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Information on EC 3.5.1.23 - ceramidase
for references in articles please use BRENDA:EC3.5.1.23
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.1 In linear amides
3.5.1.23 ceramidase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.5.1.23
-
adipor1
- sphingolipids
- obesity
-
adipokine
- agonist
- sphingomyelinase
- sphingomyelin
- lysosomal
- farber
-
obese
- leptin
- adipocytes
-
amp-activated
- sphingosine-1-phosphate
- peroxisome
- cardiovascular
-
proliferator-activated
- triglyceride
-
globular
-
insulin-sensitizing
-
high-fat
- tnf
- smases
-
adipocytokine
-
adipocyte-derived
-
monophosphate-activated
-
anti-atherogenic
-
t-cadherin
- steatosis
-
adiposity
- glucosylceramide
- glycosphingolipids
-
obesity-related
-
antidiabetic
- 1-phosphate
-
seven-transmembrane
- gaucher
- dihydrosphingosine
-
p-ampk
- palmitoyltransferase
-
homa-ir
-
sphingoid
- hoarseness
-
ceramide-induced
- sphinganine
-
ceramide-mediated
- dihydroceramide
-
myoclonic
-
adipocyte-secreted
- analysis
- pharmacology
- drug development
- medicine
-
hypoadiponectinemia
showSynonyms
adipor2, adiponectin receptor, ceramidase, acid ceramidase, asah1, neutral ceramidase, acdase, ncdase, acer2, acer3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AC
aCDase
ACER1
ACER2
ACER3
acid ceramidase
acylsphingosine deacylase
-
-
-
-
alkaline ceramidase
alkaline ceramidase 1
alkaline ceramidase 2
alkaline ceramidase 3
ASAH-1
ASAH1
ASAH2
ASAH2B
AtNCER1
CDase
ceramidase
Dacer
Drosophila alkaline ceramidase
glycosphingolipid ceramide deacylase
-
-
-
-
N-acylsphingosine amidohydrolase
N-acylsphingosine amidohydrolase 2
N-acylsphingosine amidohydrolase-1
N-acylsphingosine deacylase
N-CDase
nCDase
ncer1
neutral CDase
neutral ceramidase
PHP32
-
-
-
-
Putative 32 KDA heart protein
-
-
-
-
SA_SCD
SCDase
sphingolipid ceramide N-deacylase
TOD1
turgor regulation defect 1
acid ceramidase
-
-
acid ceramidase
-
ASAH1
-
CDase
-
CDase is the only functional ceramidase present in Drosophila
N-acylsphingosine amidohydrolase
-
-
-
-
neutral ceramidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a ceramide + H2O = a carboxylate + sphingosine
-
-
-
-
a ceramide + H2O = a carboxylate + sphingosine
the enzyme has a catalytic residue Ser354 within a very highly conserved hexapeptide sequence GDVSPN in the middle of a larger conserved sequence, namely NXGDVSPNXXGP/XXC, catalytic mechanism
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
-
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
-
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
-
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
-
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
-
a ceramide + H2O = a carboxylate + sphingosine
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deacylation
hydrolysis
hydrolysis of peptide bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
ceramide and sphingolipid recycling and degradation (yeast), ceramide degradation (generic), ceramide degradation by alpha-oxidation, sphingosine and sphingosine-1-phosphate metabolism
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SYSTEMATIC NAME
IUBMB Comments
N-acylsphingosine amidohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
37289-06-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(13E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]docos-13-enamide + H2O
(13E)-docos-13-enoic acid + 7-[[(3E,5R,6S)-6-amino-5,7-dihydroxyhept-3-en-1-yl]oxy]-2H-1-benzopyran-2-one
Substrates: -
Products: -
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?
(15E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]tetracos-15-enamide + H2O
(15E)-tetracos-15-enoic acid + 7-[[(3E,5R,6S)-6-amino-5,7-dihydroxyhept-3-en-1-yl]oxy]-2H-1-benzopyran-2-one
Substrates: -
Products: -
Products: -
?
(2R)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide + H2O
(2R)-2-hydroxyicosanoic acid + 7-[[(3E,5R,6S)-6-amino-5,7-dihydroxyhept-3-en-1-yl]oxy]-2H-1-benzopyran-2-one
Substrates: -
Products: -
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?
(2R,3Z)-2-([(2E)-1-hydroxy-12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodec-2-en-1-yl]amino)heptadec-3-ene-1,3-diol + H2O
?
Substrates: 9.9% hydrolysis
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ir
(2S)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide + H2O
(2S)-2-hydroxyicosanoic acid + 7-[[(3E,5R,6S)-6-amino-5,7-dihydroxyhept-3-en-1-yl]oxy]-2H-1-benzopyran-2-one
Substrates: -
Products: -
Products: -
?
(4E,2S,3R)-2-N-(10-pyrenedecanoyl)-1,3,17-trihydroxy-17-(3,5-dinitrobenzoyl)-4-heptadecene + H2O
?
-
Substrates: -
Products: fluorescent product formed upon hydrolysis of the N-acyl bond
Products: fluorescent product formed upon hydrolysis of the N-acyl bond
?
(9E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]octadec-9-enamide + H2O
(9E)-octadec-9-enoic acid + 7-[[(3E,5R,6S)-6-amino-5,7-dihydroxyhept-3-en-1-yl]oxy]-2H-1-benzopyran-2-one
Substrates: -
Products: -
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?
11-eicosenoyl-ceramide + H2O
sphingosine + 11-eicosenoic acid
-
Substrates: -
Products: -
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?
11-eicosenoyl-dihydroceramide + H2O
dihydrosphingosine + 11-eicosenoic acid
-
Substrates: -
Products: -
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?
11-eicosenoyl-phytoceramide + H2O
phytosphingosine + 11-eicosenoic acid
-
Substrates: -
Products: -
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?
11-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hept-4-en-2-yl]undecanamide + H2O
?
2,4-dideoxy-2-(hexadecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol + H2O
hexadecanoic acid + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
Substrates: -
Products: -
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?
2,4-dideoxy-2-[[(13E)-docos-13-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol + H2O
(13E)-docos-13-enoic acid + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
Substrates: -
Products: -
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?
2,4-dideoxy-2-[[(2R)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol + H2O
(2R)-2-hydroxyicosanoic acid + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
Substrates: -
Products: -
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?
2,4-dideoxy-2-[[(2S)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol + H2O
(2S)-2-hydroxyicosanoic acid + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
Substrates: -
Products: -
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?
2,4-dideoxy-2-[[(9E)-octadec-9-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol + H2O
(9E)-octadec-9-enoic acid + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
Substrates: -
Products: -
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?
2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-2-[[(15E)-tetracos-15-enoyl]amino]-D-erythro-pentitol + H2O
(15E)-tetracos-15-enoic acid + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
Substrates: -
Products: -
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?
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
4-nitrobenzo-2-oxa-1,3-diazole-N-dodecanoylsphingosine + H2O
?
-
Substrates: -
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?
4-nitrobenzo-2-oxa-1,3-diazole-N-hexanoylsphingosine + H2O
?
-
Substrates: -
Products: -
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?
4-nitrobenzo-2-oxa-1,3-diazoyl-N-dodecanoylsphingosine + H2O
4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid + sphingosine
7-nitrobenz-2-oxa-1,3-diazole-N-lauroylsphingosine + H2O
?
-
Substrates: -
Products: -
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r
C12-NBD-Cer + H2O
NBD-dodecanoic acid + D-erythro-sphingosine
-
Substrates: the enzyme catalyzes also the reverse reaction of ceramide synthesis
Products: -
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r
C18-ceramide + H2O
stearate + sphingosine
Substrates: preferred substrate, fluorescent C18 ceramide in detergent micelles
Products: -
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?
C20:0-ceramide + H2O
arachidic acid + sphingosine
-
Substrates: low activity
Products: -
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?
C20:0-ceramide + H2O
eicosanoic acid + sphingosine
-
Substrates: -
Products: -
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?
C20:1-ceramide + H2O
C20:1 fatty acid + sphingosine
-
Substrates: -
Products: -
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?
C24-ceramide + H2O
C24 fatty acid + sphingosine
Substrates: -
Products: -
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r
C24:0-ceramide + H2O
C24:0 fatty acid + sphingosine
-
Substrates: -
Products: -
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?
C24:0-ceramide + H2O
lignoceric acid + sphingosine
-
Substrates: low activity
Products: -
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?
C24:1-ceramide + H2O
C24:1 fatty acid + sphingosine
-
Substrates: -
Products: -
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?
C2:0-ceramide + H2O
acetate + sphingosine
-
Substrates: low activity
Products: -
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?
ceramide (d18:1/16:0) + H2O
sphingosine + palmitate
Substrates: high activity
Products: -
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?
ceramide (d18:1/18:0) + H2O
sphingosine + stearate
Substrates: high activity
Products: -
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?
ceramide (d18:1/18:1) + H2O
sphingosine + oleate
Substrates: high activity
Products: -
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?
ceramide (d18:1/20:0) + H2O
sphingosine + eicosanate
Substrates: high activity
Products: -
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?
ceramide (d18:1/20:1) + H2O
sphingosine + eicosenate
Substrates: high activity
Products: -
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?
ceramide (d18:1/20:4) + H2O
sphingosine + arachidonate
Substrates: high activity
Products: -
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?
ceramide (d18:1/24:1) + H2O
sphingosine + nervonate
Substrates: high activity
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?
ceramide(d18:0/18:1) + H2O
sphinganine + oleate
Substrates: minor activity
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?
ceramide(d18:0/24:1) + H2O
sphinganine + nervonate
Substrates: minor activity
Products: -
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?
ceramide(d18:1/12:0) + H2O
sphingosine + laurate
Substrates: moderate activity
Products: -
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?
ceramide(d18:1/14:0) + H2O
sphingosine + myristate
Substrates: moderate activity
Products: -
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?
ceramide(d18:1/24:0) + H2O
sphingosine + tetracosanoate
Substrates: moderate activity
Products: -
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?
ceramide(d18:1/2:0) + H2O
sphingosine + acetate
Substrates: minor activity
Products: -
Products: -
?
ceramide(d18:1/6:0) + H2O
sphingosine + hexanoate
Substrates: moderate activity
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?
ceramide(t18:0/18:1) + H2O
phytosphingosine + oleate
Substrates: minor activity
Products: -
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?
ceramide(t18:0/24:1) + H2O
phytosphingosine + nervoate
Substrates: minor activity
Products: -
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?
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
Substrates: -
Products: -
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?
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-phytoceramide + H2O
D-erythro-sphingosine + ?
-
Substrates: substrate activity assay
Products: -
Products: -
?
D-erythro-C12-NBD-ceramide + H2O
D-erythro-sphingosine + 4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid
D-erythro-C24:1-ceramide + H2O
C24:1 fatty acid + D-erythro-sphingosine
-
Substrates: -
Products: -
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?
D-erythro-dihydrosphingosine + fatty acid
?
-
Substrates: very low ceramide synthesis activity
Products: -
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?
D-erythro-dodecanoyl-7-nitrobenz-2-oxa-1,3-diazol-4-yl-ceramide + H2O
12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoic acid + sphingosine
D-erythro-myristoyl-sphingosine + H2O
myristate + sphingosine
Substrates: -
Products: -
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?
D-erythro-octadecanoyl-ceramide + H2O
D-erythro-sphingosine + palmitic acid
-
Substrates: mtCDase specifically hydrolyzes the D-erythro-isomer of ceramide, requirements for ceramide-enzyme interaction, ligand interaction with the enzyme occurs in a high affinity low specificity manner, in contrast to catalysis which is highly specific for D-erythro-ceramide but occurs with a lower affinity
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?
D-erythro-oleoyl-sphingosine + H2O
oleate + sphingosine
Substrates: -
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?
D-erythro-palmitoyl-sphingosine + H2O
palmitate + sphingosine
Substrates: -
Products: -
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?
D-erythro-sphingosine + (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexa-4,7,10,13,16,19-enoic acid
N-((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexa-4,7,10,13,16,19-enoyl)-D-erythro-sphingosine + H2O
-
Substrates: 50% of activity
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D-erythro-sphingosine + arachidonic acid
N-arachidonyl-D-erythro-sphingosine + H2O
-
Substrates: 61% of activity
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r
D-erythro-sphingosine + behenic acid
N-behenoyl-D-erythro-sphingosine + H2O
-
Substrates: 24% of activity
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D-erythro-sphingosine + cerotic acid
N-cerotoyl-D-erythro-sphingosine + H2O
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Substrates: 4% of activity
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D-erythro-sphingosine + eicosapentaenoic acid
N-eicosapentaenyl-D-erythro-sphingosine + H2O
-
Substrates: 52% of activity
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D-erythro-sphingosine + fatty acid
?
-
Substrates: highest ceramide synthesis activity with D-erythro-sphingosine
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D-erythro-sphingosine + fatty acid
N-acyl-D-erythro-sphingosine + H2O
-
Substrates: -
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D-erythro-sphingosine + lauric acid
N-lauroyl-D-erythro-sphingosine + H2O
-
Substrates: 72% of activity
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D-erythro-sphingosine + lignoceric acid
N-lignoceroyl-D-erythro-sphingosine + H2O
-
Substrates: 6% of activity
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D-erythro-sphingosine + linoleic acid
N-linoleoyl-D-erythro-sphingosine + H2O
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Substrates: 66% of activity
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D-erythro-sphingosine + myristic acid
N-myristoyl-D-erythro-sphingosine + H2O
-
Substrates: best substrate
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D-erythro-sphingosine + oleic acid
N-oleoyl-D-erythro-sphingosine + H2O
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Substrates: 39% of activity
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D-erythro-sphingosine + palmitic acid
N-palmitoyl-D-erythro-sphingosine + H2O
-
Substrates: 70% of activity, palmitic acid can not be replaced with palmityl-CoA
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D-erythro-sphingosine + stearic acid
N-stearoyl-D-erythro-sphingosine + H2O
-
Substrates: 49% of activity
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D-erythro-tetracosanoyl-sphingosine + H2O
tetracosanoate + sphingosine
Substrates: i.e. D-e-C24:0-ceramide
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?
D-threo-sphingosine + fatty acid
?
-
Substrates: low ceramide synthesis activity
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?
dihydro-N-myristoyl-D-erythro-sphingosine + H2O
dihydro-D-erythro-sphingosine + myristate
-
Substrates: 55.9% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
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dihydro-N-palmitoyl-D-erythro-sphingosine + H2O
dihydro-D-erythro-sphingosine + palmitate
-
Substrates: 4.5% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
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dihydroceramide + H2O
dihydrosphingosine + fatty acid
-
Substrates: -
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ganglioside + H2O
lyso-ganglioside + fatty acid
-
Substrates: GM1, GM2, GM3
Products: corresponding to ganglioside type
Products: corresponding to ganglioside type
?
ganglioside GM2 + H2O
?
-
Substrates: sphingolipid, best substrate
Products: -
Products: -
?
hexadecanoyl-ceramide + H2O
hexadecanoate + sphingosine
Substrates: i.e. C16-ceramide
Products: -
Products: -
r
L-erythro-sphingosine + fatty acid
?
-
Substrates: low ceramide synthesis activity
Products: -
Products: -
?
L-threo-sphingosine + fatty acid
?
-
Substrates: low ceramide synthesis activity
Products: -
Products: -
?
linoleoylsphingosine + H2O
linoleic acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
myristic acid + sphingosine
N-myristoylsphingosine + H2O
-
Substrates: highest ceramide synthesis activity with myristic acid
Products: -
Products: -
?
N-((2S,3R)-1,3-dihydroxy-5-((2-oxo-2H-chromen-7-yl)oxy)pentan-2-yl)dodecanamide + H2O
?
Substrates: -
Products: -
Products: -
?
N-((2S,3R)-1,3-dihydroxy-5-((2-oxo-2H-chromen-7-yl)oxy)pentan-2-yl)palmitamide + H2O
palmitate + 2-amino-2,4-dideoxy-5-O-(2-oxo-2H-chromen-7-yl)-D-erythro-pentitol
-
Substrates: -
Products: -
Products: -
?
N-acetylsphingosine + H2O
acetic acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
N-arachidonoyl-ceramide + H2O
sphingosine + arachidonate
-
Substrates: -
Products: -
Products: -
?
N-arachidonoyl-dihydroceramide + H2O
dihydrosphingosine + arachidonate
-
Substrates: -
Products: -
Products: -
?
N-arachidonoyl-phytoceramide + H2O
phytosphingosine + arachidonate
-
Substrates: -
Products: -
Products: -
?
N-arachidoyl-D-erythro-sphingosine + H2O
arachidonate + D-erythro-sphingosine
Substrates: low activity
Products: -
Products: -
?
N-caproylsphingosine + H2O
caproate + sphingosine
-
Substrates: about 25% activity compared to N-oleoylsphingosine
Products: -
Products: -
?
N-dodecanoyl-7-nitrobenz-2-oxa-1,3,4-diazole-D-erythro-dihydrosphingosine + H2O
12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoate + D-erythro-dihydrosphingosine
-
Substrates: -
Products: -
Products: -
r
N-dodecanoyl-7-nitrobenz-2-oxa-1,3,4-diazole-D-erythro-phytosphingosine + H2O
12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanate + D-erythro-phytosphingosine
-
Substrates: -
Products: -
Products: -
r
N-dodecanoyl-7-nitrobenz-2-oxa-1,3,4-diazole-D-erythro-sphingosine + H2O
12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanate + D-erythro-sphingosine
-
Substrates: i.e. C12-NBD-Cer
Products: -
Products: -
r
N-hexanoyl-D-erythro-sphingosine + H2O
sphingosine + hexanoate
-
Substrates: 100.3% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
Products: -
Products: -
?
