morphology of mitochondria
malfunction
-
the absence of the enzyme is associated with reduced NF-kappaB activation and atypical morphology of mitochondria
-
malfunction
-
enzyme-deficient mutants display impaired intracellular replication in murine macrophages (associated with an inability to evade the maturing phagosome)
-
metabolism
-
S1P lyase catalyzes the irreversible degradation of sphingosine 1-phosphate in the final step of sphingolipid metabolism
metabolism
-
sphingosine-1-phosphate lyase is a key enzyme of sphingolipid metabolism
metabolism
sphingosine-1-phosphate lyase is a key enzyme of sphingolipid metabolism
metabolism
sphingosine-1-phosphate lyase is a key enzyme of sphingolipid metabolism
metabolism
-
SPL functions as the exit gate of the sphingolipid metabolism
metabolism
-
SPL functions as the exit gate of the sphingolipid metabolism
metabolism
-
SPL functions as the exit gate of the sphingolipid metabolism
physiological function
-
all S1PL-deficient genetic models used display lymphopenia, with sequestration of mature T-cells in the thymus and lymph nodes. In addition to the lymphoid phenotypes, S1PL KO mice also develop myeloid cell hyperplasia and significant lesions in the lung, heart, urinary tract, and bone, and have a markedly reduced life span. Complete absence of S1PL affects both maturation/development and egress of mature T cells from the thymus, whereas low level S1PL activity affects T-cell egress more than differentiation
physiological function
all S1PL-deficient genetic models used display lymphopenia, with sequestration of mature T-cells in the thymus and lymph nodes. In addition to the lymphoid phenotypes, S1PL KO mice also develop myeloid cell hyperplasia and significant lesions in the lung, heart, urinary tract, and bone, and have a markedly reduced life span. Complete absence of S1PL affects both maturation/development and egress of mature T cells from the thymus, whereas low level S1PL activity affects T-cell egress more than differentiation
physiological function
-
complete loss of SPL activity leads to upregulation of the antiapoptotic proteins Bcl-2 and Bcl-xL and consequently protects against apoptosis induced by chemotherapy and nutrient starvation but not against autophagy. Disruption of the gene encoding SPL is accompanied by concomitant accumulation of sphingosine and ceramide. SPL deficiency blocks the apoptotic cascade upstream of mitochondrial damage and leads to upregulation of the antiapoptotic proteins Bcl-2 and Bcl-xL without affecting the levels of the proapoptotic members Bax and Bid. Whereas starvation-induced apoptosis is reduced in Sgpl1-/- compared to Sgpl1+/+ cells, autophagy is similar in both cell types
physiological function
-
in mice with an inactive S1P lyase gene, in addition to the expected increase of sphingoid base phosphates, other sphingolipids including sphingosine, ceramide, and sphingomyelin are substantially elevated in the serum and/or liver. The S1P lyase deficiency results in changes in the levels of serum and liver lipids not directly within the sphingolipid pathway, including phospholipids, triacyglycerol, diacylglycerol, and cholesterol. Lipids in serum and lipid storage are elevated in liver, but adiposity is reduced in the S1P lyase-deficient mice. The S1P lyase deficiency causes widespread changes in the expression pattern of lipid metabolism genes, with a significant increase in the expression of PPAR, a master transcriptional regulator of lipid metabolism. The mRNA expression of the genes encoding the sphingosine kinases and S1P phosphatases, which directly control the levels of S1P, are not significantly changed in liver of the S1P lyase-deficient mice
physiological function
-
in mouse embryonic fibroblasts deficient in S1P lyase, sphingosine 1-phosphate and sphingosine concentrations are elevated about 6fold and 2fold, respectively. Resting intracellular Ca2+ is elevated and agonist-induced intracellular Ca2+ increases are augmented in S1P lyase-deficient cells both in the presence and absence of extracellular Ca2+. Intracellular Ca2+ increases and Ca2+ mobilization induced by the SERCA inhibitor, thapsigargin, are augmented. At least two cell types can be distinguished, one with a rapid and transient intracellular Ca2+-increase and the other with a slower and prolonged intracellular Ca2+ elevation upon stimulation with thapsigargin. Intracellular Ca2+ increases upon thapsigargin stimulation, reflecting overall Ca2+ release, by more than 50% in both rapidly and slowly responding S1P lyase-deficient cells
physiological function
-
incubation of lyase-deficient neurons with either sphingosine or S1P results in a similar elevation in cellular S1P, but only S1P addition to the culture medium induces apoptosis. This is not due to S1P acting on the S1P receptor but to hydrolysis of S1P to sphingosine that is phosphorylated by the cells. Although the cells produce S1P from both exogenously added sphingosine as well as sphingosine derived from exogenous S1P, the S1P from these two sources are not equivalent, because the former is primarily produced by SK1, whereas the latter is mainly formed by sphingosine kinase-2
physiological function
-
thymocyte development in SGPL1-deficient mice which exhibit postnatal discontinuation of early thymocytopoies is starting at 2 weeks after birth. SGPL-/- thymi show a loss of developing thymocytes in the thymic cortex between 2 and 4 weeks of age, whereas mature thymocytes accumulate in the medulla. Increased ceramide levels in the thymus of SGPL1-/- mice abrogates thymic development postnatally by enhanced thymocyte apoptosis and depletion of thymic ETP. Potentially therapeutic immunosuppression by SGPL1 inhibition should benefit from monitoring ceramides to prevent their increase to apoptosis-inducing levels
physiological function
-
in renal mesangial cells, endothelial cells, breast (MCF-7) and colon (HCT 116) carcinoma cells, wild type SPL from Symbiobacterium thermophilum disrupts MAPK phosphorylation stimulated by exogenous sphingosine 1-phosphate. Under in vivo conditions SPL from Symbiobacterium thermophilum inhibits tumor cell-induced angiogenesis as an sphingosine 1-phosphate-dependent process