N-hexanoyl-sphingosine + H2O
hexanoate + sphingosine
Substrates: -
Products: -
Products: -
?
N-hexanoylsphingosine + H2O
hexanoic acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
N-lauroyl-D-erythro-sphingosine + H2O
sphingosine + dodecanoate
-
Substrates: most efficient substrate, 293.2% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
Products: -
Products: -
r
N-lauroylceramide + H2O
laureate + sphingosine
Substrates: -
Products: -
Products: -
?
N-lignoceroyl-D-erythro-sphingosine + H2O
sphingosine + tetracosanoate
-
Substrates: 25.1% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
Products: -
Products: -
?
N-myristoyl-D-erythro-sphingosine + H2O
myristate + D-erythro-sphingosine
-
Substrates: best substrate
Products: -
Products: -
?
N-myristoyl-D-erythro-sphingosine + H2O
sphingosine + myristate
-
Substrates: 212.2% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
Products: -
Products: -
?
N-nervonoyl-D-erythro-sphingosine + H2O
nervonoate + D-erythro-sphingosine
Substrates: -
Products: -
Products: -
?
N-nervonoylsphingosine + H2O
nervonate + sphingosine
-
Substrates: about 80% activity compared to N-oleoylsphingosine
Products: -
Products: -
?
N-octanoylsphinganine + H2O
octanoic acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
N-oleoyl-D-erythro-sphingosine + H2O
oleate + D-erythro-sphingosine
Substrates: -
Products: -
Products: -
?
N-oleoyl-D-sphingosine + H2O
oleate + sphingosine
Substrates: -
Products: -
Products: -
?
N-oleoyl-dihydroceramide + H2O
dihydrosphingosine + oleate
-
Substrates: -
Products: -
Products: -
?
N-oleoyl-phytoceramide + H2O
phytosphingosine + oleate
-
Substrates: -
Products: -
Products: -
?
N-oleoylsphingosine + H2O
oleate + sphingosine
-
Substrates: 100% activity
Products: -
Products: -
?
N-palmitoyl sphingosine + H2O
palmitic acid + sphingosine
Substrates: -
Products: -
Products: -
?
N-palmitoyl-D-erythro-sphingosine + H2O
D-erythro-sphingosine + palmitic acid
-
Substrates: -
Products: -
Products: -
?
N-palmitoyl-D-erythro-sphingosine + H2O
sphingosine + palmitate
-
Substrates: 100% hydrolysis
Products: -
Products: -
r
N-palmitoylsphinganine + H2O
palmitate + sphinganine
Substrates: low hydrolysis rate
Products: -
Products: -
?
N-stearoyl-D-erythro-sphingosine + H2O
sphingosine + stearate
-
Substrates: 98.5% hydrolysis compared to N-palmitoyl-D-erythro-sphingosine
Products: -
Products: -
?
N-stearoylsphinganine + H2O
stearate + sphinganine
Substrates: low hydrolysis rate
Products: -
Products: -
?
N-stearoylsphingosine + H2O
stearate + sphingosine
Substrates: less efficient hydrolysis than of N-lauroylsphingosine and N-palmitoylsphingosine
Products: -
Products: -
?
N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide + H2O
?
N-[(2S,3R,4E)-1,3-dihydroxynonadec-4-en-2-yl]-12-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]dodecanamide + H2O
?
N-[(2S,3R,4E)-13-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-1,3-dihydroxytridec-4-en-2-yl]hexadecanamide + H2O
?
N-[(2S,3R,4E)-7-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-3-yl]oxy]-1,3-dihydroxyhept-4-en-2-yl]-11-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]undecanamide + H2O
?
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amine]dodecanoyl]D-erythro-sphingosine + H2O
?
Substrates: i.e. D-ribo-C12-NBD-phytoceramide
Products: -
Products: -
?
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]D-erythro-sphingosine + H2O
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoate] + D-erythro-sphingosine
Substrates: substrate C12-NBD ceramide
Products: -
Products: -
?
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]lauroyl]-phytosphingosine + H2O
N-12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]laurate + phytosphingosine
-
Substrates: i.e. D-ribo-C12-NBD-phytoceramide
Products: -
Products: -
?
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]lauroyl]-sphingosine + H2O
N-12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]laurate + sphingosine
Substrates: i.e. C12-NBD-ceramide
Products: -
Products: -
r
octadecanoyl-ceramide + H2O
octadecanoate + sphingosine
Substrates: i.e. C18-ceramide
Products: -
Products: -
r
octanoyl-D-erythro-sphingosine + H2O
?
-
Substrates: substrate activity assay
Products: -
Products: -
?
octanoyl-sphingosine + H2O
octanoate + sphingosine
-
Substrates: -
Products: -
Products: -
?
palmitoyl-D-[erythro-9,10]sphingosine + H2O
palmitate + D-erythro-sphingosine
-
Substrates: -
Products: -
Products: -
?
sphingosine + myristic acid + H2O
C14-ceramide
-
Substrates: at pH 8.0
Products: -
Products: -
?
11-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hept-4-en-2-yl]undecanamide + H2O
?
Substrates: -
Products: -
Products: -
ir
11-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hept-4-en-2-yl]undecanamide + H2O
?
Substrates: -
Products: -
Products: -
ir
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
Substrates: -
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
Substrates: -
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
-
Substrates: C12 substrate chain length
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
-
Substrates: C12 substrate chain length
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazoyl-N-dodecanoylsphingosine + H2O
4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid + sphingosine
Substrates: much faster hydrolysis than of N-lauroylsphingosine
Products: -
Products: -
?
4-nitrobenzo-2-oxa-1,3-diazoyl-N-dodecanoylsphingosine + H2O
4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid + sphingosine
-
Substrates: -
Products: -
Products: -
r
a ceramide + H2O
a carboxylate + sphingosine
Substrates: catalyzes the hydrolysis of C6:0 to C18:0 ceramides
Products: -
Products: -
?
a ceramide + H2O
a carboxylate + sphingosine
Substrates: preference for C10:0 and C18:0 ceramides
Products: -
Products: -
?
a ceramide + H2O
a carboxylate + sphingosine
Substrates: ACER1 hydrolyses C20:0-C24:0 ceramides
Products: -
Products: -
?
a ceramide + H2O
a carboxylate + sphingosine
Substrates: ACER2 hydrolyses ceramides and dihydroceramides C18:1 and C20:1
Products: -
Products: -
?
a ceramide + H2O
a carboxylate + sphingosine
Substrates: -
Products: -
Products: -
?
C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
Substrates: substrate activity assay
Products: -
Products: -
?
C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
-
Substrates: -
Products: -
Products: -
?
C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
Substrates: substrate activity assay
Products: -
Products: -
?
C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
Substrates: substrate activity assay
Products: -
Products: -
?
C12-NBD-Cer + H2O
NBD-dodecanoic acid + sphingosine
Substrates: -
Products: -
Products: -
?
C12-NBD-Cer + H2O
NBD-dodecanoic acid + sphingosine
Substrates: -
Products: -
Products: -
?
C12:0-ceramide + H2O
laurate + sphingosine
-
Substrates: preferred substrate
Products: -
Products: -
?
C16:0-ceramide + H2O
palmitate + sphingosine
Substrates: -
Products: -
Products: -
?
C16:0-ceramide + H2O
palmitate + sphingosine
-
Substrates: low activity
Products: -
Products: -
?
C18:0-ceramide + H2O
stearate + sphingosine
Substrates: -
Products: -
Products: -
?
ceramide + H2O
?
Substrates: ceramide in anionic liposomes. The negatively charged liposomes consisted of 25% mole bis(monoacylglycero)phosphate, 45% 1,2-dimyristoyl-sn-glycero-3-phosphocholine, 20% cholesterol, and 10% 12:0 ceramide
Products: -
Products: -
?
ceramide + H2O
?
-
Substrates: substrate with about 30% activity of GM2
Products: -
Products: -
?
ceramide + H2O
sphingosine + a fatty acid
-
Substrates: -
Products: sphongosine is an apoptosis mediator
Products: sphongosine is an apoptosis mediator
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: for ceramide clearance, ceramidases hydrolyze the N-acyl fatty acid, yielding in the generation of sphingosine
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: -
Products: -
Products: -
r
ceramide + H2O
sphingosine + fatty acid
-
Substrates: the recombinant enzyme shows a broad subsrate specificity with ceramides, it shows good activity with ceramides containing C6-C24 fatty acids, and preference of ceramides with monounsaturated fatty acids than saturated fatty acids, overview
Products: -
Products: -
r
ceramide + H2O
sphingosine + fatty acid
-
Substrates: C16-ceramide
Products: -
Products: -
?
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
Substrates: -
Products: -
Products: -
?
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
Substrates: -
Products: -
Products: -
?
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
D-erythro-sphingosine + ?
Substrates: -
Products: -
Products: -
?
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
D-erythro-sphingosine + ?
-
Substrates: substrate activity assay
Products: -
Products: -
?
D-erythro-C12-NBD-ceramide + H2O
D-erythro-sphingosine + 4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid
Substrates: maCER1 has a highly restricted substrate specificity, maCER1 has a major ceramidase activity and only a very minor reverse activity
Products: -
Products: -
r
D-erythro-C12-NBD-ceramide + H2O
D-erythro-sphingosine + 4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid
-
Substrates: substrate in activity assay
Products: -
Products: -
?
D-erythro-dodecanoyl-7-nitrobenz-2-oxa-1,3-diazol-4-yl-ceramide + H2O
12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoic acid + sphingosine
-
Substrates: -
Products: -
Products: -
r
D-erythro-dodecanoyl-7-nitrobenz-2-oxa-1,3-diazol-4-yl-ceramide + H2O
12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoic acid + sphingosine
-
Substrates: -
Products: -
Products: -
r
ganglioside GM3 + H2O
?
Substrates: (2S,4S,5R,6R)-5-acetamido-2-[(2S,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(E,2S,3R)-3-hydroxy-2-(octadecanoylamino)octadec-4-enoxy]oxan-3-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid, isolated and purified from porcine brain slices and human Jurkat cell culture. Product identification via a TLC plate that is developed using a solvent system containing acetic acid:n-butanol:0.25% CaCl2 (1:2:1, v/v/v) and stained with Orcinol stain to visualize l-GSL spots. Assay method development, detailed overview
Products: -
Products: -
?
ganglioside GM3 + H2O
?
Substrates: (2S,4S,5R,6R)-5-acetamido-2-[(2S,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(E,2S,3R)-3-hydroxy-2-(octadecanoylamino)octadec-4-enoxy]oxan-3-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid, isolated and purified from porcine brain slices and human Jurkat cell culture. Product identification via a TLC plate that is developed using a solvent system containing acetic acid:n-butanol:0.25% CaCl2 (1:2:1, v/v/v) and stained with Orcinol stain to visualize l-GSL spots. Assay method development, detailed overview
Products: -
Products: -
?
glycolipid + H2O
?
Substrates: comparison of EGCase and SCDase GSL profiles in biological samples
Products: -
Products: -
?
glycolipid + H2O
?
Substrates: comparison of EGCase and SCDase GSL profiles in biological samples
Products: -
Products: -
?
N-acyl-sphingosine + H2O
a carboxylate + sphingosine
-
Substrates: the Asah2-encoded neutral ceramidase is a key enzyme for the catabolism of dietary sphingolipids and regulates the cellular levels of bioactive sphingolipid metabolites, ceramide, sphingosine, and sphingosine 1-phosphate, in the intestinal tract
Products: -
Products: -
?
N-acyl-sphingosine + H2O
a carboxylate + sphingosine
-
Substrates: -
Products: -
Products: -
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: AC catalyzes the hydrolysis of ceramide to sphingosine and fatty acid
Products: -
Products: -
r
N-acylsphingosine + H2O
a carboxylate + sphingosine
Substrates: CDase hydrolyzes the amide bond in ceramides to yield free fatty acid and sphingosine
Products: -
Products: -
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: CDase cleaves the N-acyl linkage of ceramide to produce sphingosine and free fatty acid
Products: -
Products: -
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: involved in the biosynthesis of ceramide, crucial enzyme for the regulation of the intracellular balance of the contents of ceramide, sphingosine and possibly sphingosine 1-phosphate
Products: -
Products: -
r
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: involved in the biosynthesis of ceramide, crucial enzyme for the regulation of the intracellular balance of the contents of ceramide, sphingosine and possibly sphingosine 1-phosphate
Products: -
Products: -
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: -
Products: -
Products: -
r
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: -
Products: -
Products: -
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
Substrates: CDase catalyzes the hydrolysis of the N-acyl linkage of ceramide to produce sphingosine
Products: -
Products: -
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: CDase cleaves the N-acyl linkage of ceramide into sphingosine and free fatty acid, brain CDase is able to catalyze the reverse reaction, i.e. ceramide synthesis
Products: -
Products: -
r
N-acylsphingosine + H2O
a carboxylate + sphingosine
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Substrates: CDase cleaves the N-acyl linkage of ceramide to produce sphingosine and free fatty acid
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N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
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N-acylsphingosine + H2O
carboxylate + sphingosine
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Substrates: the carboxylate is a fatty acid
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N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
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N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
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N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
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N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid, Ypc1p can catalyse the reverse reaction, i.e. the condensation of non-esterified fatty acids with phytosphingosine or dihydrosphingosine. The cysteine residues at positions 27 and 219 are required for reverse ceramidase activity
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N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid. The cysteine residues at positions 27 and 219 are required for reverse ceramidase activity
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N-hexanoyl-D-erythro-sphingosine + H2O
hexanoate + D-erythro-sphingosine
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Substrates: -
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N-hexanoyl-D-erythro-sphingosine + H2O
hexanoate + D-erythro-sphingosine
Substrates: -
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N-lauroyl-D-erythro-sphingosine + H2O
laurate + D-erythro-sphingosine
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Substrates: the enzyme catalyzes also the reverse reaction of ceramide synthesis
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N-lauroyl-D-erythro-sphingosine + H2O
laurate + D-erythro-sphingosine
Substrates: best substrate
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N-lauroylsphingosine + H2O
laurate + sphingosine
Substrates: more efficient hydrolysis than of N-palmitoylsphingosine and N-stearoylsphingosine, less efficient hydrolysis than of 4-nitrobenzo-2-oxa-1,3-diazoyl-N-dodecanoylsphingosine
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N-lauroylsphingosine + H2O
laurate + sphingosine
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Substrates: about 95% activity compared to N-oleoylsphingosine
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N-lauroylsphingosine + H2O
lauric acid + sphingosine
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Substrates: optimal substrate, AC also efficiently catalyzes ceramide synthesis
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N-lauroylsphingosine + H2O
lauric acid + sphingosine
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Substrates: -
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N-lauroylsphingosine + H2O
lauric acid + sphingosine
Substrates: ASAH1 hydrolyzes mainly unsaturated ceramides containing C6-C16 acyl chains
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N-lignoceroyl-D-erythro-sphingosine + H2O
lignocerate + D-erythro-sphingosine
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Substrates: low activity
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N-lignoceroyl-D-erythro-sphingosine + H2O
lignocerate + D-erythro-sphingosine
Substrates: low activity
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N-octanoylsphingosine + H2O
octanoic acid + sphingosine
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Substrates: -
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N-octanoylsphingosine + H2O
octanoic acid + sphingosine
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Substrates: -
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N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
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Substrates: common substrate in erythrocytes
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N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
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Substrates: i.e. D-e-C18:1-ceramide, common substrate in erythrocytes
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N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
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Substrates: common substrate in erythrocytes
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N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
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Substrates: i.e. D-e-C18:1-ceramide, common substrate in erythrocytes
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N-oleoylsphingosine + H2O
oleic acid + sphingosine
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Substrates: -
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N-oleoylsphingosine + H2O
oleic acid + sphingosine
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Substrates: -
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N-oleoylsphingosine + H2O
oleic acid + sphingosine
-
Substrates: -
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N-palmitoyl-D-erythro-sphingosine + H2O
palmitate + D-erythro-sphingosine
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Substrates: -
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N-palmitoyl-D-erythro-sphingosine + H2O
palmitate + D-erythro-sphingosine
Substrates: -
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N-palmitoylsphinganine + H2O
palmitic acid + sphinganine
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Substrates: -
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N-palmitoylsphinganine + H2O
palmitic acid + sphinganine
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Substrates: -
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N-palmitoylsphinganine + H2O
palmitic acid + sphinganine
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Substrates: -
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N-palmitoylsphingosine + H2O
palmitate + sphingosine
Substrates: less efficient hydrolysis than of N-lauroylsphingosine, more efficient hydrolysis than of N-stearoylsphingosine
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N-palmitoylsphingosine + H2O
palmitate + sphingosine
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Substrates: about 65% activity compared to N-oleoylsphingosine
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N-palmitoylsphingosine + H2O
palmitic acid + sphingosine
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Substrates: -
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N-palmitoylsphingosine + H2O
palmitic acid + sphingosine
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Substrates: -
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N-palmitoylsphingosine + H2O
palmitic acid + sphingosine
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Substrates: -
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N-palmitoylsphingosine + H2O
palmitic acid + sphingosine
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Substrates: -
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N-palmitoylsphingosine + H2O
palmitic acid + sphingosine
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Substrates: -
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N-stearoyl-D-erythro-sphingosine + H2O
stearate + D-erythro-sphingosine
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Substrates: -
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N-stearoyl-D-erythro-sphingosine + H2O
stearate + D-erythro-sphingosine
Substrates: low activity
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N-stearoylsphinganine + H2O
stearic acid + sphinganine
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Substrates: -
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N-stearoylsphinganine + H2O
stearic acid + sphinganine
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Substrates: -
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N-stearoylsphinganine + H2O
stearic acid + sphinganine
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Substrates: -
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N-stearoylsphingosine + H2O
stearic acid + sphingosine
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Substrates: -
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N-stearoylsphingosine + H2O
stearic acid + sphingosine
-
Substrates: -
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N-stearoylsphingosine + H2O
stearic acid + sphingosine
-
Substrates: -
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N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide + H2O
?
Substrates: 5.6% hydrolysis
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N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide + H2O
?
Substrates: 6.2% hydrolysis
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N-[(2S,3R,4E)-1,3-dihydroxynonadec-4-en-2-yl]-12-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]dodecanamide + H2O
?
Substrates: 6.1% hydrolysis
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N-[(2S,3R,4E)-1,3-dihydroxynonadec-4-en-2-yl]-12-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]dodecanamide + H2O
?
Substrates: 63.3% hydrolysis
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N-[(2S,3R,4E)-13-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-1,3-dihydroxytridec-4-en-2-yl]hexadecanamide + H2O
?
Substrates: 6.3% hydrolysis
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N-[(2S,3R,4E)-13-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-1,3-dihydroxytridec-4-en-2-yl]hexadecanamide + H2O
?
Substrates: 3.9% hydrolysis
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N-[(2S,3R,4E)-7-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-3-yl]oxy]-1,3-dihydroxyhept-4-en-2-yl]-11-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]undecanamide + H2O
?
Substrates: fluorescently labelled ceramide analogue, 4.0% hydrolýsis
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N-[(2S,3R,4E)-7-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-3-yl]oxy]-1,3-dihydroxyhept-4-en-2-yl]-11-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]undecanamide + H2O
?
Substrates: fluorescently labelled ceramide analogue, 5.8% hydrolýsis
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palmitoyl sphingosine + H2O
palmitate + sphingosine
Substrates: substrate activity assay
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palmitoyl sphingosine + H2O
palmitate + sphingosine
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Substrates: substrate activity assay
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palmitoyl-sphingosine + H2O
palmitate + sphingosine
Substrates: -
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palmitoyl-sphingosine + H2O
palmitate + sphingosine
-
Substrates: -
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palmitoyl-sphingosine + H2O
palmitate + sphingosine
Substrates: -
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additional information
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Substrates: ceramidase catalyzes the hydrolysis of ceramide to form sphingosine
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Substrates: the enzyme has autoproteolytic activity
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Substrates: the enzyme has autoproteolytic activity
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Substrates: ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
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Substrates: ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
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Substrates: ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
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Substrates: critical role of AC in the regulation of sphingolipid metabolism
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Substrates: cooperative prosurvival activity by MAP kinases ERK and Akt in human alveolar macrophages is dependent on high levels of acid ceramidase activity, overview, blocking of acid ceramidase but not sphingosine kinase activity in alveolar macrophages leads to decreased ERK and Akt activity and induction of cell death, sphingosine and L-threo-dihydrosphingosine reverse the antisurvival effects of acid ceramidase inhibition in alveolar macrophages
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Substrates: CER2 catalyzes the hydrolysis of ceramides derived from both the de novo and sphingomyelin breakdown pathways, Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and sphingosine 1-phosphate
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Substrates: CER2 catalyzes the hydrolysis of ceramides derived from both the de novo and sphingomyelin breakdown pathways, Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and sphingosine 1-phosphate
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Substrates: acidic and alkaline isozyme activities increase with keratinocyte differentiation, while the activities of phytoalkaline and neutral isozymes decrease, overview
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Substrates: diacylglycerol assay, i.e. ceramide:DAG assay
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Substrates: neutral ceramidase plays a major role in ceramide metabolism in the human gut
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Substrates: acid ceramidase plays a critical role in the regulation of ceramide and sphingosine metabolism
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Substrates: ASAH1 hydrolyzes ceramides and regulates neuronal development, and its deficiency often results in mental retardation. Results of linkage disequilibrium and polymorphism analyses suggest that a particular group of haplotypes in ASAH1 represents a signature of recent positive Darwinian selection
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Substrates: ceramidase catalyzes the hydrolysis of ceramide into sphingosine and a free fatty acid
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Substrates: ceramidase catalyzes the hydrolysis of ceramide to form sphingosine
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Substrates: acid ceramidase deacylates ceramide and yields sphingosine
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Substrates: ACER3 can catalyze the hydrolysis of unsaturated long-chain dihydroceramides as efficiently as unsaturated long-chain ceramides. ACER1 and ACER2, the homologues of ACER3, also catalyzed the hydrolysis of certain dihydroceramide species to generate dihydrosphingosine
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Substrates: ACER3 hydrolyzes C18:1-, C20:1-, C20:4-ceramides, C18:1-, C20:1-, C20:4-dihydroceramides, and C18:1-, C20:1-, C20:4-phytoceramides in vitro
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Substrates: ACER2 shows a broader substrate specificity catalyzing the hydrolysis of various ceramides. The luminal ACER2 N-terminal tail, comprising 36 amino acid residues, is important for ACER2 activity, but the terminal 13 amino acid residues are not required for its activity
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Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
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Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
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Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
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Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
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Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
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Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
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Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
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Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
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Substrates: acid ceramidase catalyzes the hydrolysis of ceramide to constituent sphingoid base, sphingosine, and fatty acid
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Substrates: the N-acyl moiety of ceramide is cleaved by ceramidases to form the lysolipid sphingosine that undergoes further phosphorylation to sphingosine-1-phosphate
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Substrates: design and synthesis of a set of fluorescently labeled ceramides as substrates for acid and neutral ceramidases, overview. Although both the dyes, (acyl-(4-nitro-2,1,3-benzoxadiazol-7-yl)aminoethyl)-ceramide and acyl-Nile red-ceramide do not have any noticeable preference for the substitution at acyl or sphingosine part in ceramide towards hydrolysis by acid ceramidase, the ceramides with acyl-substituted NBD and Sph-substituted NR dyes have been found to be a better substrate for neutral ceramidase
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Substrates: design and synthesis of a set of fluorescently labeled ceramides as substrates for acid and neutral ceramidases, overview. Although both the dyes, (acyl-(4-nitro-2,1,3-benzoxadiazol-7-yl)aminoethyl)-ceramide and acyl-Nile red-ceramide do not have any noticeable preference for the substitution at acyl or sphingosine part in ceramide towards hydrolysis by acid ceramidase, the ceramides with acyl-substituted NBD and Sph-substituted NR dyes have been found to be a better substrate for neutral ceramidase
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Substrates: the enzyme directly interacts with and binds steroidogenic factor 1, interaction site analysis, overview
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Substrates: the enzyme directly interacts with and binds steroidogenic factor 1, interaction site analysis, overview
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Substrates: ADIPOR2 may have a preference for C18 ceramide substrate, but can also hydrolyse shorter (C6 ceramide) and longer (C24 ceramide) substrates, but to a lesser extent. Low overall ceramidase catalytic activity of ADIPOR2. Substrate binding structure, overview. The substrate amide carbonyl contacts the R278TM5 and Y328TM6 side chains, which are typical carbonyl-polarizing and oxyanion-stabilizing residues in zinc-dependent hydrolases
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Substrates: the enzyme performs autocatalysis. Substrate modeling suggests distinct catalytic mechanisms for substrate hydrolysis versus autocleavage
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Substrates: the enzyme has broad substrate specificity with preference for ceramides with a medium acyl-chain or a mono unsaturated long acyl-chain. The enzyme prefers ceramides with unsaturated acyl-chains over ceramides with saturated acyl-chains of the same length, and it does not use phytoceramides as substrates, suggesting that LsnCer is a ceramide-specific ceramidase
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Substrates: the enzyme has broad substrate specificity with preference for ceramides with a medium acyl-chain or a mono unsaturated long acyl-chain. The enzyme prefers ceramides with unsaturated acyl-chains over ceramides with saturated acyl-chains of the same length, and it does not use phytoceramides as substrates, suggesting that LsnCer is a ceramide-specific ceramidase
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Substrates: maCER1 may play a role in regulating the levels of bioactive lipids ceramide and sphingosine-1-phosphate, as well as complex sphingolipids, maCER1 may have a specific role in skin function
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Substrates: maCER1 may play a role in regulating the levels of bioactive lipids ceramide and sphingosine-1-phosphate, as well as complex sphingolipids, maCER1 may have a specific role in skin function
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Substrates: not: D-erythro-C12-NBD-dihydroceramide, D-ribo-C12-NBD-phytoceramide, L-threo-C12-NBD-ceramide
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Substrates: not: D-erythro-C12-NBD-dihydroceramide, D-ribo-C12-NBD-phytoceramide, L-threo-C12-NBD-ceramide
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Substrates: the enzyme is involved in ceramide metabolism at the plasma membrane and in extracellular milieu, hydrolysis of ceramide on the cell surface, overview, involvement of the enzyme in stimulus-induced Cer metabolism by doxorubicin
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Substrates: the enzyme is involved in degradation of epidermal ceramides, ceramidase activity is not age-dependent
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Substrates: acid ceramidase, but not acid sphingomyelinase, is required for tumor necrosis factor-alpha-induced prostaglandin PGE2 production, overview
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Substrates: cleaves the N-acyl linkage of ceramides into a sphingosine base and a free fatty acid
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Substrates: ceramidase catalyzes the hydrolysis of ceramide to form sphingosine and free fatty acid
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Substrates: the N-acyl moiety of ceramide is cleaved by ceramidases to form the lysolipid sphingosine that undergoes further phosphorylation to sphingosine-1-phosphate
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Substrates: recombinant NlnCDase shows a broad capacity to hydrolyze different ceramide varieties and has a preference for the short and medium chain ceramide, the substrate preference in descending order is C12-ceramide, C6-ceramide, and C16-ceramide. The enzyme shows low activity for the very-short chain C2-ceramide and the long chain substrates C20-ceramide and C24-ceramide
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Substrates: CDase may be a virulence factor
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Substrates: the C-terminal tail is essential for enzyme activity and correct folding
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Substrates: ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeruginosa
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Substrates: ceramidase enhances cytotoxicity induced by hemolytic phospholipase C
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Substrates: ceramidase catalyzes the hydrolysis of ceramide to generate sphingosine and fatty acid, also found to catalyze the reverse reaction
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Substrates: ceramidase catalyzes the hydrolysis of ceramide to generate sphingosine and fatty acid, also found to catalyze the reverse reaction
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Substrates: the Pseudomonas neutral CDase can hydrolyze ceramide in intact erythrocytes, leading to hemolysis. The reaction mechanism for ceramide hydrolysis in vivo appears to be the same as that for ceramide hydrolysis in vitro because the mutation of residues surrounding the catabolic zinc ion abolish the hemolytic activity along with ceramide hydrolysis by CDase in intact erythrocytes
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Substrates: the enzyme is able to effectively degrade ceramide in the presence of Staphylococcus aureus-derived lipids or neutral detergents
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Substrates: the enzyme can hydrolyze human skin-specific omega-hydroxyacyl ceramides
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Substrates: ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeruginosa
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Substrates: ceramidase enhances cytotoxicity induced by hemolytic phospholipase C
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Substrates: broad substrate specificity
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Substrates: neutral ceramidase is involved in the regulation of ceramide-mediated signaling
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Substrates: not: glycosphingolipids, e.g. GalCer, sulfatide, Galbeta(1-3)GalNAcbeta(1-4)(NeuAcalpha(2-3))Galbeta(1-4)Glcbeta(1-1)ceramide, sphingomyelin
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?
additional information
?
-
-
Substrates: no substrate in the ceramide synthesis reaction: palmitoyl-CoA
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?
additional information
?
-
-
Substrates: the C-terminal residues Ile-758 and Phe-756 are essential for enzyme function, the C-terminal tail is indispensable for the correct folding, localization and enzyme activity
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is important in digestion of sphingolipids
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?
additional information
?
-
-
Substrates: neutral ceramidase is a key enzyme for hydrolysis of sphingomyelin in the gut
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?
additional information
?
-
Substrates: ceramidase deacylates ceramide to form sphingosine
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?
additional information
?
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to generate sphingosine and fatty acid, also found to catalyze the reverse reaction
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?
additional information
?
-
-
Substrates: long chain dihydroceramide dihydro-hexanoyl-D-erythro-sphingosine is resistant to the enzyme
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?
additional information
?
-
-
Substrates: the enzyme prefers medium-chain or long chain ceramides over short-chain ceramides as substrates
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
C20:0-ceramide + H2O
eicosanoic acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
C20:1-ceramide + H2O
C20:1 fatty acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
C24:0-ceramide + H2O
C24:0 fatty acid + sphingosine
-
Substrates: -
Products: -
Products: -
?
D-erythro-C24:1-ceramide + H2O
C24:1 fatty acid + D-erythro-sphingosine
-
Substrates: -
Products: -
Products: -
?
D-erythro-myristoyl-sphingosine + H2O
myristate + sphingosine
Substrates: -
Products: -
Products: -
?
D-erythro-oleoyl-sphingosine + H2O
oleate + sphingosine
Substrates: -
Products: -
Products: -
?
D-erythro-palmitoyl-sphingosine + H2O
palmitate + sphingosine
Substrates: -
Products: -
Products: -
?
D-erythro-tetracosanoyl-sphingosine + H2O
tetracosanoate + sphingosine
Substrates: i.e. D-e-C24:0-ceramide
Products: -
Products: -
?
dihydroceramide + H2O
dihydrosphingosine + fatty acid
-
Substrates: -
Products: -
Products: -
?
N-acyl-sphingosine + H2O
a carboxylate + sphingosine
-
Substrates: the Asah2-encoded neutral ceramidase is a key enzyme for the catabolism of dietary sphingolipids and regulates the cellular levels of bioactive sphingolipid metabolites, ceramide, sphingosine, and sphingosine 1-phosphate, in the intestinal tract
Products: -
Products: -
?
ceramide + H2O
sphingosine + a fatty acid
-
Substrates: -
Products: sphongosine is an apoptosis mediator
Products: sphongosine is an apoptosis mediator
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
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?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
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?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: for ceramide clearance, ceramidases hydrolyze the N-acyl fatty acid, yielding in the generation of sphingosine
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?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: -
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?
ceramide + H2O
sphingosine + fatty acid
Substrates: -
Products: -
Products: -
?
ceramide + H2O
sphingosine + fatty acid
-
Substrates: -
Products: -
Products: -
r
glycolipid + H2O
?
Substrates: comparison of EGCase and SCDase GSL profiles in biological samples
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?
glycolipid + H2O
?
Substrates: comparison of EGCase and SCDase GSL profiles in biological samples
Products: -
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?
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: involved in the biosynthesis of ceramide, crucial enzyme for the regulation of the intracellular balance of the contents of ceramide, sphingosine and possibly sphingosine 1-phosphate
Products: -
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r
N-acylsphingosine + H2O
a carboxylate + sphingosine
-
Substrates: involved in the biosynthesis of ceramide, crucial enzyme for the regulation of the intracellular balance of the contents of ceramide, sphingosine and possibly sphingosine 1-phosphate
Products: -
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?
N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
Products: -
Products: -
?
N-acylsphingosine + H2O
carboxylate + sphingosine
-
Substrates: the carboxylate is a fatty acid
Products: -
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?
N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
Products: -
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?
N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
Products: -
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?
N-acylsphingosine + H2O
carboxylate + sphingosine
Substrates: the carboxylate is a fatty acid
Products: -
Products: -
r
N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
-
Substrates: common substrate in erythrocytes
Products: -
Products: -
?
N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
-
Substrates: common substrate in erythrocytes
Products: -
Products: -
?
additional information
?
-
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to form sphingosine
Products: -
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?
additional information
?
-
Substrates: ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
Products: -
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?
additional information
?
-
-
Substrates: ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: critical role of AC in the regulation of sphingolipid metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: cooperative prosurvival activity by MAP kinases ERK and Akt in human alveolar macrophages is dependent on high levels of acid ceramidase activity, overview, blocking of acid ceramidase but not sphingosine kinase activity in alveolar macrophages leads to decreased ERK and Akt activity and induction of cell death, sphingosine and L-threo-dihydrosphingosine reverse the antisurvival effects of acid ceramidase inhibition in alveolar macrophages
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?
additional information
?
-
Substrates: CER2 catalyzes the hydrolysis of ceramides derived from both the de novo and sphingomyelin breakdown pathways, Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and sphingosine 1-phosphate
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?
additional information
?
-
-
Substrates: CER2 catalyzes the hydrolysis of ceramides derived from both the de novo and sphingomyelin breakdown pathways, Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and sphingosine 1-phosphate
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?
additional information
?
-
Substrates: acidic and alkaline isozyme activities increase with keratinocyte differentiation, while the activities of phytoalkaline and neutral isozymes decrease, overview
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?
additional information
?
-
-
Substrates: neutral ceramidase plays a major role in ceramide metabolism in the human gut
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?
additional information
?
-
-
Substrates: acid ceramidase plays a critical role in the regulation of ceramide and sphingosine metabolism
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?
additional information
?
-
-
Substrates: ASAH1 hydrolyzes ceramides and regulates neuronal development, and its deficiency often results in mental retardation. Results of linkage disequilibrium and polymorphism analyses suggest that a particular group of haplotypes in ASAH1 represents a signature of recent positive Darwinian selection
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?
additional information
?
-
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide into sphingosine and a free fatty acid
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?
additional information
?
-
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to form sphingosine
Products: -
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?
additional information
?