physiological function
-
SPL contributes to oxidative stress by depleting sphingosine 1-phosphate pools available for cardioprotective signaling
physiological function
-
SPL is the final enzyme in the sphingolipid degradative pathway and an important regulator of sphingosine 1-phosphate as well as the levels of other sphingolipid intermediates which influence various aspects of cell growth, proliferation and death. SPL is necessary for maintaining lipid homeostasis and appropriate cell fate responses. SPL serves as a therapeutic target for immune modulation
physiological function
-
SPL is the final enzyme in the sphingolipid degradative pathway and an important regulator of sphingosine 1-phosphate as well as the levels of other sphingolipid intermediates which influence various aspects of cell growth, proliferation and death. SPL is necessary for maintaining lipid homeostasis and appropriate cell fate responses. SPL serves as a therapeutic target for immune modulation
physiological function
SPL is the final enzyme in the sphingolipid degradative pathway and an important regulator of sphingosine 1-phosphate as well as the levels of other sphingolipid intermediates which influence various aspects of cell growth, proliferation and death. SPL is necessary for maintaining lipid homeostasis and appropriate cell fate responses. SPL serves as a therapeutic target for immune modulation
physiological function
-
SPL modulates the kinetics of DNA repair, speed of recovery from G2 cell cycle arrest and the extent of apoptosis after ionizing radiation. SPL expression affects the Cdk1-cyclin B complex
physiological function
-
SPL plays a crucial role in the migration of T-cells from lymphoid tissues by maintaining the sphingosine 1-phosphate gradient necessary for T-cells to egress from the lymph nodes into the blood stream. SPL plays a central role in neutrophil egress from blood to tissues. SPL is a central and crucial regulator of lipid homeostasis. SPL activity is linked to an increase in CER levels in response to stress factors and is involved in apoptosis
physiological function
a myoblast sphingosine-1-phosphate lyase-knockdown cell accumulates intracellular and extracellular sphingosine-1-phosphate and fails to form myotubes under conditions that normally stimulate myogenic differentiation. Under differentiation conditions, knockdown cells also demonstrate delayed induction of myogenic microRNAs, miR-1, miR-206, and miR-486. Knockdown cells successfully differentiate when treated with an S1P1 agonist, S1P2 antagonist, and combination treatments, which also increase myogenic miRNA levels. Knockdown cells transfected with mimics for miR-1 or miR-206 also overcome the differentiation block
physiological function
-
in C4-2B and PC-3 cells, silencing of sphingosine 1-phosphate lyase enhances survival after irradiation or chemotherapy by decreasing expression of proteins involved in sensing and repairing DNA damage or apoptosis, respectively. Enforced expression of sphingosine 1-phosphate lyase sensitizes cancer cells to irradiation or docetaxel by tilting the ceramide/sphingosine 1-phosphate balance toward cell death
physiological function
-
inducible sphingosine-1-phosphate lyase knockout mice featuring partial reduction of sphingosine-1-phosphate lyase activity are viable but feature profound reduction of peripheral T cells, similar to the constitutive knockout mice. While thymic T cell development in these mice appears normal, mature T cells are retained in thymus and lymph nodes, leading to reduced T cell numbers in spleen and blood, with a skewing towards increased proportions of memory T cells and T regulatory cells. The inducible knockout mice are protected in experimental autoimmune encephalomyelitis. T cell immigration into the CNS is profoundly reduced
physiological function
-
silencing or inhibition of sphingosine-1-phosphate lyase with short interfering RNA or active site-directed inhibitors in cultured mammalian cells does not cause a relevant increase of sphingosine-1-phosphate in the cells. The addition of sphingosine to cultures of cell lines or primary cells provides a source of intracellular sphingosine-1-phosphate that is susceptible to degradation by the lyase and, hence, increases on inhibition or silencing of the enzyme
physiological function
-
sphingosine phosphate lyase knockdown via short hairpin RNA in embryonic stem cells shows a 5fold increase in cellular sphingosine 1-phosphate levels, increased proliferation rates and high expression of cell surface pluripotency markers SSEA1 and OCT4 compared to vector control cells. Knockdown cells show robust activation of STAT3 and a 10fold increase in S1P2 expression. Inhibition of S1P2 or STAT3 reverses the proliferation and pluripotency phenotypes of knockdown cells. Inhibition of S1P2 attenuates, in a dose-dependent fashion, the high levels of OCT4 and STAT3 activation. Knockdown cells are capable of generating embryoid bodies from which muscle stem cells, called satellite cells, can be isolated
physiological function
-
enzyme expression in mature T cells contributes to efficient thymic egress
physiological function
-
enzyme overexpression reduces cytokine-induced endoplasmic reticulum stress, regulates Ca2+ homeostasis and Bcl2-associated death promotor phosphorylation in INS1E cells, and protects against cytokine-mediated inhibition of cell proliferation and caspase-3 activation in insulin-secreting INS1E cells
physiological function
-
the enzyme plays a critical role in virulence and is required for intracellular survival
physiological function
-
the enzyme plays a critical role in virulence and is required for intracellular survival
physiological function
-
the enzyme plays a critical role in virulence and is required for intracellular survival
-
Show AA Sequence and Transmembrane Helices (114 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
59480
61000 - 65000
63500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer or hexamer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) polypropylene glycol 400 and 10% (v/v) 1-propanol