-
-
Substrates: acid ceramidase deacylates ceramide and yields sphingosine
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?
additional information
?
-
-
Substrates: ACER3 can catalyze the hydrolysis of unsaturated long-chain dihydroceramides as efficiently as unsaturated long-chain ceramides. ACER1 and ACER2, the homologues of ACER3, also catalyzed the hydrolysis of certain dihydroceramide species to generate dihydrosphingosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
Products: -
Products: -
?
additional information
?
-
Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
Products: -
Products: -
?
additional information
?
-
Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
Products: -
Products: -
?
additional information
?
-
Substrates: only the natural D-erythro-ceramide isomer is used as substrate of the four stereoisomers of ceramide. Dihydroceramide or phytoceramide forms, shortening the length of the alkyl backbone, methylation of the primary or secondary hydroxyl groups results in reduction or loss of the neutral ceramidase activity
Products: -
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?
additional information
?
-
-
Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
Products: -
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?
additional information
?
-
Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
Products: -
Products: -
?
additional information
?
-
Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
Products: -
Products: -
?
additional information
?
-
Substrates: short acyl-chain ceramides (i.e. C16 acyl chain) are poor substrates for acid ceramidase
Products: -
Products: -
?
additional information
?
-
Substrates: acid ceramidase catalyzes the hydrolysis of ceramide to constituent sphingoid base, sphingosine, and fatty acid
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?
additional information
?
-
Substrates: the N-acyl moiety of ceramide is cleaved by ceramidases to form the lysolipid sphingosine that undergoes further phosphorylation to sphingosine-1-phosphate
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?
additional information
?
-
Substrates: maCER1 may play a role in regulating the levels of bioactive lipids ceramide and sphingosine-1-phosphate, as well as complex sphingolipids, maCER1 may have a specific role in skin function
Products: -
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?
additional information
?
-
-
Substrates: maCER1 may play a role in regulating the levels of bioactive lipids ceramide and sphingosine-1-phosphate, as well as complex sphingolipids, maCER1 may have a specific role in skin function
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in ceramide metabolism at the plasma membrane and in extracellular milieu, hydrolysis of ceramide on the cell surface, overview, involvement of the enzyme in stimulus-induced Cer metabolism by doxorubicin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in degradation of epidermal ceramides, ceramidase activity is not age-dependent
Products: -
Products: -
?
additional information
?
-
-
Substrates: acid ceramidase, but not acid sphingomyelinase, is required for tumor necrosis factor-alpha-induced prostaglandin PGE2 production, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves the N-acyl linkage of ceramides into a sphingosine base and a free fatty acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to form sphingosine and free fatty acid
Products: -
Products: -
?
additional information
?
-
Substrates: the N-acyl moiety of ceramide is cleaved by ceramidases to form the lysolipid sphingosine that undergoes further phosphorylation to sphingosine-1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: CDase may be a virulence factor
Products: -
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?
additional information
?
-
-
Substrates: ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeruginosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: ceramidase enhances cytotoxicity induced by hemolytic phospholipase C
Products: -
Products: -
?
additional information
?
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to generate sphingosine and fatty acid, also found to catalyze the reverse reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to generate sphingosine and fatty acid, also found to catalyze the reverse reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: the Pseudomonas neutral CDase can hydrolyze ceramide in intact erythrocytes, leading to hemolysis. The reaction mechanism for ceramide hydrolysis in vivo appears to be the same as that for ceramide hydrolysis in vitro because the mutation of residues surrounding the catabolic zinc ion abolish the hemolytic activity along with ceramide hydrolysis by CDase in intact erythrocytes
Products: -
Products: -
?
additional information
?
-
-
Substrates: ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeruginosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: ceramidase enhances cytotoxicity induced by hemolytic phospholipase C
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: neutral ceramidase is involved in the regulation of ceramide-mediated signaling
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is important in digestion of sphingolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: neutral ceramidase is a key enzyme for hydrolysis of sphingomyelin in the gut
Products: -
Products: -
?
additional information
?
-
Substrates: ceramidase deacylates ceramide to form sphingosine
Products: -
Products: -
?
additional information
?
-
Substrates: ceramidase catalyzes the hydrolysis of ceramide to generate sphingosine and fatty acid, also found to catalyze the reverse reaction
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Mg2+
Mn2+
Na+
NaCl
at 150 mM NaCl, acer-1 seedlings dramatically loose vitality compared with the wild-type, the amiR-ACER-1 seedlings are the most sensitive to salt, showing obvious differences from the other genotypes after 100 mM NaCl treatment for 12 days
Zn2+
additional information
Ca2+
-
activates, required by ACER2 for both its in vitro and cellular activities. Cellular ACER2 activity is inhibited by depletion of Ca2+ from Golgi lumen
Ca2+
ACER3 has a catalytic Zn2+ binding site in its core and a Ca2+ binding site physically and functionally connected to the Zn2+, two residues appear to play critical roles in physically linking the Ca2+ and the Zn2+ sites, W20 and E33. E33 carboxylate interacts with the Ca2+ ion and is in close proximity to H81TM2 side chain, while H81TM2 coordinates the Zn2+, Ca2+-binding site within the N-terminus, structure overview. The Ca2+ ion is coordinated by six oxygens from the D19 carboxylate (bidentate), the W20 backbone carbonyl, the E22 backbone carbonyl, the N24 side chain carbonyl, and the E33 carboxylate (monodentate)
Ca2+
-
a calcium or magnesium ion is presumed to be important for stabilizing the two domains
Mg2+
-
a calcium or magnesium ion is presumed to be important for stabilizing the two domains
Mg2+
the maximum activity with Mg2+ is only 36% of that in presence of optimal Ca2+ or Ba2+ concentrations
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
-
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
-
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
dependent on, ACER3 has a catalytic Zn2+ binding site in its core and a Ca2+ binding site physically and functionally connected to the Zn2+. Two residues appear to play critical roles in physically linking the Ca2+ and the Zn2+ sites, W20 and E33. E33 carboxylate interacts with the Ca2+ ion and is in close proximity to H81TM2 side chain, while H81TM2 coordinates the Zn2+. Zn2+ is coordinated by three His residues (H81TM2, H217TM7, and H221TM7) and a water molecule forming hydrogen bonds with S77TM2 and D92TM3. The residues forming this Zn2+ binding site are strictly conserved among the ACER family, and across species from yeast to human
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
-
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
-
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
-
neutral CDase contains a zinc ion in the active site that functions as a catalytic center, the active center of CDase is the zinc ion itself, with the reaction following a similar mechanism as observed for zinc-dependent carboxypeptidase
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
-
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
additional information
Zn2+, and EDTA have little effect on the activity
additional information
-
Mg2+ and Mn2+ have no effect on ceramidase activity in ACER2 microsomes
additional information
-
neutral ceramidase is not affected by Ca2+, Mg2+ or Mn2+. No cations are required to activate neutral ceramidase
additional information
neutral ceramidase is not affected by Ca2+, Mg2+ or Mn2+. No cations are required to activate neutral ceramidase
additional information
neutral ceramidase is not affected by Ca2+, Mg2+ or Mn2+. No cations are required to activate neutral ceramidase
additional information
neutral ceramidase is not affected by Ca2+, Mg2+ or Mn2+. No cations are required to activate neutral ceramidase
additional information
-
the enzyme activity is not affected by Mg2+, Mn2+, Ni+, and Zn2+
additional information
-
divalent cation required, without strong specificity
additional information
-
the ceramide synthesis activity is totally independent of stimulating cations
additional information
-
the enzyme is not affected by Li+, Na+, Mn2+ and Mg2+
additional information
112 kDa CDase from kidney is not activated by Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R, 2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
inhibits in vitro
(1R,2R) 2-(N-tetradecylamino)-1-(4-NO2)-phenyl-1,3-dihydroxy-propane HCl
-
-
(1R,2R)-2-N-(tetradecanoylamino)-1-(4'-nitrophenyl)-propyl-1,3-O,O-(N,N-dimethylamino)acetate dihydrochloride
i.e. LCL521 or Di-DMG-B13, is a lysosomotropic inhibitor of ACDase, inhibition mechanism, overview. Low dose of LCL521 (0.001 mM) effectively inhibits ACDase in cells, but the effects are transient. A higher dose of LCL521 (0.01 mM) causes profound decrease of sphingosine and increase of ceramide, but additionally affects the processing and regeneration of the ACDase protein, with biphasic and reversible effects on the expression of ACDase, which parallels the long term changes of cellular sphingosine and ceramide. Finally, the higher concentrations of LCL521 also inhibit dihydroceramide desaturase (DES-1, EC 1.14.19.17). LCL521 inhibits ACDase specifically among the ceramidases in vitro, which is reinforced by the lysosomal targeting
(1S, 2R)-D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
inhibitor of alkaline ceramidase; inhibitor of alkaline ceramidase; inhibitor of neutral ceramidase
(2S)-3-([5-[(1S)-1-[[2,6-dimethyl-4'-(trifluoromethyl)[1,1'-biphenyl]-4-yl]oxy]-2-methylpropyl]thiophene-2-carbonyl]amino)-2-hydroxypropanoic acid
0.02 mM, 61.39% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
(E)-4-[(2S,3R)-N-1,3-dihydroxyoctadecan-2-ylamino]4-oxo-2-butenoic acid
-
1-(4-carbamoylanilino)-1-oxopropan-2-yl (4E)-2-tert-butyl-4-[(thiophen-2-yl)methylidene]-1,2,3,4-tetrahydroacridine-9-carboxylate
0.02 mM, 41.71% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
modification of carboxyl groups completely inhibits forward and reverse reaction
12-amino-N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]dodecanamide
-
2,3-Butanedione
-
modification of Arg causes about 50% inhibition of forward and reverse reaction
2-methyl-N-(4-phenoxyphenyl)piperidine-1-carboxamide
0.02 mM, 53.75% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
2-oxo-N,5-diphenyl-1,3-oxazole-3(2H)-carboxamide
0.005 mM, 20% inhibition
2-oxo-N-(4-phenylbutyl)-5-(1,3-thiazol-2-yl)-1,3-oxazole-3(2H)-carboxamide
-
2-oxo-N-(4-phenylbutyl)-5-(1,3-thiazol-4-yl)-1,3-oxazole-3(2H)-carboxamide
-
2-oxo-N-(4-phenylbutyl)-5-(quinoxalin-2-yl)-1,3-oxazole-3(2H)-carboxamide
-
2-[3-(4-butylphenyl)-3-oxopropyl]-1H-indene-1,3(2H)-dione
0.02 mM, 60.38% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
3,3-dimethyl-1-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]butan-1-one
0.02 mM, 58.95% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
3-(6-phenylhexanoyl)-1,3-oxazolidin-2-one
above, pH and temperature not specified in the publication, 9.4% inhibition at 0.02 mM
3-(cyclopropylmethyl)-5-fluoro-N-hexyl-2,4-dioxopyrimidine-1-carboxamide
-
3-bromo-N-methyl-N-[2-(pyridin-2-yl)ethyl]benzene-1-sulfonamide
0.02 mM, 75.46% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
3-[(2E)-3-(4-methoxyphenyl)-1-oxo-2-propen-1-yl]-6-methyl-4-phenyl-2(1H)-quinolinone
-
-
3-[4-(cyclohexyloxy)benzoyl]-1,3-oxazolidin-2-one
above, pH and temperature not specified in the publication, 18.3% inhibition at 0.02 mM
3-[6-(3-chlorophenyl)hexanoyl]-1,3-oxazolidin-2-one
above, pH and temperature not specified in the publication, 14.7% inhibition at 0.02 mM
3-[6-(4-hydroxyphenyl)hexanoyl]-1,3-oxazolidin-2-one
above, pH and temperature not specified in the publication, 4.9% inhibition at 0.02 mM
4-(4-chlorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
4-methyl-2-oxo-5-phenyl-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(1-methyl-1H-indazol-3-yl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(1-methylpiperidin-4-yl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(2-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(3-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(4-chlorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(4-fluoro-3-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(4-fluorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-(4-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-chloro-3-[(hexylamino)carbonyl]-3,6-dihydro-2,6-dioxo-1(2H)-pyrimidinecarboxylic acid, 2-methylpropyl ester
-
-
5-chloro-N-hexyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
-
5-fluoro-N-hexyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
-
5-fluoro-N-hexyl-3-(2-methylpropanoyl)-2,4-dioxopyrimidine-1-carboxamide
-
5-methyl-2-oxo-4-phenyl-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-[3-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-[4-fluoro-2-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-[4-fluoro-2-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-pentyl-1,3-oxazole-3(2H)-carboxamide
-
5-[4-fluoro-2-(1-methylpiperidin-4-yl)phenyl]-N-(2-methylpropyl)-2-oxo-1,3-oxazole-3(2H)-carboxamide
0.01 mM, 38% inhibition
5-[4-fluoro-3-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
-
5-[4-fluoro-3-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-pentyl-1,3-oxazole-3(2H)-carboxamide
-
5-[4-fluoro-3-(1-methylpiperidin-4-yl)phenyl]-N-(2-methylpropyl)-2-oxo-1,3-oxazole-3(2H)-carboxamide
0.01 mM, 26% inhibition
6-(4-fluorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
-
6-(4-fluorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide}
in vivo plasma pharmacokinetic profile in mice, overview
6-chloro-N-hexyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
-
cardiolipin
-
inhibits the ceramide synthesis activity: total inhibition at 2.5-5 mol%, activates the ceramidase activity, mechanism
Ceranib-1
-
i.e. 3-(3-(4-methoxyphenyl)acryloyl)-6-methyl-4-phenylquinolin-2(1H)-one
cholesterol
-
0.08 mM or below, decreases the hydrolysis of ceramide by a maximum of two-thirds
D-erythro-urea-C16-ceramide
-
mtCDase, competitive inhibition, IC50: 0.33 mol%
ethyl 5-fluoro-3-(hexylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
-
isobutyl 5-fluoro-3-(hexylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
-
LCL521
a lysosomotropic prodrug inhibitor of acid ceramidase, inhibition in vivo leads to decreased cell viability
lysophosphatidylcholine
-
ceramide synthesis activity, 10 mol%, moderate inhibition
methyl 5-fluoro-3-(hexylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
-
methyl 5-fluoro-3-(octylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
-
myristaldehyde
-
competitively inhibits the ceramide synthesis activity, 2.5-3 mol%, about 50% inhibition
N-((1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl)-12-(dimethylamino)dodecanamide
-
-
N-(3-methoxypropyl)-2-oxo-5-phenyl-1,3-oxazole-3(2H)-carboxamide
0.1 mM, 53% inhibition
N-(4-chloro-3-nitrophenyl)-N'-prop-2-en-1-ylthiourea
0.02 mM, 63.38% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
N-(butan-2-yl)-2-oxo-5-phenyl-1,3-oxazole-3(2H)-carboxamide
0.01 mM, 21% inhibition
N-bromosuccinimide
-
modification of Trp completely inhibits forward and reverse reaction
N-hexyl-2,4-dioxo-5-(trifluoromethyl)-3,4-dihydropyrimidine-1(2H)-carboxamide
-
N-hexyl-5,6-dimethyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
-
N-hexyl-5-(4-methylpiperazin-1-yl)-2,4-dioxopyrimidine-1-carboxamide
-
N-hexyl-5-methyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
-
N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]-12-(dimethylamino)dodecanamide
-
N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]dodecane-1-sulfonamide
-
N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]tridecan-1-aminium chloride
-
N-[(1R,2R)-1,3-dihydroxy-1-phenylpropan-2-yl]tridecan-1-aminium chloride
-
N-[(1R,2S)-1-hydroxy-1-phenylpropan-2-yl]-12-(1-methylhydrazinyl)dodecanamide
-
N-[(1S,2R)-1-hydroxy-1-(4-nitrophenyl)propan-2-yl]dodecane-1-sulfonamide
-
N-[(2R)-2-hydroxy-2-(pyridin-3-yl)ethyl]-12-(1-methylhydrazinyl)dodecanamide
-
N-[(2R)-2-hydroxy-2-(pyridin-4-yl)ethyl]-12-(1-methylhydrazinyl)dodecanamide
-
N-[(2S,3R,4E)-14-azido-1,3-dihydroxytetradec-4-en-2-yl]-2-bromoacetamide
-
N-[(3,4-dichlorophenyl)methyl]-N-methyl-1-[(4-methylphenyl)methyl]-5-oxopyrrolidine-3-carboxamide
0.02 mM, 59.17% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
N-[2-hydroxy-2-(pyridin-3-yl)ethyl]-12-(1-methylhydrazinyl)dodecanamide
-
N-[5-(3-[4-[(2-tert-butyl-1,3-dioxolan-2-yl)methoxy]-3-methylphenyl]pentan-3-yl)-7-methyl-1-benzofuran-2-carbonyl]glycine
0.02 mM, 67.39% inhibition. Selective inhibition of acid ceramidase over neural ceramidase
palmitaldehyde
-
ceramide synthesis activity, 2.5-3 mol%, about 50% inhibition
phorbol myristate acetate
-
phorbol myristate acetate, PMA, decreases the expression of ACER2 in HeLa cells
phosphatidylglycerol
-
ceramide synthesis activity, 10 mol%, moderate inhibition
(1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
potent inhibitor of acid ceramidase
(1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
-
(1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
the efficacy of (1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol in vitro as well as in intact cells can be enhanced by suitable modification of functional groups; the efficacy of the inhibitor in vitro as well as in intact cells can be enhanced by suitable modification of functional groups
(1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
-
(1S,2R)-D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
-
i.e. D-e-MAPP, an alkaline ceramidase inhibitor, that potently and specifically inhibits ACER1, ACER2, and ACER3 activity
(1S,2R)-D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
inhibits in vitro
(1S,2R)-D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
-
i.e. D-e-MAPP, an alkaline ceramidase inhibitor, that potently and specifically inhibits ACER activity
2-mercaptoethanol
-
inhibits both ceramidase and ceramide synthesis activity
carmofur
a drug used in treatment of colorectal cancers and a potent in vivo active inhibitor of intracellular acid ceramidase activity. The potent noncompetitive inhibitor enzyme inhibitor has is anti-proliferative effects. Carmofur inhibits acid ceramidase and increases ceramide levels in human SW403 and LNCaP cells
carmofur
a specific ASAH1 inhibitor, inhibition by carmofur contributes to cytotoxicity
carmofur
a drug used in treatment of human colorectal cancers and a potent noncompetitive inhibitor in vivo active inhibitor of intracellular acid ceramidase activity
Ceranib-2
-
a specific acid ceramidase inhibitor, reduces SARS-CoV-2 replication
D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
-
inhibitor of alkaline ceramidase
D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
-
inhibitor of alkaline ceramidase
D-erythro-sphingosine
recombinant CDase, more inhibitory than L-erythro-sphingosine
D-erythro-sphingosine
-
IC50: 0.04 mol%, mt-CDase is inhibited by all stereoisomers of sphingosine with IC50 ranging from 0.04 to 0.14 mol%
di-isopropyl fluorophosphate
the substrate protects against inhibition
EDTA
recombinant CDase, complete inhibition, Ca2+ restores activity
EGTA
recombinant CDase, complete inhibition, Ca2+ restores activity
glycodeoxycholate
inhibits in vitro neutral ceramidase activity
L-erythro-sphingosine
recombinant CDase, 0.02 mM, 20% inhibition, less inhibitory than L-erythro-sphingosine
L-erythro-sphingosine
-
competitive inhibitor of ceramide synthesis activity
N-oleoylethanolamine
low potency, inhibitor of acid ceramidase
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]2,2-dibromoacetamide
strong inhibition
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]2-bromoacetamide
strong inhibition
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]2-methylacrylamide
strong inhibition
oleoylethanolamide
i.e. N-oleylethanolamine; i.e. N-oleylethanolamine
oleoylethanolamide
i.e. N-oleylethanolamine; i.e. N-oleylethanolamine
phosphatidic acid
-
ceramide synthesis activity, 2.5-5 mol%, total inhibition
phosphatidylcholine
inhibitor of alkaline ceramidase; inhibitor of alkaline ceramidase; inhibitor of neutral ceramidase
phosphatidylcholine
-
ceramide synthesis activity, 10 mol%, moderate inhibition
phosphatidylserine
-
ceramide synthesis activity, 10 mol%, moderate inhibition
taurocholate
inhibits in vitro neutral ceramidase activity
taurodeoxycholate
inhibits in vitro neutral ceramidase activity
Triton X-100
2fold activation at 0.1-0.2%, but inhibitory beyond the optimum concentration
additional information
-
no inhibition by phosphatidylethanolamine, phosphatidylinositol, phosphatidylglycerol
-
additional information
no inhibition by protease inhibitors such as aprotinin, PMSF, leupeptin, and pepstatin
-
additional information
-
no inhibition by protease inhibitors such as aprotinin, PMSF, leupeptin, and pepstatin
-
additional information
-
desipramine downregulates acid ceramidase in cancer cells, which is almost completely reversible by leupeptin and CA074ME, but not by pepstatin A, mechanism, overview
-
additional information
-
cellular ACER2 activity is inhibited by depletion of Ca2+ from Golgi lumen
-
additional information
-
N-methyl ceramide, 1-O-methyl ceramide, cis-D-erythro ceramide or N,N-dimethyl-D-erythrosphingosine have no effect on neutral ceramidase; all stereoisomers of D-erythro-ceramide and sphingosine (L-threo, D-threo, and L-erythro isomers), N-methyl-D-erythro-sphingosine and D-erythro-urea-C16-ceramide show significant inhibitory effects on neural ceramidase
-
additional information
N-methyl ceramide, 1-O-methyl ceramide, cis-D-erythro ceramide or N,N-dimethyl-D-erythrosphingosine have no effect on neutral ceramidase; all stereoisomers of D-erythro-ceramide and sphingosine (L-threo, D-threo, and L-erythro isomers), N-methyl-D-erythro-sphingosine and D-erythro-urea-C16-ceramide show significant inhibitory effects on neural ceramidase
-
additional information
N-methyl ceramide, 1-O-methyl ceramide, cis-D-erythro ceramide or N,N-dimethyl-D-erythrosphingosine have no effect on neutral ceramidase; all stereoisomers of D-erythro-ceramide and sphingosine (L-threo, D-threo, and L-erythro isomers), N-methyl-D-erythro-sphingosine and D-erythro-urea-C16-ceramide show significant inhibitory effects on neural ceramidase
-
additional information
N-methyl ceramide, 1-O-methyl ceramide, cis-D-erythro ceramide or N,N-dimethyl-D-erythrosphingosine have no effect on neutral ceramidase; all stereoisomers of D-erythro-ceramide and sphingosine (L-threo, D-threo, and L-erythro isomers), N-methyl-D-erythro-sphingosine and D-erythro-urea-C16-ceramide show significant inhibitory effects on neural ceramidase
-
additional information
-
DMAPP has no affect on ceramidase activity up to at least 0.3 mM. N-oleoylethanolamine has no affect on ceramidase activity
-
additional information
a class of benzoxazolone carboxamides act as the first potent and systemically active inhibitors of the acid ceramidase. Prototype members of this class inhibit the enzyme with low nanomolar potency by covalent binding to the catalytic cysteine. No inhibition by N-methyl-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide, 4-phenylbutyl 2-oxo-1,3-benzoxazole-3(2H)-carboxylate, and 3-(6-phenylhexanoyl)-1,3-benzoxazol-2(3H)-one, while 2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carbothioamide is unstable
-
additional information
amide- and sulfonamide-based compounds as potential inhibitors of ceramidases, synthesis and inhibitory potencies, overview. The hydrophobicity and the steric effects of longer alkyl chains (n-Pr, n-Bu or t-Bu groups) at the phenyl ring are important for an enhanced selectivity towards acid ceramidase over neutral ceramidase
-
additional information
amide- and sulfonamide-based compounds as potential inhibitors of ceramidases, synthesis and inhibitory potencies, overview. The hydrophobicity and the steric effects of longer alkyl chains (n-Pr, n-Bu or t-Bu groups) at the phenyl ring are important for an enhanced selectivity towards acid ceramidase over neutral ceramidase
-
additional information
structural modification of the known ceramidase inhibitors (1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol and N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]-12-(dimethylamino)dodecanamide generates more potent ceramidase inhibitors that are active in intact cells and not only elevates the cellular ceramide levels, but also enhances cell death
-
additional information
structural modification of the known ceramidase inhibitors (1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol and N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]-12-(dimethylamino)dodecanamide generates more potent ceramidase inhibitors that are active in intact cells and not only elevates the cellular ceramide levels, but also enhances cell death
-
additional information
modifications in the chemical scaffold of carmofur yield acid ceramidase inhibitors that act synergistically with standard antitumoral drugs to prevent cancer cell proliferation, design of chemosensitizing agents, overview
-
additional information
-
modifications in the chemical scaffold of carmofur yield acid ceramidase inhibitors that act synergistically with standard antitumoral drugs to prevent cancer cell proliferation, design of chemosensitizing agents, overview
-
additional information
synthesis of several analogues of SABRAC that are potent irreversible enzyme inhibitors by reaction with the active site Cys143, fluorescent SABRAC analogues are used for enzyme detection
-
additional information
a selective inhibitor of ACER3 with drug-like properties is described, which is active in living cells. Discovery and mechanism of action of small molecule inhibitors of ceramidases
-
additional information
not inhibited by Mg2+, phytosphingosine, dihydrosphingosine
-
additional information
-
not inhibited by Mg2+, phytosphingosine, dihydrosphingosine
-
additional information
a class of benzoxazolone carboxamides act as the first potent and systemically active inhibitors of the acid ceramidase. Prototype members of this class inhibit the enzyme with low nanomolar potency by covalent binding to the catalytic cysteine. No inhibition by N-methyl-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide, 4-phenylbutyl 2-oxo-1,3-benzoxazole-3(2H)-carboxylate, and 3-(6-phenylhexanoyl)-1,3-benzoxazol-2(3H)-one, while 2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carbothioamide is unstable
-
additional information
not inhibited by 1 mM iodoacetic acid, 0.1 mM 2-mercaptoethanol, 0.05 mM hexadecylsulfonylfluoride, 1 mM p-phenylmethylsulfonylfluoride, 0.2 mM D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol, 0.5 mM N-oleoylethanolamine, L(-)- and D(-)-norephenedrin
-
additional information
-
not inhibited by N-methyl-hexadecanoyl-ceramide, 1-O-methyl-hexadecanoyl-ceramide, 3-O-methyl-hexadecanoyl-ceramide, cis-D-erythro-hexadecanoyl-ceramide, 3-O-methyl-D-erythro-sphingosine, requirements for inhibition of mtCDase
-
additional information
-
the ceramide synthesis activity is not inhibited in vitro and in cells by fuminosin B1, not inhibited by EDTA or ATP, both up to 10 mM
-
additional information
EDTA, Mn2+ and Mg2+ have little effect on activity of 112 kDa CDase from kidney
-
additional information
-
the enzyme is stable to trypsin and chymotrypsin exposure
-
additional information
no inhibition by protease inhibitors such as aprotinin, PMSF, leupeptin, and pepstatin
-
additional information
-
GMP, GDT, GTP, TDP, TTP, UDP, and UTP, ADP and AMP have no significant effects on the enzyme activity. S-1-P has no inhibitory effect
-
additional information
synthesis and evaluation of a series of 2,4-dioxopyrimidine-1-carboxamides as acid ceramidase enzyme inhibitors, structural features of uracil derivatives that are critical for inhibition, overview. No inhibition by 7 and 27b, while 4o, 26 and 30 are unstable
-
additional information
the reverse ceramidase activity in microsomes can only be blocked by a lysine residuespecific reagent when the reagent has access to Ypc1p from the lumenal side
-
additional information
the reverse ceramidase activity in microsomes can only be blocked by a lysine residuespecific reagent when the reagent has access to Ypc1p from the lumenal side
-
additional information
-
the reverse ceramidase activity in microsomes can only be blocked by a lysine residuespecific reagent when the reagent has access to Ypc1p from the lumenal side
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
-
a bile salt analog
adiponectin
activates the ceramidase activity of adiponectin receptor ADIPOR2 about 20fold. Adiponectin is a hormone, secreted mainly from adipocytes, that stimulates glucose utilization and fatty-acid oxidation
-
all-trans retinoic acid
-
all-trans retinoic acid, ATRA, increases the expression of ACER2 in HeLa cells
cAMP-responsive element binding protein
-
CREB is a central regulator os ASAH1 gene transcription
-
cytokine
a cytokine mixture of interleukin-1beta, tumor necrose factor-alpha and interferon-gamma is used
-
Detergents
-
required for activity, e.g. NP-40, sodium cholate, Triton X-100, or Tween-20
N-(4-hydroxyphenyl)retinamide
increases isoform ACER2 activity and mRNA, but not isoforms ACER1 or ACER3
saposin-D
a hydrophobic surface surrounding the substrate binding channel appears to be a site of membrane attachment where the enzyme accepts substrates facilitated by the accessory protein, saposin-D
-
cardiolipin
-
phosphatidylglycerol and cardiolipin, which are major lipid components of Staphylococcus aureus, are effective in stimulating the hydrolysis of human skin-type ceramides in the absence of detergents
cardiolipin
-
activates the ceramidase activity by 2.5fold at 8-10 mol%, inhibits the ceramide synthesis activity, mechanism
phosphatidylglycerol
-
phosphatidylglycerol and cardiolipin, which are major lipid components of Staphylococcus aureus, are effective in stimulating the hydrolysis of human skin-type ceramides in the absence of detergents
sodium cholate
112 kDa CDase from kidney, optimum concentration: 0.4-2%, 4-5fold activation
sodium taurodeoxycholate
-
activates the recombinant enzyme about 2fold, optimally at 1%
sodium taurodeoxycholate
112 kDa CDase from kidney, optimum concentration: 0.1-0.2%, 4-5fold activation
Triton X-100
-
activates the recombinant enzyme about 2fold, optimally at 0.05%
Triton X-100
2fold activation at 0.1-0.2%, but inhibitory beyond the optimum concentration
additional information
phosphatidylethanolamine and phosphatidylcholine have little effect on the activity regardless of the concentration
-
additional information
Bac-Dacer microsomes cause a twofold increase in ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide at pH 9.0
-
additional information
-
Bac-Dacer microsomes cause a twofold increase in ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide at pH 9.0
-
additional information
serum deprivation up-regulates both haCER2 mRNA and activity in recombinant HeLa cells, haCER2mRNA is also up-regulated in some tumors
-
additional information
-
serum deprivation up-regulates both haCER2 mRNA and activity in recombinant HeLa cells, haCER2mRNA is also up-regulated in some tumors
-
additional information
-
acid ceramidase requires anionic lysosomal lipids and saposin as cofactors for efficient hydrolysis of ceramide in vivo
-
additional information
acid ceramidase requires anionic lysosomal lipids and saposin as cofactors for efficient hydrolysis of ceramide in vivo
-
additional information
acid ceramidase requires anionic lysosomal lipids and saposin as cofactors for efficient hydrolysis of ceramide in vivo
-
additional information
acid ceramidase requires anionic lysosomal lipids and saposin as cofactors for efficient hydrolysis of ceramide in vivo
-
additional information
-
ACTH/cAMP signaling stimulates the enzyme transcription and activity
-
additional information
ACTH/cAMP signaling stimulates the enzyme transcription and activity
-
additional information
infection with the rice strip virus or treatment with insecticides significantly increase LsnCer mRNA expression and its enzymatic activity in Laodelphax striatellus
-
additional information
-
infection with the rice strip virus or treatment with insecticides significantly increase LsnCer mRNA expression and its enzymatic activity in Laodelphax striatellus
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
(13E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]docos-13-enamide
pH 7.4, 37°C
0.04
(15E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]tetracos-15-enamide
pH 7.4, 37°C
0.042
(2R)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide
pH 7.4, 37°C
0.087 - 0.19
(2R,3Z)-2-([(2E)-1-hydroxy-12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodec-2-en-1-yl]amino)heptadec-3-ene-1,3-diol
0.021
(2S)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide
pH 7.4, 37°C
0.0005
(4E,2S,3R)-2-N-(10-pyrenedecanoyl)-1,3,17-trihydroxy-17-(3,5-dinitrobenzoyl)-4-heptadecene
-
-
0.139
(9E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]octadec-9-enamide
pH 7.4, 37°C
0.016
2,4-dideoxy-2-(hexadecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.028
2,4-dideoxy-2-[[(13E)-docos-13-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.016
2,4-dideoxy-2-[[(2R)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.014
2,4-dideoxy-2-[[(2S)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.028
2,4-dideoxy-2-[[(9E)-octadec-9-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.08
2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-2-[[(15E)-tetracos-15-enoyl]amino]-D-erythro-pentitol
pH 7.4, 37°C
0.0987
N-dodecanoyl-7-nitrobenz-2-oxa-1,3,4-diazole-D-erythro-sphingosine
-
pH 8.0, 37°C
0.193 - 0.204
N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide
0.085 - 0.11
N-[(2S,3R,4E)-1,3-dihydroxynonadec-4-en-2-yl]-12-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]dodecanamide
0.036 - 0.082
N-[(2S,3R,4E)-13-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-1,3-dihydroxytridec-4-en-2-yl]hexadecanamide
0.1418 - 0.1818
N-[(2S,3R,4E)-7-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-3-yl]oxy]-1,3-dihydroxyhept-4-en-2-yl]-11-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]undecanamide
0.01548 - 0.066
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amine]dodecanoyl]D-erythro-sphingosine
-
0.00332
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]lauroyl]-sphingosine
pH 4.0, 40°C
0.087
(2R,3Z)-2-([(2E)-1-hydroxy-12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodec-2-en-1-yl]amino)heptadec-3-ene-1,3-diol
pH 4.5, 37°C, recombinant enzyme
0.19
(2R,3Z)-2-([(2E)-1-hydroxy-12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodec-2-en-1-yl]amino)heptadec-3-ene-1,3-diol
pH 7.0, 37°C, recombinant enzyme
0.06
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide
pH 7.5, 37°C, recombinant enzyme
0.0601
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide
pH 7.5, 37°C, recombinant enzyme
0.389
N-lauroylsphingosine
-
pH 4.5, 37°C, recombinant AC expressed in CHO cells, 14C-labeled substrate
0.389
N-lauroylsphingosine
pH 4.5, 37°C, 14C-labeled substrate
0.4132
N-lauroylsphingosine
-
pH 4.5, 37°C, recombinant AC expressed in CHO cells, BODIPY-conjugated substrate
0.4132
N-lauroylsphingosine
pH 4.5, 37°C, BODIPY-conjugated substrate
0.193
N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide
pH 7.0, 37°C, recombinant enzyme
0.204
N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide
pH 4.5, 37°C, recombinant enzyme
0.085
N-[(2S,3R,4E)-1,3-dihydroxynonadec-4-en-2-yl]-12-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]dodecanamide
pH 7.0, 37°C, recombinant enzyme
0.11
N-[(2S,3R,4E)-1,3-dihydroxynonadec-4-en-2-yl]-12-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]dodecanamide
pH 4.5, 37°C, recombinant enzyme
0.036
N-[(2S,3R,4E)-13-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-1,3-dihydroxytridec-4-en-2-yl]hexadecanamide
pH 7.0, 37°C, recombinant enzyme
0.082
N-[(2S,3R,4E)-13-[[9-(ethylamino)-5-oxo-5H-benzo[a]phenoxazin-2-yl]oxy]-1,3-dihydroxytridec-4-en-2-yl]hexadecanamide
pH 4.5, 37°C, recombinant enzyme
0.1418
N-[(2S,3R,4E)-7-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-3-yl]oxy]-1,3-dihydroxyhept-4-en-2-yl]-11-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]undecanamide
pH 7.0, 37°C
0.1818
N-[(2S,3R,4E)-7-[[9-(diethylamino)-5-oxo-5H-benzo[a]phenoxazin-3-yl]oxy]-1,3-dihydroxyhept-4-en-2-yl]-11-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]undecanamide
pH 4.5, 37°C
0.01548
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amine]dodecanoyl]D-erythro-sphingosine
pH 9.4, 37°C, wild-type enzyme, i.e. D-ribo-C12-NBD-phytoceramide
-
0.038
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amine]dodecanoyl]D-erythro-sphingosine
pH 9.4, 37°C, mutant enzyme S77A, i.e. D-ribo-C12-NBD-phytoceramide
-
0.066
N-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amine]dodecanoyl]D-erythro-sphingosine
pH 7.5, 37°C, mutant enzyme S77C, i.e. D-ribo-C12-NBD-phytoceramide