in complex with (R)-6-(4-(4-benzyl-7-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl)nicotinonitrile, hanging drop vapor diffusion method
sitting drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K271A
C344A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
C65L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
C65L/K67L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
C65L/K67L/S70L/N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-16
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-31
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-31/C65L/K67L/S70L/N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-54
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-57
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-81
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
H268A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
H340A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K380A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K386A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K67L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K67L/S70L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
N6A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
S70L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
S70L/N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
Y554A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
Y554F
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
additional information
-
enzyme null mutant, exhibits dihydrosphingosine-1-phosphate lyase activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable towards Triton X-100 and no significant inhibition of the enzyme is observed up to a concentration of 15 mg/ml
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Superdex S-200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Saccharomyces cerevisiae
fusion protein with green fluorescence protein, expressed in HEK293 cells
fusion protein with green fluorescence protein, expressed in Saccharomyces cerevisiae
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
basal SPL activity is low in wild type cardiac tissue but is activated 3fold in response to 50 min of ischemia
-
enzyme expression is down-regulated in rice plants after treatments with salicylic acid, benzothiadiazole and 1-amino cyclopropane-1-carboxylic acid
-
enzyme expression is induced by infection with a virulent strain of Magnaporthe oryzae
-
high SPL transcription of H1155 cells is regulated by specificity protein 1 and GATA-4 protein/specificity protein 1 complex formation
-
mRNA expression for both sphingosine kinase and sphingosine 1-phosphate lyase are up-regulated throughout all four stages in human breast cancer patients. Exogenous administration of S1P produces a bell-shaped dose response for apoptosis in normal mammary gland MCF12A cells but a sigmoid-shaped apoptotic response in breast cancer MCF7 cells. Co-administration of S1P enhances the cytotoxicity of anticancer drug docetaxel against MCF7 cells
-
SGPL1 gene expression is downregulated in colon cancer and is upregulated in certain malignant tissues, for example, in ovarian cancers as well as in the skin of patients suffering from atopic dermatitis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
analysis
-
use of BODIPY-labeled sphinganine substrate, allows fluorescent product detection by HPLC. The reaction is linear over a 30 min time period
analysis
-
easy and sensitive procedure to determine sphingosine-1-phosphate lyase activity. The assay uses C17-sphinganine-1-phosphate as substrate and the aldehyde product, pentadecanal, is quantified as its pentafluorobenzyloxime derivative by GC/MS. Derivatization of pentadecanal is performed as a one-step reaction, and the oxime product is directly injected for GC/MS analysis without any further purification. Limit of detection is 281 fmol. The assay is linear with both protein concentration and incubation time up to 20 microg and 40 min, respectively
analysis
-
the addition of sphingosine to cultures of cell lines or primary cells provides a source of intracellular sphingosine 1-phosphate that is susceptible to degradation by the lyase and, hence, increases on inhibition or silencing of the enzyme. Development of a biochemical assay optimized with respect to sphingosine concentration, incubation time, and cell density and establishment for routine use with HEK293 cells. The assay is suitable for the testing of novel active site-directed sphongosine-1-phosphate lyase inhibitors
medicine
-
some effects of immune modulator FTY720 are due to disruption of sphingosine-1-phosphate metabolism
medicine
-
some effects of immune modulator FTY720 are due to disruption of sphingosine-1-phosphate metabolism
medicine
all S1PL-deficient genetic models used display lymphopenia, with sequestration of mature T-cells in the thymus and lymph nodes. In addition to the lymphoid phenotypes, S1PL KO mice also develop myeloid cell hyperplasia and significant lesions in the lung, heart, urinary tract, and bone, and have a markedly reduced life span. Complete absence of S1PL affects both maturation/development and egress of mature T cells from the thymus, whereas low level S1PL activity affects T-cell egress more than differentiation
medicine
-
complete loss of SPL activity leads to upregulation of the antiapoptotic proteins Bcl-2 and Bcl-xL and consequently protects against apoptosis induced by chemotherapy and nutrient starvation but not against autophagy
medicine
-
following the oral administration of 10 and 100 mg/kg 2-acetyl-4(5)-tetrahydroxybutyl imidazole to male rats, 2-acetyl-4(5)-tetrahydroxybutyl imidazole is rapidly absorbed and reaches a plasma peak level at 1 h post-dosing. Splenic S1P increases and reaches the peak level at 24 h. Blood lymphocyte count decreases as the splenic S1P level increases. 2-Acetyl-4(5)-tetrahydroxybutyl imidazole plasma concentration is linked to splenic S1P concentration using an indirect model incorporated with a four-step signal transduction model. In turn, the S1P level is directly coupled with blood lymphocyte number
medicine
-