-
additional information
additional information
-
kinetic data for the ceramide synthesis reaction, random sequential kinetic mechanism
-
additional information
additional information
classical MichaelisMenten kinetics
-
additional information
additional information
-
classical MichaelisMenten kinetics
-
additional information
additional information
-
ACER2 follows Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics of hydrolysis, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
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
0.004977
(13E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]docos-13-enamide
pH 7.4, 37°C
0.008415
(15E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]tetracos-15-enamide
pH 7.4, 37°C
0.022954
(2R)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide
pH 7.4, 37°C
0.007257
(2S)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide
pH 7.4, 37°C
0.1
(4E,2S,3R)-2-N-(10-pyrenedecanoyl)-1,3,17-trihydroxy-17-(3,5-dinitrobenzoyl)-4-heptadecene
-
-
0.003761
(9E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]octadec-9-enamide
pH 7.4, 37°C
0.00328
2,4-dideoxy-2-(hexadecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.001397
2,4-dideoxy-2-[[(13E)-docos-13-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.002655
2,4-dideoxy-2-[[(2R)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.003075
2,4-dideoxy-2-[[(2S)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.000423
2,4-dideoxy-2-[[(9E)-octadec-9-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.001581
2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-2-[[(15E)-tetracos-15-enoyl]amino]-D-erythro-pentitol
pH 7.4, 37°C
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
0.1508
(13E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]docos-13-enamide
pH 7.4, 37°C
0.2104
(15E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]tetracos-15-enamide
pH 7.4, 37°C
0.5465
(2R)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide
pH 7.4, 37°C
0.3456
(2S)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]-2-hydroxyicosanamide
pH 7.4, 37°C
0.0271
(9E)-N-[(2S,3R,4E)-1,3-dihydroxy-7-[(2-oxo-2H-1-benzopyran-7-yl)oxy]hept-4-en-2-yl]octadec-9-enamide
pH 7.4, 37°C
0.02051
2,4-dideoxy-2-(hexadecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.0499
2,4-dideoxy-2-[[(13E)-docos-13-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.1659
2,4-dideoxy-2-[[(2R)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.2196
2,4-dideoxy-2-[[(2S)-2-hydroxyicosanoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.0154
2,4-dideoxy-2-[[(9E)-octadec-9-enoyl]amino]-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
pH 7.4, 37°C
0.1976
2,4-dideoxy-5-O-(2-oxo-2H-1-benzopyran-7-yl)-2-[[(15E)-tetracos-15-enoyl]amino]-D-erythro-pentitol
pH 7.4, 37°C
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
0.0000297
2-bromo-N-[(2S,3R,4E)-1,3-dihydroxyoctadec-4-en-2-yl]acetamide
25 mM sodium acetate buffer, pH 4.5, 37°C, substrate 2,4-dideoxy-2-(dodecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
0.0000971
2-chloro-N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]acetamide
25 mM sodium acetate buffer, pH 4.5, 37°C, substrate 2,4-dideoxy-2-(dodecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
0.0000267
Bodipy-SOBRAC
25 mM sodium acetate buffer, pH 4.5, 37°C, substrate 2,4-dideoxy-2-(dodecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
0.0000988
Bodipy-SOCLAC
25 mM sodium acetate buffer, pH 4.5, 37°C, substrate 2,4-dideoxy-2-(dodecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
0.0000357
N-[(2S,3R,4E)-14-azido-1,3-dihydroxytetradec-4-en-2-yl]-2-bromoacetamide
25 mM sodium acetate buffer, pH 4.5, 37°C, substrate 2,4-dideoxy-2-(dodecanoylamino)-5-O-(2-oxo-2H-1-benzopyran-7-yl)-D-erythro-pentitol
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
0.042
(1R,2R)-2- N-(tetradecylamino)-1-phenyl-1,3-propandiol hydrochloride
Homo sapiens
pH and temperature not specified in the publication
-
0.01
(1R,2R)-2-(tetradecanoylamino)-1-(4'-nitrophenyl-1,3-propandiol)
Homo sapiens
pH and temperature not specified in the publication
-
0.015
(2R,3Z)-N-(1-hydroxyoctadec-3-en-2-yl)pivaloylamide
Homo sapiens
pH and temperature not specified in the publication
-
0.0111
(2S)-3-([5-[(1S)-1-[[2,6-dimethyl-4'-(trifluoromethyl)[1,1'-biphenyl]-4-yl]oxy]-2-methylpropyl]thiophene-2-carbonyl]amino)-2-hydroxypropanoic acid
Homo sapiens
pH 4.5, 37°C
0.0158
1-(4-carbamoylanilino)-1-oxopropan-2-yl (4E)-2-tert-butyl-4-[(thiophen-2-yl)methylidene]-1,2,3,4-tetrahydroacridine-9-carboxylate
Homo sapiens
pH 4.5, 37°C
0.000029
1-hexylcarbamoyl-5-fluorouracil
Homo sapiens
pH and temperature not specified in the publication
0.000007
2-oxo-4-phenyl-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00009
2-oxo-5-phenyl-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000064
2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
Homo sapiens
pH 7.4, 37°C
0.000059
2-oxo-N-(4-phenylbutyl)-5-(1,3-thiazol-2-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000044
2-oxo-N-(4-phenylbutyl)-5-(1,3-thiazol-4-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000032
2-oxo-N-(4-phenylbutyl)-5-(pyrazin-2-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000025
2-oxo-N-(4-phenylbutyl)-5-(pyridin-2-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00007
2-oxo-N-(4-phenylbutyl)-5-(pyridin-3-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000018
2-oxo-N-(4-phenylbutyl)-5-(pyridin-4-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000037
2-oxo-N-(4-phenylbutyl)-5-(quinoxalin-2-yl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000025
2-oxo-N-pentyl-4-phenyl-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000039
2-oxo-N-pentyl-5-phenyl-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0367
2-[3-(4-butylphenyl)-3-oxopropyl]-1H-indene-1,3(2H)-dione
Homo sapiens
pH 4.5, 37°C
0.0489
3,3-dimethyl-1-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]butan-1-one
Homo sapiens
pH 4.5, 37°C
0.00027
3-(6-phenylhexanoyl)-1,3-oxazolidin-2-one
Rattus norvegicus
above, pH and temperature not specified in the publication
0.000061
3-(cyclopropylmethyl)-5-fluoro-N-hexyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.00002
3-benzoyl-5-fluoro-N-hexyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.0106
3-bromo-N-methyl-N-[2-(pyridin-2-yl)ethyl]benzene-1-sulfonamide
Homo sapiens
pH 4.5, 37°C
0.000018
3-ethyl-5-fluoro-N-hexyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.028
3-[(2E)-3-(4-methoxyphenyl)-1-oxo-2-propen-1-yl]-6-methyl-4-phenyl-2(1H)-quinolinone
Homo sapiens
pH and temperature not specified in the publication
-
0.000092
3-[4-(cyclohexyloxy)benzoyl]-1,3-oxazolidin-2-one
Rattus norvegicus
above, pH and temperature not specified in the publication
0.000009
3-[6-(3-chlorophenyl)hexanoyl]-1,3-oxazolidin-2-one
Rattus norvegicus
above, pH and temperature not specified in the publication
0.000061
3-[6-(4-hydroxyphenyl)hexanoyl]-1,3-oxazolidin-2-one
Rattus norvegicus
above, pH and temperature not specified in the publication
0.000005
4-(4-chlorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000069
4-methyl-2-oxo-5-phenyl-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000092
5-(1-methyl-1H-indazol-3-yl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
5-(1-methylpiperidin-4-yl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000177
5-(2-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000341
5-(3-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000083
5-(4-chlorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00008
5-(4-fluoro-3-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000185
5-(4-fluorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0004
5-(4-methoxyphenyl)-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0055
5-(benzyl(methyl)amino)-N-hexyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.0015
5-chloro-3-[(hexylamino)carbonyl]-3,6-dihydro-2,6-dioxo-1(2H)-pyrimidinecarboxylic acid, 2-methylpropyl ester
Homo sapiens
pH and temperature not specified in the publication
-
0.000067
5-chloro-N-hexyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000067
5-chloro-N-hexyl-2,4-dioxo-pyrimidine-1-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000733
5-ethyl-N-hexyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000029
5-fluoro-N-hexyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000021
5-fluoro-N-hexyl-3-(2-methylpropanoyl)-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000013
5-fluoro-N-hexyl-3-methyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.0000046
5-fluoro-N-octyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000042
5-methyl-2-oxo-4-phenyl-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000012
5-trifluoromethyl-N-hexyl-2,4-dioxo-pyrimidine-1-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000153
5-[3-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000337
5-[4-fluoro-2-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000129
5-[4-fluoro-2-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-pentyl-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000341
5-[4-fluoro-3-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-(4-phenylbutyl)-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.001923
5-[4-fluoro-3-(1-methylpiperidin-4-yl)phenyl]-2-oxo-N-pentyl-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000079
6-(4-fluorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
Homo sapiens
pH 7.4, 37°C
0.000031
6-bromo-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
Homo sapiens
pH 7.4, 37°C
0.000029
carmofur
Rattus norvegicus
pH and temperature not specified in the publication
20
EDTA
Rattus norvegicus
-
in 50 mM Tris (pH 7.5) containing 0.3% (v/v) Triton X-100, at 37°C
0.000012
ethyl 5-fluoro-3-(hexylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
Rattus norvegicus
pH 4.5, 37°C
1
Fe3+
Rattus norvegicus
-
in 50 mM Tris (pH 7.5) containing 0.3% (v/v) Triton X-100, at 37°C
0.000016
isobutyl 5-fluoro-3-(hexylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
Rattus norvegicus
pH 4.5, 37°C
0.000007
methyl 5-fluoro-3-(hexylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
Rattus norvegicus
pH 4.5, 37°C
0.000004
methyl 5-fluoro-3-(octylcarbamoyl)-2,6-dioxopyrimidine-1-carboxylate
Rattus norvegicus
pH 4.5, 37°C
0.05
N-((1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl)-12-(dimethylamino)dodecanamide
Homo sapiens
pH and temperature not specified in the publication
-
0.002 - 4
N-(2-ethoxyethyl)-2-oxo-5-phenyl-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0017
N-(2-methylpropyl)-2-oxo-5-phenyl-1,3-oxazole-3(2H)-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000426
N-hexyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000012
N-hexyl-2,4-dioxo-5-(trifluoromethyl)-3,4-dihydropyrimidine-1(2H)-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000177
N-hexyl-2,4-dioxo-5-phenylpyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000426
N-hexyl-2,4-dioxo-pyrimidine-1-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000053
N-hexyl-3-methyl-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.0014
N-hexyl-5-(4-methylpiperazin-1-yl)-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000417
N-hexyl-5-(hydroxymethyl)-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000051
N-hexyl-5-bromo-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000147
N-hexyl-5-iodo-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.0011
N-hexyl-5-methoxy-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.00146
N-hexyl-5-methyl-2,4-dioxo-3,4-dihydropyrimidine-1(2H)-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.0015
N-hexyl-5-methyl-2,4-dioxo-pyrimidine-1-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0034
N-hexyl-5-methylamino-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000875
N-hexyl-5-morpholino-2,4-dioxopyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.000007
N-octyl-2,4-dioxo-5-(trifluoromethyl)pyrimidine-1-carboxamide
Rattus norvegicus
pH 4.5, 37°C
0.5
N-oleoylethanolamine
Homo sapiens
pH and temperature not specified in the publication
0.00053
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]2,2-dibromoacetamide
Homo sapiens
pH and temperature not specified in the publication
0.000052
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]2-bromoacetamide
Homo sapiens
pH and temperature not specified in the publication
0.0112
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]2-methylacrylamide
Homo sapiens
pH and temperature not specified in the publication
0.0239
N-[(3,4-dichlorophenyl)methyl]-N-methyl-1-[(4-methylphenyl)methyl]-5-oxopyrrolidine-3-carboxamide
Homo sapiens
pH 4.5, 37°C
0.0066
N-[5-(3-[4-[(2-tert-butyl-1,3-dioxolan-2-yl)methoxy]-3-methylphenyl]pentan-3-yl)-7-methyl-1-benzofuran-2-carbonyl]glycine
Homo sapiens
pH 4.5, 37°C
0.08
sphingosine
Mus musculus
product inhibition in a dose-dependent manner, IC50: 0.08 mM
5
Zn2+
Rattus norvegicus
-
in 50 mM Tris (pH 7.5) containing 0.3% (v/v) Triton X-100, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000002
0.0000208
0.00125
CDase null mutant and CDase null expressing fat body driven CDase
0.0338
-
pH 4.5, 37°C, recombinant AC expressed in CHO cells, hydrolysis of N-lauroylsphingosine
0.218
intracellular recombinant CDase expressed in Escherichia coli DH5alpha, pH 8.5, hydrolysis of N-palmitoyl sphingosine
0.239
extracellular wild-type CDase, pH 8.5, hydrolysis of N-palmitoyl sphingosine
1.91
pH 7.5, 37°C, 112 kDa CDase from kidney, hydrolysis of 4-nitrobenzo-2-oxa-1,3-diazoyl-N-dodecanoylsphingosine
additional information
additional information
sphingolipid level analysis by mass spectrometry, overview
additional information
-
sphingolipid level analysis by mass spectrometry, overview
additional information
relative activities of isozymes during keratinocyte differentiation, tissue distribution of isozymes expression levels, overview
additional information
relative activities of wild-type and mutant enzymes, overview
additional information
-
relative activities of wild-type and mutant enzymes, overview
additional information
-
determination of sphingolipid levels by mass spectrometry
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.5
4.5
5.5 - 6
-
ceramide synthesis reaction, distinct pH-optima for the degradative and synthetic reaction
6 - 7
6 - 8
7 - 10
7.4
7.5
8 - 9
8.5
9.4
9.5
4.5
-
ceramidase reaction, distinct pH-optima for the degradative and synthetic reaction
5
synthesis reaction, with NBD-dodecanoic acid and sphingosine as substrates
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
5 - 11
6 - 9
6.5 - 10.5
maCER1 has a negligible activity at pH lower than 6.5 or higher than 10.5
additional information
-
NlnCDase enzyme has a broad pH range for its activity
4 - 10
-
activity range, recombinant enzyme, forward reaction, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
recombinant CDase from inclusion bodies, expressed in Escherichia coli BL21 without its signal peptide, isoelectric focusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
696443, 697862, 700316, 711799, 711949, 711958, 712489, 712496, 718697, 719197, 719536, 719608, 719918, 720438, 720471
-
-
brenda
five isozymes: acid ceramidase, neutral ceramidase, and three alkaline ceramidases ACER1, ACER2, and ACER3
-
-
brenda
five isozymes: acid, neutral, phytoalkaline, and alkaline-1 and -2 isozymes
SwissProt
brenda
F508del mouse, mouse model with well-characterized intestinal pathology
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
acid ceramidase is an essential factor required for embryo survival that functions by removing ceramide from the newly formed embryos, thus inhibiting the default apoptosis pathway
brenda
a significantly lower level of acid ceramidase expression was detected in gingival tissues from periodontal patients compared to those from healthy subjects
brenda
-
skin squamous cell carcinoma cells, express very low levels of ACER3
brenda
-
alkaline ceramidase activity and the generation of sphingosine and sphingosine-1-phosphate are increased during erythroid differentiation in K562 erythroleukemic cells, e.g. induced by chemotherapeutic agent cytosine arabinoside, Ara-C
brenda
SJGBM2-10y cell medium, which is rich in secreted ASAH1, promotes 50% more cell growth than SJGBM2 medium containing a lower level of secreted ASAH1
brenda
additional information
neutral ceramidase is highly expressed in colorectal tissues
brenda
enzyme expression vector, recombinant enzyme
brenda
-
when the strain is cultured with sphingomyelin or phosphatidylcholine, production of the enzyme drastically increases, causing the increase of hemolytic activity in the cellfree culture supernatant. Ceramide and sphingosine are effective in promoting the production of ceramidase
brenda
-
when the strain is cultured with sphingomyelin or phosphatidylcholine, production of the enzyme drastically increases, causing the increase of hemolytic activity in the cellfree culture supernatant. Ceramide and sphingosine are effective in promoting the production of ceramidase
-
brenda
-
acid ceramidase is closely associated with malignant progression in human prostate cancer tissues. Acid ceramidase upregulation generates tumor cells that are resistant to normal homeostatic control mechanisms, have an increased number of metastatic characteristics and exhibit resistance to chemotherapy
brenda
differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis, distribution of acid and alkaline isozymes, overview
brenda
differentiated interfollicular epidermis, high expression
brenda
ubiquitously expressed in human tissues, with a particularly high expression in the heart and kidney
brenda
in rat hepatocytes, neutral CDase signals appear as many foci distributed throughout the cytoplasm partially co-localizing with the LPG85 signal, a marker for lysosomes/late endosomes
brenda
a strong signal for neutral CDase is detected in zebrafish intestine at the luminal surface of the villi and microvilli of adsorptive epithelial cells
brenda
-
neutral ceramidase is expressed in the intestine and released in the intestinal lumen
brenda
highly expressed in intestinal system
brenda
-
neutral ceramidase activities both in the intestinal mucosa and content are reduced by bile diversion. The presence of bile salts is important for maintaining high intraluminal levels of neutral ceramidase
brenda
differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis
brenda
Ca2+ markedly upregulates the human acid ceramidase. Its upregulation mediates the Ca2+-induced growth arrest and differentiation of human epidermal keratinocytes by sphingosine and sphingosine phosphate
brenda
Ca2+ markedly upregulates the human alkaline ceramidase 1. Its upregulation mediates the Ca2+-induced growth arrest and differentiation of human epidermal keratinocytes by sphingosine and sphingosine phosphate
brenda
ubiquitously expressed in human tissues, with a particularly high expression in the heart and kidney
brenda
high CDase expression, enzyme is mainly localized at the apical membrane of proximal tubules, distal tubules and collecting ducts, enzyme is enriched in the raft microdomains with cholesterol and GM1 ganglioside
brenda
high expression level of neutral ceramidase, at the top of themicrovilli in proximal tubule cells
brenda
low CDase expression, enzyme is distributed with late endosomes/lysosomes in hepatocytes
brenda
human melanoma biopsies reveal heterogeneous staining of ASAH1 and low ASAH1 expression at the melanoma invasive front. ASAH1 is highly expressed and active in about 60% of melanoma cells, and its expression correlates with that of MITF
brenda
the enzyme is localized in the nuclei of H295R adrenocortical cells
brenda
-
acid ceramidase is an essential component of the in vivo oocyte and embryo environment, it is expressed in the cortex and membrane at all stages of human oocyte maturation, expression analysis, overview
brenda
high enzyme level, increased expression of acid ceramidase in highly metastatic clones derived from PC-3 prostate cancer cells. The highly aggressive and metastatic PC-3/Mc cells display levels of acid ceramidase activity that are 2.5 to 4times higher than those of PC-3/S cells
brenda
-
acid ceramidase is closely associated with malignant progression in human prostate cancer tissues. Acid ceramidase upregulation generates tumor cells that are resistant to normal homeostatic control mechanisms, have an increased number of metastatic characteristics and exhibit resistance to chemotherapy
brenda
predominantly expressed in skin
brenda
only expressed at the intestinal brush border of the small intestine
brenda
highest expression level of neutral ceramidase, on the epithelial mucosa in the jejunum and ileum, neutral CDase is highly expressed in the small intestine along the brush border
brenda
additional information
tissue localization study, expression analysis, overview
brenda
additional information
high mRNA levels in the pupal stage
brenda
additional information
-
high mRNA levels in the pupal stage
-
brenda
additional information
-
quantitation of acid ceramidase mRNA, overview, little ceramidase protein or activity, or sphingosine, in monocytes
brenda
additional information
isozyme tissue distribution, alkaline isozyme 1 is active for epidermis, small intestine, and thymus, all other isozymes are abundant, overview
brenda
additional information
neutral ceramidase is ubiquitously expressed in various mammalian tissues
brenda
additional information
the nCDase subtype is a ubiquitously expressed enzyme
brenda
additional information
acid ceramidase is abnormally expressed in various types of human cancer (e.g., prostate, head and neck, and colon) and serum enzyme levels are elevated in melanoma patients relative to control subjects
brenda
additional information
-
acid ceramidase is abnormally expressed in various types of human cancer (e.g., prostate, head and neck, and colon) and serum enzyme levels are elevated in melanoma patients relative to control subjects
brenda
additional information
no significant fluctuation is detected for neutral or alkaline ceramidases in either gingival samples or cell cultures
brenda
additional information
-
no significant fluctuation is detected for neutral or alkaline ceramidases in either gingival samples or cell cultures
brenda
additional information
very low expression of maCER1 in organs and tissues other than skin
brenda
additional information
-
very low expression of maCER1 in organs and tissues other than skin
brenda
additional information
neutral ceramidase is ubiquitously expressed in various mammalian tissues
brenda
additional information
-
the NlnCDase has higher transcript level and activity in adults than in eggs and nymphs, and in the reproductive organs (ovaries and spermaries) than in other tissues (i.e. heads, thorax, legs, midguts)
brenda
additional information
neutral ceramidase is ubiquitously expressed in various mammalian tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ACER2 has 7 putative transmembrane domains, ACER2 membrane topology, overview. The N-terminal tail is necessary for both ACER2 activity and Golgi localization
brenda
inactive recombinant CDase expressed in Escherichia coli BL21 without its signal peptide
brenda
recombinant CDase expressed in Escherichia coli DH5alpha is most likely present in periplasm
-
brenda
additional information
the enzyme localizes predominantly to the endoplasmic reticulum, and partially to the Golgi complex
brenda
maCER1 is localized to the endoplasmic reticulum and contains a Golgi to ER retrieval signal sequence
brenda
Myc-tagged CDase expressed in HEK-239 cells, a 113 kDa endoplasmic reticulum-form matures into a 133 kDa CDase during processing in the Golgi apparatus
brenda
-
113 kDa developing form, enzyme which is truncated at the C-terminus by four amino acids is retained in the endoplasmic reticulum and rapidly degraded without transportation to the Golgi apparatus
brenda
a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells
brenda
the N- and C-terminal ends of Ypc1p are oriented towards the lumen and cytosol, respectively, cytosolic or lumenal loops
brenda
CDase is distributed with late endosomes/lysosomes in hepatocytes
brenda
the neutral ceramidase is exclusively secreted into the medium through a vesicular transport system when expressed in S2 cells
-
brenda
-
the majority of the recombinant AC overexpressed in CHO cells is secreted into the culture media
-
brenda
wild-type CDase from 3-L culture, recombinant CDase expressed in Pseudomonas putida KT2440 and Pichia pastoris GS115
-
brenda
the enzyme localizes predominantly to the endoplasmic reticulum, and partially to the Golgi complex
brenda
seven putative transmembrane domains allow for protein association with the Golgi apparatus
brenda
Myc-tagged CDase expressed in HEK-239 cells, a 113 kDa endoplasmic reticulum-form matures into a 133 kDa CDase during processing in the Golgi apparatus
brenda
a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells
brenda
recombinant CDase expressed in Escherichia coli DH5alpha and BL21
brenda
acid ceramidase is synthesized from a 53-55 kDa polypeptide precursor which is proteolytically processed into the 13 kDa alpha-subunit and 30 kDa beta-subunit
brenda
CDase is distributed with late endosomes/lysosomes in hepatocytes
brenda
the neutral ceramidase is membrane-bound, enzyme membrane topology, overview
brenda
the neutral ceramidase is membrane-bound, enzyme membrane topology, overview
brenda
ACER3 is an intramembrane enzyme with a seven transmembrane domain architecture
brenda
the neutral ceramidase is membrane-bound, enzyme membrane topology, overview
brenda
membrane-bound, 112 kDa-form, mainly localized at the apical membrane of proximal tubules, distal tubules and collecting ducts of kidney, microsome, sequence contains one possible transmembrane domain
brenda
membrane topology of rat neutral CDase, overview. A rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells
brenda
enzyme membrane topology, overview
brenda
kidney, microsomal fraction contains a large amount of membrane-bound 112 kDa neutral CDase
-
brenda
-
type II integral protein with its N-terminal end anchored to the plasma membrane and C-terminal end exposed to the extracellular space
brenda
transmembrane enzyme
brenda
-
wild-type CDase is located at plasma membranes
brenda
a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells. The CDase is transported to the plasma membrane through the classical ER/Golgi pathway
brenda
additional information
subcellular localization study, expression analysis, overview
-
brenda
additional information
-
ACER2 C- and N-termini are oriented in the lumen of the Golgi complex and cytosol, respectively
-
brenda
additional information
determination and analysis of subcellular localization of wild-type and recombinantly overexpressed immunostained nCDase
-
brenda
additional information
-
the enzyme has a putative signal peptide of 25 residues at the N-terminal
-
brenda
additional information
-
subcellular localization of wild-type and several C-terminal truncated CDases
-
brenda
additional information
the cell-surface expression of CDase is strongly inhibited by brefeldin A or treatment at 5°C, neutral and alkaline enzyme membrane topology, overview
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
the discovery of the contributions of dysregulation of the ACER family to aging, cancer, and inflammatory, metabolic, and neurodegenerative diseases reveals novel targets for disease interventions
drug target
-
acid ceramidase is a key enzyme in SARS-CoV-2 replication and, thus, as a promising antiviral target
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
-
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
-
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
-
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
-
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
-
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
-
ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview
evolution
distant homologues from nCDase are found in taxa all over evolution reinforcing a crucial role for ceramide
evolution
the Arabidopsis thaliana ceramidase AtNCER1 is a homologue of human neutral ceramidase
evolution
ADIPORs display distant homology with alkaline ceramidases, comparison of structures of ADIPOR1 and ADIPOR2
evolution
the fold of ACER3 is similar to adiponectin receptors (ADIPORs), structure comparisons, overview
evolution
distant homologues from nCDase are found in taxa all over evolution reinforcing a crucial role for ceramide
evolution
distant homologues from nCDase are found in taxa all over evolution reinforcing a crucial role for ceramide
evolution
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distant homologues from nCDase are found in taxa all over evolution reinforcing a crucial role for ceramide
evolution
distant homologues from nCDase are found in taxa all over evolution reinforcing a crucial role for ceramide
evolution
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the Arabidopsis thaliana ceramidase AtNCER1 is a homologue of human neutral ceramidase
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malfunction
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cells deficient in acid ceramidase exhibit defects in CCL5 transcriptional induction
malfunction
acid ceramidase ASAH1 knockdown leads to a decrease in cell proliferation with a concomitant reduction in the protein levels of BETA-catenin, proliferating cell nuclear antigen, and cyclin B2. ASAH1 silencing increases basal and cAMP-dependent cortisol and dehydroepiandrosterone secretion
malfunction
abnormal overexpression of acid ceramidase is related to tumor progression and protection from cell death, while deficiency of acid ceramidase results in Farber disease
malfunction
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inhibition of acid ceramidase activity stimulates apoptotic cell death. Point mutations in the acid ceramidase gene cause rare autosomal recessive Farber disease. Homozygous acid ceramidase-deficient mice are embryonic lethal
malfunction
knockdown of the zebrafish neutral CDase with an antisense morpholino oligonucleotide led to an increase in the number of zebrafish embryos with severe morphological abnormalities, such as defects in blood circulation, which were possibly caused by abnormal heart formation
malfunction
KO mice are impaired in the intestinal degradation of sphingolipids
malfunction
Farber disease, also known as Farber's lipogranulomatosis, is a clinically heterogeneous autosomal recessive disease caused by mutations in the ASAH1 gene, genotype-phenotype correlation, overview
malfunction
enzyme-deficient tod1 mutant pollen tubes have higher turgor than wild-type and show growth retardation both in pistils and in agarose medium. In addition, tod1 mutant guard cells are insensitive to abscisic acid-induced stomatal closure, whereas sphingosine-1-phosphate, a putative downstream component of abscisic acid signalling and product of alkaline ceramidases, promotes closure in both wild-type and tod1, TOD1 is sufficient to rescue pollen tube growth defect. Pollen tube growth defects of tod1-2 are suppressed by the gaut13 mutation, a single-nucleotide substitution in the galacturonosyltransferase13 gene. Phenotypes, overview
malfunction
the acer-1 T-DNA insertion mutant has pleiotropic phenotypes, including reduction of leaf size, dwarfing and an irregular wax layer, compared with wild-type plants, higher level of phytoceramides in acer-1 and amiR-ACER-1 plants than in the wild-type, phenotype, overview. Acer-1 mutants and AtACER RNAi lines show increased sensitivity to salt stress, and lines overexpressing AtACER show increased tolerance to salt stress. Reduction of AtACER also increases plant susceptibility to Pseudomonas syringae
malfunction
inhibition of acid ceramidase activity sensitizes tumor cells to the effects of antineoplastic agents and radiation. Carmofur inhibits acid ceramidase and increases ceramide levels in human SW403 and LNCaP cells
malfunction
inhibition of acid ceramidase activity sensitizes tumor cells to the effects of antineoplastic agents and radiation
malfunction
ASAH1-knockdown PC-3/Mc cells show impairment of ceramide catabolism with increased sphingosine levels, sphingolipid content, overview. ASAH1 knockdown by shRNA inhibits the growth of PC-3/Mc cells under low-density and low-serum conditions and abrogates their anchorage-independent colony-forming potential
malfunction
enzyme overexpression attenuates steroidogenic factor 1-stimulated CYP17A1 reporter gene activity. The enzyme not only abrogates Bt2cAMP-dependent CYP17A1 reporter gene activity but also inhibits SF-1-stimulated CYP17A1 reporter gene activity in both untreated and Bt2cAMP-stimulated cells
malfunction
overexpression of Ypc1p protein significantly increases the levels of free long-chain bases and long-chain base-phosphates and reduces the biosynthetic flow of long-chain bases towards mature sphingolipids, whereas deletion of gene YPC1 causes a significant increase in mature sphingolipids
malfunction
a tetracycline-inducible ASAH1 short hairpin RNA H295R human adrenocortical stable cell line shows increased transcription of multiple steroidogenic genes, including Cytochrome P450 monooxygenase (CYP)17A1, CYP11B1/2, CYP21A2, steroidogenic acute regulatory protein, hormone-sensitive lipase, 18-kDa translocator protein, and the melanocortin-2 receptor. Induced gene expression positively correlates with enhanced histone H3 acetylation at target promoters. Repression of ASAH1 expression also induces the expression of members of the nuclear receptor nuclear receptor subfamily 4 family while concomitantly suppressing the expression of dosage-sensitive sex reversal, adrenal hypoplasia critical region, on chromosome X, gene 1. ASAH1 knockdown alters the expression of genes involved in sphingolipid metabolism and changes the cellular amounts of distinct sphingolipid species. Enzyme silencing increases basal and cAMP-dependent cortisol and dehydroepiandrosterone secretion, establishing ASAH1 as a pivotal regulator of steroidogenic capacity in the human adrenal cortex
malfunction
leptomycin B prevents acid ceramidase and sphingosine 1-phosphate mediated loss of nuclear PTEN, suggesting an active exportin-mediated event
malfunction
overexpression of Ydc1p protein significantly increases the levels of free long-chain bases and long-chain base-phosphates and reduces the biosynthetic flow of long-chain bases towards mature sphingolipids
malfunction
NS-1 cell nCDase-containing exosomes block apoptosis induced by palmitate
malfunction
a significantly lower level of acid ceramidase expression was detected in gingival tissues from periodontal patients compared to those from healthy subjects
malfunction
acid ceramidase overexpression in HL-60 confers resistance to the acute myeloid leukemia chemotherapeutic drugs, cytarabine, mitoxantrone, and daunorubicin, and is linked to P-glycoprotein upregulation
malfunction
inhibition of nCDase decreases the development and progression of colorectal tumor growth. Cells overexpressing nCDase are protected from the cell death and Golgi fragmentation induced by C6-ceramide, and they show reduced levels of C6-ceramide and higher levels of sphingosine-1-phosphate (S1P) and sphingosine. nCDase-overexpressing cells show larger increases of sphingosine by 2.3fold compared to control
malfunction
the genetic loss or inhibition of acid ceramidase prevents formation of glycosphingoid bases
malfunction
genetic loss or inhibition of acid ceramidase prevents formation of glycosphingoid bases
malfunction
the enzyme is overexpressed in several types of cancer and Alzheimer's disease, and its genetic defect causes different incurable disorders
malfunction
ASAH1 reduction stimulates cell migration to the same extent as MITF inhibition. ASAH1 silencing in different cell types results in a significant increase in FAK phosphorylation. Conversely, forced expression of ASAH1 inhibits FAK phosphorylation. ASAH1-depleted cells are positive for the senescence-associated beta-galactosidase staining, and also MITF-silenced melanoma cells display features of senescence
malfunction
upregulation of ASAH1 confers resistance to radiation by altering the sphingolipid metabolism pathway. ASAH1 plays a similar role in recurrent or irradiated glioblastoma multiforme. ASAH1 inhibition by camofur results in cell death and elevated levels of ceramides in U87, SJGBM2, U87-10gy and SJGBM2-10gy cells
malfunction
a Dacer-deficient Drosophila melanogaster mutant has higher catalase (CAT) activity and CAT transcription level, leading to higher resistance to oxidative stress induced by paraquat. Altered antioxidative activity in Dacer mutant might be responsible for increased oxidative stress resistance. Quantitative proteomic analysis of wild-type and mutant cells. Three oxidoreductases, including two cytochrome P450 (CG3050, CG9438) and an oxoglutarate/iron-dependent dioxygenase (CG17807), are most significantly upregulated in the Dacer overexpressing mutant
malfunction
loss of function in E33G-ACER3 mutant found in leukodystrophic patients, ACER3 deficiency leads to progressive leukodystrophy in early childhood, mutation impaires the ACER3 ceramidases activity in patients' cells. This loss of function results in higher level of several ceramide species in the blood, in particular for the ACER3 preferred substrates, C18:1 and C20:1 ceramides. It is proposed that these aberrant levels of ceramides in the brain result in an incorrect central myelination leading to the clinical phenotype associated with the ACER3 mutant, i.e., neurological regression at 6-13 months of age, truncal hypotonia, appendicular spasticity, dystonia, optic disc pallor, peripheral neuropathy, and neurogenic bladder
malfunction
abnormal function of the enzyme leads to Farber disease, spinal muscular atrophy with progressive myoclonic epilepsy, and is associated with Alzheimer's, diabetes, and cancer. Structural mapping of disease mutations reveals that most destabilize the protein fold
malfunction
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knocking down NlnCDase by RNA interference increases female survival under starvation and temperature stresses
malfunction