humanized knock-in mice harboring one allele such as S1PLH/- or two alleles such as S1PLH/H of human S1PL express less than 10 and 20% of normal S1PL activity, respectively. This partial restoration of S1PL activity is sufficient to fully protect both humanized mouse lines from the lethal non-lymphoid lesions that develop in S1PL-/- mice, but fails to restore normal T-cell development and trafficking. The complete absence of S1PL affects both maturation/development and egress of mature T-cells from the thymus, whereas low level S1PL activity affects T-cell egress more than differentiation
medicine
-
incubation of lyase-deficient neurons with either sphingosine or S1P results in a similar elevation in cellular S1P, but only S1P addition to the culture medium induces apoptosis. This is not due to S1P acting on the S1P receptor but to hydrolysis of S1P to sphingosine that is phosphorylated by the cells. Although the cells produce S1P from both exogenously added sphingosine as well as sphingosine derived from exogenous S1P, the S1P from these two sources are not equivalent, because the former is primarily produced by SK1, whereas the latter is mainly formed by sphingosine kinase-2
medicine
-
mRNA expression for both sphingosine kinase and sphingosine 1-phosphate lyase are up-regulated throughout all four stages in human breast cancer patients
medicine
-
thymocyte development in SGPL1-deficient mice which exhibit postnatal discontinuation of early thymocytopoies is starting at 2 weeks after birth. SGPL-/- thymi show a loss of developing thymocytes in the thymic cortex between 2 and 4 weeks of age, whereas mature thymocytes accumulate in the medulla. Increased ceramide levels in the thymus of SGPL1-/- mice abrogates thymic development postnatally by enhanced thymocyte apoptosis and depletion of thymic ETP. Potentially therapeutic immunosuppression by SGPL1 inhibition should benefit from monitoring ceramides to prevent their increase to apoptosis-inducing levels
medicine
-
S1P lyase is a therapeutic target for ischemia-reperfusion injury of the heart
medicine
-
in fresh human prostatectomy specimens, a remarkable decrease in sphingosine 1-phosphate lyase enzymatic activity is found in tumor samples, as compared with normal adjacent tissues. A significant relationship between loss of sphingosine 1-phosphate lyase expression and higher Gleason score is confirmed. Sphingosine 1-phosphate lyase protein expression and activity are inversely correlated with those of sphingosine kinase-1, the enzyme producing sphingosine 1-phosphate. Sphingosine 1-phosphate lyase and sphingosine kinase expressions are independently predictive of aggressive cancer on tissue microarray
medicine
-
inducible sphingosine-1-phosphate lyase knockout mice featuring partial reduction of sphingosine-1-phosphate lyase activity are viable but feature profound reduction of peripheral T cells, similar to the constitutive knockout mice. While thymic T cell development in these mice appears normal, mature T cells are retained in thymus and lymph nodes, leading to reduced T cell numbers in spleen and blood, with a skewing towards increased proportions of memory T cells and T regulatory cells. The inducible knockout mice are protected in experimental autoimmune encephalomyelitis. T cell immigration into the CNS is profoundly reduced
medicine
-
inhibition of sphingosine-1-phosphate lyase activity rendes sphingosine 1-phosphate an efficient S1P1 receptor internalizing compound and abrogated sphingosine-1-phosphate-mediated sustained signaling, suggesting that sphingosine-1-phosphate lyase by facilitating S1P1 receptor recycling is essential for sphingosine-1-phosphate-mediated sustained signaling, and that synthetic agonists are functional antagonists because they are not sphingosine-1-phosphate lyase substrates
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stoffel, W.; Lekim, D; Stich, G.
Distribution and properties of dihydrosphingosine-1-phosphate aldolase (Sphinganine-1-phosphate alkanal-lyase)
Hoppe-Seyler's Z. Physiol. Chem.
350
1233-1241
1969
Bos taurus, Wickerhamomyces ciferrii, Rattus norvegicus, Sus scrofa
brenda
Shimojo, T.; Akino, T.; Miura, Y.; Schroepfer, G.J
Shingolipid base metabolism
J. Biol. Chem.
251
4448-4457
1976
Rattus norvegicus
brenda
Shimojo, T; Schroepfer, Jr., G.J.
Sphingolipid base metabolism Sphinganine-1-phosphate lyase: Identification of ethanolamine 1-phosphate as product
Biochim. Biophys. Acta
431
433-446
1976
Rattus norvegicus
brenda
Stoffel, W.; Grol, M.
Chemistry and biochemistry of 1-desoxysphinganine 1-phosphonate (dihydrosphingosine-1-phosphonate)
Chem. Phys. Lipids
13
372-388
1974
Rattus norvegicus, Tetrahymena pyriformis
brenda
Stoffel, W.; Assmann, G.
Degradation in vitro of phytosphingosine (4D-Hydroxysphinganine)
Hoppe-Seyler's Z. Physiol. Chem.
353
965-970
1972
Rattus norvegicus
brenda
Akino, T.; Shimojo, Y.; Schroepfer, Jr., G.J.
Stereospecificity of proton uptake in the enzymatic conversion of sphinganine 1-phosphate to ethanolamine 1-phosphate
J. Am. Chem. Soc.
96
939-940
1974
Rattus norvegicus
brenda
Van Veldhoven, P.P.; Mannaerts, G.P
Subcellular localisation and membrane topology of sphingosine-1-phosphate lyase in rat liver
J. Biol. Chem.
266
12502-12507
1991
Rattus norvegicus
brenda
Van Veldhoven, P.P.
Sphingosine-phosphate lyase
Adv. Lipid Res.
26
69-98
1993
Canis lupus familiaris, Cavia porcellus, Homo sapiens, Platyrrhini, Mus musculus, Rattus norvegicus, Sus scrofa, Tetrahymena pyriformis
brenda
Van Veldhoven, P.P.; Mannaerts, G.P.
Sphinganine 1-phosphate metabolism in cultured skin fibroblasts: evidence for the existence of a sphingosine phosphatase
Biochem. J.
299
597-601
1994
Canis lupus familiaris, Homo sapiens
brenda
Saba, J.D.; Nara, F.; Bielawska, A.; Garrett, S.; Hannun, Y.A.
The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase
J. Biol. Chem.
272
26087-26090
1997
Saccharomyces cerevisiae
brenda
Zhou, J.; Saba, J.D.
Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast
Biochem. Biophys. Res. Commun.
242
502-507
1998
Mus musculus (Q8R0X7), Mus musculus
brenda
Van Veldhoven, P.P.; Gijsbers, S.; Mannaerts, G.P.; Vermeesch, J.R.; Brys, V.
Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q221
Biochim. Biophys. Acta
1487
128-134
2000
Homo sapiens (O95470), Homo sapiens
brenda
Li, G.; Foote, C.; Alexander, S.; Alexander, H.
Sphingosine-1-phosphate lyase has a central role in the development of Dictyostelium discoideum
Development
128
3473-3483
2001
Dictyostelium discoideum (Q54RV9), Dictyostelium discoideum
brenda
Kihara, A.; Ikeda, M.; Kariya, Y.; Lee, E.Y.; Lee, Y.M.; Igarashi, Y.
Sphingosine-1-phosphate lyase is involved in the differentiation of F9 embryonal carcinoma cells to primitive endoderm
J. Biol. Chem.
278
14578-14585
2003
Mus musculus
brenda
Mendel, J.; Heinecke, K.; Fyrst, H.; Saba, J.D.
Sphingosine phosphate lyase expression is essential for normal development in Caenorhabditis elegans
J. Biol. Chem.
278
22341-22349
2003
Caenorhabditis elegans
brenda
Reiss, U.; Oskouian, B.; Zhou, J.; Gupta, V.; Sooriyakumaran, P.; Kelly, S.; Wang, E.; Merrill, A.H., Jr.; Saba, J.D.
Sphingosine-phosphate lyase enhances stress-induced ceramide generation and apoptosis
J. Biol. Chem.
279
1281-1290
2004
Homo sapiens (O95470), Homo sapiens
brenda
Van Veldhoven, P.P.
Sphingosine-1-phosphate lyase
Methods Enzymol.
311
244-254
2000
Homo sapiens, Mammalia, Mus musculus, Rattus norvegicus, Tetrahymena pyriformis
brenda
Ikeda, M.; Kihara, A.; Igarashi, Y.
Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5'-phosphate binding domain exposed to the cytosol
Biochem. Biophys. Res. Commun.
325
338-343
2004
Mus musculus
brenda
Ikeda, M.; Kihara, A.; Kariya, Y.; Lee, Y.M.; Igarashi, Y.
Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme
Biochem. Biophys. Res. Commun.
329
474-479
2005
Mus musculus
brenda
Bandhuvula, P.; Tam, Y.Y.; Oskouian, B.; Saba, J.D.
The immune modulator FTY720 inhibits sphingosine-1-phosphate lyase activity
J. Biol. Chem.
280
33697-33700
2005
Homo sapiens, Mus musculus
brenda
Min, J.; Van Veldhoven, P.P.; Zhang, L.; Hanigan, M.H.; Alexander, H.; Alexander, S.
Sphingosine-1-phosphate lyase regulates sensitivity of human cells to select chemotherapy drugs in a p38-dependent manner
Mol. Cancer Res.
3
287-296
2005
Homo sapiens
brenda
Kim, D.H.; Lee, Y.S.; Lee, Y.M.; Oh, S.; Yun, Y.P.; Yoo, H.S.
Elevation of sphingoid base 1-phosphate as a potential contributor to hepatotoxicity in fumonisin B1-exposed mice
Arch. Pharm. Res.
30
962-969
2007
Mus musculus
brenda
Miyazaki, Y.; Hiraide, M.; Shibuya, H.
Molecular cloning of functional genes for high growth-temperature and salt tolerance of the basidiomycete Fomitopsis pinicola isolated in a mangrove forest in Micronesia
Biosci. Biotechnol. Biochem.
71
273-278
2007
Fomitopsis pinicola, Fomitopsis pinicola 130-2
brenda
Peest, U.; Sensken, S.C.; Andreani, P.; Haenel, P.; Van Veldhoven, P.P.; Graeler, M.H.
S1P-lyase independent clearance of extracellular sphingosine 1-phosphate after dephosphorylation and cellular uptake
J. Cell. Biochem.
104
756-772
2008
Homo sapiens
brenda
Niu, Y.; Chen, K.; Wang, J.; Liu, X.; Qin, H.; Zhang, A.; Wang, D.
Molecular and functional characterization of sphingosine-1-phosphate lyase homolog from higher plants
J. Integr. Plant Biol.
49
323-335
2007
Oryza sativa, Arabidopsis thaliana (Q9C509)
-
brenda
Bandhuvula, P.; Fyrst, H.; Saba, J.D.
A rapid fluorescence assay for sphingosine-1-phosphate lyase enzyme activity
J. Lipid Res.
48
2769-2778
2007
Homo sapiens, Mus musculus
brenda
Oskouian, B.; Sooriyakumaran, P.; Borowsky, A.D.; Crans, A.; Dillard-Telm, L.; Tam, Y.Y.; Bandhuvula, P.; Saba, J.D.
Sphingosine-1-phosphate lyase potentiates apoptosis via p53- and p38-dependent pathways and is down-regulated in colon cancer
Proc. Natl. Acad. Sci. USA
103
17384-17389
2006
Homo sapiens, Mus musculus
brenda
Bandhuvula, P.; Saba, J.D.
Sphingosine-1-phosphate lyase in immunity and cancer: silencing the siren
Trends Mol. Med.
13
210-217
2007
Caenorhabditis elegans, Dictyostelium discoideum, Drosophila melanogaster, Homo sapiens, Leishmania major, Mus musculus, Rattus norvegicus
brenda
Mukhopadhyay, D.; Howell, K.S.; Riezman, H.; Capitani, G.
Identifying key residues of sphinganine-1-phosphate lyase for function in vivo and in vitro
J. Biol. Chem.
283
20159-20169
2008
Saccharomyces cerevisiae (Q05567)
brenda
Colie, S.; Codogno, P.; Levade, T.; Andrieu-Abadie, N.
Regulation of cell death by sphingosine 1-phosphate lyase
Autophagy
6
426-427
2010
Mus musculus
brenda
Bandhuvula, P.; Li, Z.; Bittman, R.; Saba, J.D.
Sphingosine 1-phosphate lyase enzyme assay using a BODIPY-labeled substrate
Biochem. Biophys. Res. Commun.
380
366-370
2009
Homo sapiens
brenda
Dunlap, K.A.; Kwak, H.I.; Burghardt, R.C.; Bazer, F.W.; Magness, R.R.; Johnson, G.A.; Bayless, K.J.
The sphingosine 1-phosphate (S1P) signaling pathway is regulated during pregnancy in sheep
Biol. Reprod.
82
876-887
2010
Ovis aries
brenda
Claas, R.F.; ter Braak, M.; Hegen, B.; Hardel, V.; Angioni, C.; Schmidt, H.; Jakobs, K.H.; Van Veldhoven, P.P.; zu Heringdorf, D.M.
Enhanced Ca2+ storage in sphingosine-1-phosphate lyase-deficient fibroblasts
Cell. Signal.
22
476-483
2010
Mus musculus
brenda
Ling, B.; Chen, L.; Alcorn, J.; Ma, B.; Yang, J.
Sphingosine-1-phosphate: a potential therapeutic agent against human breast cancer
Invest. New Drugs
29
396-399
2009
Homo sapiens
brenda
Hagen, N.; Van Veldhoven, P.P.; Proia, R.L.; Park, H.; Merrill, A.H.; van Echten-Deckert, G.
Subcellular origin of sphingosine 1-phosphate is essential for its toxic effect in lyase-deficient neurons
J. Biol. Chem.
284
11346-11353
2009
Mus musculus
brenda
Bektas, M.; Allende, M.L.; Lee, B.G.; Chen, W.; Amar, M.J.; Remaley, A.T.; Saba, J.D.; Proia, R.L.
Sphingosine 1-phosphate lyase deficiency disrupts lipid homeostasis in liver
J. Biol. Chem.
285
10880-10889
2010
Mus musculus
brenda
Weber, C.; Krueger, A.; Muenk, A.; Bode, C.; Van Veldhoven, P.P.; Graeler, M.H.
Discontinued postnatal thymocyte development in sphingosine 1-phosphate-lyase-deficient mice
J. Immunol.
183
4292-4301
2009
Mus musculus
brenda
Bagdanoff, J.T.; Donoviel, M.S.; Nouraldeen, A.; Tarver, J.; Fu, Q.; Carlsen, M.; Jessop, T.C.; Zhang, H.; Hazelwood, J.; Nguyen, H.; Baugh, S.D.; Gardyan, M.; Terranova, K.M.; Barbosa, J.; Yan, J.; Bednarz, M.; Layek, S.; Courtney, L.F.; Taylor, J.; Digeorge-Foushee, A.M.; Gopinathan, S.; Bruce, D.; Smi, S.m.i.t.
Inhibition of sphingosine-1-phosphate lyase for the treatment of autoimmune disorders
J. Med. Chem.
52
3941-3953
2009
Mus musculus
brenda
Vogel, P.; Donoviel, M.S.; Read, R.; Hansen, G.M.; Hazlewood, J.; Anderson, S.J.; Sun, W.; Swaffield, J.; Oravecz, T.
Incomplete inhibition of sphingosine 1-phosphate lyase modulates immune system function yet prevents early lethality and non-lymphoid lesions
PLoS ONE
4
e4112
2009
Homo sapiens, Mus musculus (Q8R0X7), Mus musculus
brenda
Yu, X.Q.; Kramer, J.; Moran, L.; ONeill, E.; Nouraldeen, A.; Oravecz, T.; Wilson, A.G.
Pharmacokinetic/pharmacodynamic modelling of 2-acetyl-4(5)-tetrahydroxybutyl imidazole-induced peripheral lymphocyte sequestration through increasing lymphoid sphingosine 1-phosphate
Xenobiotica
40
350-356
2010
Rattus norvegicus
brenda
Serra, M.; Saba, J.
Sphingosine 1-phosphate lyase, a key regulator of sphingosine 1-phosphate signaling and function
Adv. Enzyme Regul.
50
349-362
2010
Homo sapiens, Rattus norvegicus, Mus musculus (Q8R0X7)
brenda
Bandhuvula, P.; Honbo, N.; Wang, G.Y.; Jin, Z.Q.; Fyrst, H.; Zhang, M.; Borowsky, A.D.; Dillard, L.; Karliner, J.S.; Saba, J.D.
S1P lyase: a novel therapeutic target for ischemia-reperfusion injury of the heart
Am. J. Physiol. Heart Circ. Physiol.
300
H1753-H1761
2011
Mus musculus
brenda
Berdyshev, E.V.; Goya, J.; Gorshkova, I.; Prestwich, G.D.; Byun, H.S.; Bittman, R.; Natarajan, V.
Characterization of sphingosine-1-phosphate lyase activity by electrospray ionization-liquid chromatography/tandem mass spectrometry quantitation of (2E)-hexadecenal
Anal. Biochem.
408
12-18
2011
Mus musculus
brenda
Ito, H.; Yoshida, K.; Murakami, M.; Hagiwara, K.; Sasaki, N.; Kobayashi, M.; Takagi, A.; Kojima, T.; Sobue, S.; Suzuki, M.; Tamiya-Koizumi, K.; Nakamura, M.; Banno, Y.; Nozawa, Y.; Murate, T.
Heterogeneous sphingosine-1-phosphate lyase gene expression and its regulatory mechanism in human lung cancer cell lines
Biochim. Biophys. Acta
1811
119-128
2011
Homo sapiens
brenda
Kumar, A.; Oskouian, B.; Fyrst, H.; Zhang, M.; Paris, F.; Saba, J.D.
S1P lyase regulates DNA damage responses through a novel sphingolipid feedback mechanism
Cell Death Dis.
2
e119
2011
Mus musculus
brenda
Berdyshev, E.V.; Gorshkova, I.; Usatyuk, P.; Kalari, S.; Zhao, Y.; Pyne, N.J.; Pyne, S.; Sabbadini, R.A.; Garcia, J.G.; Natarajan, V.
Intracellular S1P generation is essential for S1P-induced motility of human lung endothelial cells: role of sphingosine kinase 1 and S1P lyase
PLoS ONE
6
e16571
2011
Homo sapiens
brenda
Huwiler, A.; Bourquin, F.; Kotelevets, N.; Pastukhov, O.; Capitani, G.; Gruetter, M.G.; Zangemeister-Wittke, U.
A prokaryotic S1P lyase degrades extracellular S1P in vitro and in vivo: implication for treating hyperproliferative disorders
PLoS ONE
6
e22436
2011
Symbiobacterium thermophilum
brenda
Bourquin, F.; Capitani, G.; Gruetter, M.G.
PLP-dependent enzymes as entry and exit gates of sphingolipid metabolism
Protein Sci.
20
1492-1508
2011
Saccharomyces cerevisiae, Homo sapiens, Myxococcus xanthus, Symbiobacterium thermophilum
brenda
Bourquin, F.; Riezman, H.; Capitani, G.; Gruetter, M.G.
Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism
Structure
18
1054-1065
2010
Saccharomyces cerevisiae, Homo sapiens (O95470), Homo sapiens, Symbiobacterium thermophilum (Q67PY4), Symbiobacterium thermophilum
brenda
Billich, A.; Beerli, C.; Bergmann, R.; Bruns, C.; Loetscher, E.
Cellular assay for the characterization of sphingosine-1-phosphate lyase inhibitors
Anal. Biochem.
434
247-253
2013
Homo sapiens
brenda
Smith, G.S.; Kumar, A.; Saba, J.D.
Sphingosine phosphate lyase regulates murine embryonic stem cell proliferation and pluripotency through an S1P2/STAT3 signaling pathway
Biomolecules
3
351-368
2013
Mus musculus
brenda
Gatfield, J.; Monnier, L.; Studer, R.; Bolli, M.H.; Steiner, B.; Nayler, O.
Sphingosine-1-phosphate (S1P) displays sustained S1P1 receptor agonism and signaling through S1P lyase-dependent receptor recycling
Cell. Signal.
26
1576-1588
2014
Homo sapiens
brenda
Reina, E.; Camacho, L.; Casas, J.; Van Veldhoven, P.P.; Fabrias, G.
Determination of sphingosine-1-phosphate lyase activity by gas chromatography coupled to electron impact mass spectrometry
Chem. Phys. Lipids
165
225-231
2012
Mus musculus
brenda
Park, S.M.; Angel, C.E.; McIntosh, J.D.; Brooks, A.E.; Middleditch, M.; Chen, C.J.; Ruggiero, K.; Cebon, J.; Dunbar, P.R.
Sphingosine-1-phosphate lyase is expressed by CD68(+) cells on the parenchymal side of marginal reticular cells in human lymph nodes
Eur. J. Immunol.
44
2425-2436
2014
Homo sapiens
brenda
de la Garza-Rodea, A.S.; Baldwin, D.M.; Oskouian, B.; Place, R.F.; Bandhuvula, P.; Kumar, A.; Saba, J.D.
Sphingosine phosphate lyase regulates myogenic differentiation via S1P receptor-mediated effects on myogenic microRNA expression
FASEB J.
28
506-519
2014
Mus musculus (Q8R0X7), Mus musculus
brenda
Borowsky, A.D.; Bandhuvula, P.; Kumar, A.; Yoshinaga, Y.; Nefedov, M.; Fong, L.G.; Zhang, M.; Baridon, B.; Dillard, L.; de Jong, P.; Young, S.G.; West, D.B.; Saba, J.D.
Sphingosine-1-phosphate lyase expression in embryonic and adult murine tissues
J. Lipid Res.
53
1920-1931
2012
Mus musculus
brenda
Brizuela, L.; Ader, I.; Mazerolles, C.; Bocquet, M.; Malavaud, B.; Cuvillier, O.
First evidence of sphingosine 1-phosphate lyase protein expression and activity downregulation in human neoplasm: implication for resistance to therapeutics in prostate cancer
Mol. Cancer Ther.
11
1841-1851
2012
Homo sapiens
brenda
Billich, A.; Baumruker, T.; Beerli, C.; Bigaud, M.; Bruns, C.; Calzascia, T.; Isken, A.; Kinzel, B.; Loetscher, E.; Metzler, B.; Mueller, M.; Nuesslein-Hildesheim, B.; Kleylein-Sohn, B.
Partial deficiency of sphingosine-1-phosphate lyase confers protection in experimental autoimmune encephalomyelitis
PLoS ONE
8
e59630
2013
Mus musculus
brenda
Ceccom, J.; Loukh, N.; Lauwers-Cances, V.; Touriol, C.; Nicaise, Y.; Gentil, C.; Uro-Coste, E.; Pitson, S.; Maurage, C.A.; Duyckaerts, C.; Cuvillier, O.; Delisle, M.B.
Reduced sphingosine kinase-1 and enhanced sphingosine 1-phosphate lyase expression demonstrate deregulated sphingosine 1-phosphate signaling in Alzheimers disease
Acta Neuropathol. Commun.
2
12
2014
Homo sapiens
brenda
Dinges, J.; Harris, C.M.; Wallace, G.A.; Argiriadi, M.A.; Queeney, K.L.; Perron, D.C.; Dominguez, E.; Kebede, T.; Desino, K.E.; Patel, H.; Vasudevan, A.
Hit-to-lead evaluation of a novel class of sphingosine 1-phosphate lyase inhibitors
Bioorg. Med. Chem. Lett.
26
2297-2302
2016
Homo sapiens
brenda
Sanllehi, P.; Casasampere, M.; Abad, J.L.; Fabrias, G.; Lopez, O.; Bujons, J.; Casas, J.; Delgado, A.
The first fluorogenic sensor for sphingosine-1-phosphate lyase activity in intact cells
Chem. Commun. (Camb.)
53
5441-5444
2017
Homo sapiens (O95470)
brenda
Suh, J.H.; Eltanawy, A.; Rangan, A.; Saba, J.D.
A facile stable-isotope dilution method for determination of sphingosine phosphate lyase activity
Chem. Phys. Lipids
194
101-109
2016
Homo sapiens, Mus musculus
brenda
Sanllehi, P.; Abad, J.L.; Casas, J.; Delgado, A.
Inhibitors of sphingosine-1-phosphate metabolism (sphingosine kinases and sphingosine-1-phosphate lyase)
Chem. Phys. Lipids
197
69-81
2016
Homo sapiens
brenda
Sanllehi, P.; Abad, J.L.; Bujons, J.; Casas, J.; Delgado, A.
Studies on the inhibition of sphingosine-1-phosphate lyase by stabilized reaction intermediates and stereodefined azido phosphates
Eur. J. Med. Chem.
123
905-915
2016
Homo sapiens, Symbiobacterium thermophilum
brenda
Hahn, C.; Tyka, K.; Saba, J.D.; Lenzen, S.; Gurgul-Convey, E.
Overexpression of sphingosine-1-phosphate lyase protects insulin-secreting cells against cytokine toxicity
J. Biol. Chem.
292
20292-20304
2017
Rattus norvegicus
brenda
Zamora-Pineda, J.; Kumar, A.; Suh, J.H.; Zhang, M.; Saba, J.D.
Dendritic cell sphingosine-1-phosphate lyase regulates thymic egress
J. Exp. Med.
213
2773-2791
2016
Mus musculus
brenda
McLean, C.J.; Marles-Wright, J.; Custodio, R.; Lowther, J.; Kennedy, A.J.; Pollock, J.; Clarke, D.J.; Brown, A.R.; Campopiano, D.J.
Characterization of homologous sphingosine-1-phosphate lyase isoforms in the bacterial pathogen Burkholderia pseudomallei
J. Lipid Res.
58
137-150
2017
Burkholderia pseudomallei (Q63IP8), Burkholderia pseudomallei, Burkholderia pseudomallei K96243 (Q63IP8), Burkholderia pseudomallei K96243
brenda
Weiler, S.; Braendlin, N.; Beerli, C.; Bergsdorf, C.; Schubart, A.; Srinivas, H.; Oberhauser, B.; Billich, A.
Orally active 7-substituted [(4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]nicotinonitriles as active-site inhibitors of sphingosine 1-phosphate lyase for the treatment of multiple sclerosis
J. Med. Chem.
57
5074-5084
2014
Homo sapiens (O95470), Homo sapiens
brenda
Ohtoyo, M.; Tamura, M.; Machinaga, N.; Muro, F.; Hashimoto, R.
Sphingosine 1-phosphate lyase inhibition by 2-acetyl-4-(tetrahydroxybutyl)imidazole (THI) under conditions of vitamin B6 deficiency
Mol. Cell. Biochem.
400
125-133
2015
Mus musculus
brenda
Custodio, R.; McLean, C.J.; Scott, A.E.; Lowther, J.; Kennedy, A.; Clarke, D.J.; Campopiano, D.J.; Sarkar-Tyson, M.; Brown, A.R.
Characterization of secreted sphingosine-1-phosphate lyases required for virulence and intracellular survival of Burkholderia pseudomallei
Mol. Microbiol.
102
1004-1019
2016
Burkholderia pseudomallei, Burkholderia thailandensis, Burkholderia pseudomallei K96243
brenda
Zhang, H.; Jin, X.; Huang, L.; Hong, Y.; Zhang, Y.; Ouyang, Z.; Li, X.; Song, F.; Li, D.
Molecular characterization of rice sphingosine-1-phosphate lyase gene OsSPL1 and functional analysis of its role in disease resistance response
Plant Cell Rep.
33
1745-1756
2014
Oryza sativa
brenda
Abu Khweek, A.; Kanneganti, A.; Guttridge D, D.C.; Amer, A.O.
The sphingosine-1-phosphate lyase (LegS2) contributes to the restriction of Legionella pneumophila in murine macrophages
PLoS ONE
11
e0146410
2016
Legionella pneumophila, Legionella pneumophila JR32
brenda
Schuemann, J.; Grevot, A.; Ledieu, D.; Wolf, A.; Schubart, A.; Piaia, A.; Sutter, E.; Cote, S.; Beerli, C.; Pognan, F.; Billich, A.; Moulin, P.; Walker, U.J.
Reduced activity of sphingosine-1-phosphate lyase induces podocyte-related glomerular proteinuria, skin irritation, and platelet activation
Toxicol. Pathol.
43
694-703
2015
Mus musculus, Rattus norvegicus
brenda
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