nCDase downregulation induces a decrease of cell growth and neuronal differentiation. Gemcitabine treated cells show an increase of the levels of specific ceramides, attributed to a reduction of nCDase expression. The increased ceramide is also implicated in suppression of cell growth. UVB irradiation decreases nCDase activity in keratinocytes, and ceramidase inhibition or siRNA-mediated suppression sensitizes keratinocytes to low-dose-UVB-induced apoptosis. ATRA downregulated nCDase expression at the message level results in less protein and activity in SH-SY5Y neuroblastoma cells. Inhibition of nCDase in colorectal cancer (CRC) cells induces a decrease of phosphorylation of GSK3beta, which activates the kinase. In turn, activated GSK3beta phosphorylated beta-catenin, resulting in a significant decrease in its levels. Inhibition of nCDase results in dephosphorylation and inactivation of Akt, which is responsible for the loss of phosphorylation of GSK3beta and the loss of beta-catenin. Cells overexpressing nCDase are protected from cell death induced by the short chain C6-ceramide
malfunction
nCDase deficient mice are viable with no obvious deficiency under normal breeding conditions. Further investigation reveals that nCDase deficient mice are not able to degrade dietary sphingolipids. Gemcitabine treated cells show an increase of the levels of specific ceramides, attributed to a reduction of nCDase expression. The increased ceramide is also implicated in suppression of cell growth. nCDase deficient mice treated with DSS show a paradoxical elevation of sphingosine and an increase of sphingosine 1-phosphate. Knockout mice are partly protected from brain injury. MEFs from nCDase deficient mice present an increase of autophagic flux and more specifically mitophagy when subjected to the 2DG/AA model of necroptosis. They showed as well that inhibition of autophagy reverses this phenotype. Inhibition of nCDase may enhance cell survival by increasing the clearance of damaged mitochondria via mitophagy
malfunction
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the knockdown of this enzyme enhances survival of the female planthopper at high (32°C) or low (22°C) temperature
malfunction
ACER3 dysfunction during development is associated with severe neuropathy
malfunction
mutations lead to Farber Disease and spinal muscular atrophy with progressive myoclonic epilepsy. Overexpression in cancer, Gaucher Disease, ulcerative colitis, glaucoma, keloids and intratauterine growth restriction
malfunction
associated diseases: Farber's disease, Alzheimer's disease, cancer, diabetes, and spinal muscular atrophy
malfunction
altered function of mutated ASAH1 is recognized in spinal muscular atrophy with progressive myoclonic epilepsy and Farber's lipogranulomatosis. Alteration in acid ceramidase activity or a change in the expression level of ASAH1 in Alzheimer's disease, cancer, and type 2 diabetes
malfunction
Acer2 deficiency results in embryonic lethality due to the atrophy of the fetal blood vessel network in the placenta. Acer2 deficiency in both the mother and fetus decreases the placental levels of sphingolipids, including sphingoid bases (sphingosine and dihydrosphingosine) and sphingoid base-1-phosphates (sphingosine-1-phophate and dihydrosphingosine-1-phosphate) and results in the in utero death of about 50% of embryos at E12.5
malfunction
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knocking down NCER through RNA interference increases the levels of ceramides in BPH females and ovaries, which results in a delay in oocyte maturation, a reduction in oviposition and egg hatching rate, as well as the production of vulnerable offspring
malfunction
associated diseases: Alzheimer's disease and various metabolic diseases
malfunction
knocking out Acer2 decreases the levels of sphingosine, but not dihydrosphingosine, sphingosine-1-phosphate, nor dihydrosphingosine-1-phosphated, in lymph nodes and spleen. Knocking out MmACER2 does not affect the levels of ceramides, dihydroceramides, sphingomyelins, or monohexosylceramides in whole blood. Knocking out MmACER2 slightly increases the levels of ceramides, but not dihydroceramides
malfunction
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enzyme-deficient tod1 mutant pollen tubes have higher turgor than wild-type and show growth retardation both in pistils and in agarose medium. In addition, tod1 mutant guard cells are insensitive to abscisic acid-induced stomatal closure, whereas sphingosine-1-phosphate, a putative downstream component of abscisic acid signalling and product of alkaline ceramidases, promotes closure in both wild-type and tod1, TOD1 is sufficient to rescue pollen tube growth defect. Pollen tube growth defects of tod1-2 are suppressed by the gaut13 mutation, a single-nucleotide substitution in the galacturonosyltransferase13 gene. Phenotypes, overview
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metabolism
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inverse regulation of ACER2 and dihydrosphingosine desaturase is an important mechanism by which N-(4-hydroxyphenyl)retinamide exerts its cytotoxic and apoptotic effects in tumor cells
metabolism
Dacer plays a role in fly development and longevity by controlling the metabolism of ceramides
metabolism
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the enzyme is one of the key players, which determine the dynamic balance between the intracellular levels of ceramide and its breakdown products, in ceramide metabolism and sphingolipid biosynthesis, metabolism and interconversions, overview
metabolism
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ceramide metabolism, sphingolipid signaling, and aberrant ceramide signaling and cancer development, overview. Pathways of sphingolipid metabolism, overview
metabolism
key biological functions of ceramidases in biotic and abiotic stresses in plants
metabolism
acid ceramidase catalyzes the hydrolysis of ceramide into sphingosine, in turn a substrate of sphingosine kinases that catalyze its conversion into the mitogenic sphingosine 1-phosphate
metabolism
ACTH/cAMP signaling promotes nuclear sphingolipid metabolism in an enzyme-dependent manner. ACTH/cAMP signaling promotes the recruitment of the enzyme to multiple steroidogenic gene promoters
metabolism
acid ceramidase overexpression increased NF-kappaB activation whereas NF-kappaB inhibitors reduce P-glycoprotein levels, indicating that the NF-kappaB pathway contributes to acid ceramidase-mediated modulation of P-glycoprotein expression
metabolism
adiponectin receptors (ADIPORs) are integral membrane proteins that control glucose and lipid metabolism by mediating, at least in part, a cellular ceramidase activity that catalyses the hydrolysis of ceramide to produce sphingosine and a free fatty acid. ADIPOR2 possesses intrinsic basal ceramidase activity that is enhanced by adiponectin
metabolism
the enzyme is a target of the microphthalmia-associated transcription factor (MITF). ASAH1 controls the switch between the proliferative and invasive phenotype in melanoma cells, and MITF also is a critical regulator of switch between proliferative and invasive phenotypes promoted by melanoma plasticity. MITF is also involved in the regulation of sphingolipid metabolism
metabolism
sphingolipid metabolism and interconnected bioactive metabolites derived from ceramide, overview. Ceramide, the essential synthetic building block for sphingomyelin, glycosphingolipids, and ceramide-1-phosphate is hydrolyzed by ceramidase to fatty acid and sphingosine, which then is phosphorylated to sphingosine-1-phosphate (S1P) by sphingosine kinases
metabolism
deletion of neutral ceramidase in multiple breast cancer models in female mice accelerates tumor growth
metabolism
ceramide plays a crucial role in metabolic and disease states, and therefore, the degrading enzyme ceramidase is the critical regulator that maintains ceramide homeostasis inside cells. A disturbance in the balance between ceramide and sphingosine-1 phosphate interferes with healthy metabolism. Consumption of a high-fat diet leads to the development of obesity-related diseases, where ceramide is involved. An accumulation of ceramide is observed in nonalcoholic fatty liver disease, Type 2 diabetes mellitus, cancer, inflammatory bowel disease, and Alzheimer's disease
metabolism
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Dacer plays a role in fly development and longevity by controlling the metabolism of ceramides
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physiological function
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synthesis of sphingosine is essential for oxidative stress-induced apoptosis of photoreceptors, pathway regulation, overview
physiological function
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ACER3 specifically controls the hydrolysis of ceramides carrying unsaturated long acyl chains, unsaturated long-chain ceramides
physiological function
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ACER2 plays an important role in cellular responses by regulating the hydrolysis of ceramides in cells, activity regulation, overview
physiological function
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ACER2 catalyzes the hydrolysis of dihydroceramides to generate dihydrosphingosine. ACER2 upregulation plays a key role in mediating the N-(4-hydroxyphenyl)retinamide-induced generation of dihydrosphingosine as well as the cytotoxicity of 4-HPR in tumor cells, while ACER3 has a limited role, overview
physiological function
Dacer plays a role in fly development and longevity by controlling the metabolism of ceramides. Dacer inactivation delays Drosophila pre-adult development, while Dacer inactivation increases Drosophila lifespan
physiological function
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the enzyme is involved in ceramide metabolism and is a critical regulator of cancer cell growth and/or survival, acid ceramidase upregulation in prostate cancer plays a role in tumor development. A dysfunctional ceramide pathway is responsible for tumor progression and resistance to chemotherapy and radiation
physiological function
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alkaline ceramidases have a compensatory role in controlling sphingosine and sphingosine 1-phosphate generation in erythroid cells
physiological function
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alkaline ceramidases have a compensatory role in controlling sphingosine and sphingosine 1-phosphate generation in erythroid cells
physiological function
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acid ceramidase improves the quality of oocytes and embryos and the outcome of in vitro fertilization, the level of the enzyme is positively correlated with the quality of human embryos formed in vitro. Addition of recombinant acid ceramidase to human oocyte culture medium maintains the healthy cell morphology in vitro
physiological function
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co-expression of acid sphingomyelinase and acid ceramidase is sufficient to strongly induce CCL5 transcription
physiological function
acid ceramidase ASAH1 is a global regulator of steroidogenic capacity and adrenocortical gene expression
physiological function
intestinal secreted neutral ceramidase is involved in digestion of dietary sphingolipids
physiological function
acid ceramidase activity enhances acid sphingomyelinase secretion
physiological function
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the enzyme determines cell fate, namely, death or survival, by controlling the balance between the intracellular levels of ceramide and sphingosine 1-phosphate. Acid ceramidase plays an important role in tumorigenesis and in prolonging the survival of cells
physiological function
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acid ceramidase, through generation of sphingosine-1-phosphate, promotes an invasive phenotype in prostate cancer and promotes Ets1 nuclear expression and binding to the promoter region of matrix-degrading protease cathepsin B. Acid ceramidase overexpression promotes pericellular localization of cathepsin B and its translocation to the outer leaflet of the cell membrane
physiological function
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neutral ceramidase is a key participant of ceramide formation in liver mitochondria. The reverse activity of neutral ceramidase contributes to sphingolipid homeostasis in this organelle in vivo. The enzyme contributes to the overall ceramide profile of liver mitochondria at basal conditions in vivo
physiological function
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neutral ceramidase is a key participant of ceramide formation in liver mitochondria. The reverse activity of neutral ceramidase contributes to sphingolipid homeostasis in this organelle in vivo. The enzyme contributes to the overall ceramide profile of liver mitochondria at basal conditions in vivo
physiological function
neutral CDase may be involved in a pathway for the digestion of dietary sphingolipids in mice
physiological function
neutral CDase is expressed in the intestines of humans and plays a major role in ceramide metabolism in the gut
physiological function
ceramide hydrolysis by acid ceramidase stops the biological activity of ceramides and influences survival and function of normal and neoplastic cells
physiological function
LsnCer is a bona fide neutral ceramidase that may have a role in adaption of Laodelphax striatellus to environmental stresses
physiological function
the influence of sphingolipids, such as ceramide and its metabolite sphingosine 1-phosphate, on signal transduction pathways under cell stress is important to survival adaptation responses. A protective feedback mechanism mitigates the apoptotic effect of ionizing radiation-induced ceramide generation. c-Jun-regulated acid veramidase mediates PCa cell radioresistance and relapse in vitro and in vivo
physiological function
the enzyme catalyzes the lysosomal degradation of ceramide to sphingosine and fatty acid
physiological function
alkaline ceramidase TOD1 is preferentially expressed in pollen tubes and in silique guard cells, where it is required for turgor pressure regulation, it is a key turgor pressure regulator in plant cells, molecular mechanism. Turgor pressure plays pivotal roles in the growth and movement of walled cells
physiological function
ceramide hydrolysis by acid ceramidase stops the biological activity of ceramides and influences survival and function of normal and neoplastic cells
physiological function
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the bacterial enzyme alone does not affect TNF-alpha gene expression in three-dimensionally cultured human primary keratinocytes. In the presence of the detergent Triton X-100, which damages stratum corneum structure, the active enzyme, but not heat-inactivated enzyme or inactive mutant enzyme, induces the production of TNF-alpha, endothelin-1, and interleukin-8, indicating that this production is dependent on ceramidase activity, it is also inhibited by a sphingosine kinase inhibitor and by an sphingosine 1-phosphate receptor antagonist VPC 23019. Among various ceramide metabolites, sphingosine and sphingosine 1-phosphate enhance the gene expression of TNF-alpha, endothelin-1, and interleukin-8, overview
physiological function
the enzyme is involved in salt tolerance and in disease resistance
physiological function
acid ceramidase is a cysteine amidase that hydrolyses the proapoptotic lipid ceramide, and is abnormally high in several human tumors, which is suggestive of a role in chemoresistance. The enzyme is involved in the regulation of ceramide levels in cells and modulates the ability of this lipid messenger to influence the survival, growth and death of tumor cells
physiological function
acid ceramidase is a cysteine amidase that hydrolyses the proapoptotic lipid ceramide, and is abnormally high in several human tumors, which is suggestive of a role in chemoresistance. The enzyme is involved in the regulation of ceramide levels in cells and modulates the ability of this lipid messenger to influence the survival, growth and death of tumor cells
physiological function
nuclear receptor steroidogenic factor 1 is essential for steroidogenic gene transcription. Acid ceramidase represses nuclear receptor steroidogenic factor 1-dependent gene transcription in H295R human adrenocortical cells by binding to the receptor, molecular mechanism, overview. The enzyme is a coregulatory protein that represses steroidogenic factor 1 function by directly binding to the receptor on steroidogenic factor 1 target gene promoters and plays a key role for nuclear lipid metabolism in regulating gene transcription
physiological function
acid ceramidase directly regulates the intracellular balance of ceramide, sphingosine, and sphingosine-1-phosphate by catalyzing the hydrolysis of ceramide into sphingosine. The enzyme plays a role in glucocorticoid production and regulating steroidogenic capacity
physiological function
tumor promotion of acid ceramidase in prostate cancer. Impact of acid ceramidase on the nuclear-cytoplasmic trafficking of tumor suppressor PTEN, immunohistochemical analysis, overview. Acid ceramidase, through sphingosine 1-phosphate, promotes nuclear export of PTEN as a means of promoting tumor formation, cell proliferation, and resistance to therapy. Acid ceramidase promotes a reduction in nuclear PTEN that is dependent upon sphingosine 1-phosphate-mediated activation of Akt
physiological function
nCDase regulates the levels of bioactive sphingolipid metabolites in the intestinal tract. Exosomes expressing nCDase can protect INS-1 cells or rat primary Langerhans islets against apoptosis induced by high dose cytokines
physiological function
endogenous acid ceramidase protects epithelial cells from Porphyromonas gingivalis (ATCC 33277)-induced inflammation in vitro. Anti-inflammatory and anti-apoptotic effects of acid ceramidase in host cells exposed to periodontal bacteria, and the attenuation of the expression of host-protective acid ceramidase in periodontal lesions
physiological function
signalling effects induced by acid ceramidase in human epithelial or leukemic cell lines
physiological function
acid ceramidase promotes drug resistance in acute myeloid leukemia through NF-kappaB-dependent P-glycoprotein upregulation. Elevated acid ceramidase levels in acute myeloid leukemia contribute to blast survival. Important role for the enzyme in drug resistance as well as cell survival
physiological function
ceramidases hydrolyze ceramides into sphingosine and fatty acids, with sphingosine being further metabolized into sphingosine-1-phosphate (S1P). Ceramidases control the levels of these bioactive sphingolipids in cells and tissues. Neutral ceramidase (nCDase) activity is involved in Wnt/beta-catenin signaling. nCDase is involved in the metabolism of C6-ceramide to sphingosine and subsequently to S1P and possibly ceramide. nCDase is found to be located in both the plasma membrane and in the Golgi apparatus, but it has minimal effects on basal levels of ceramide, sphingosine, or S1P
physiological function
acid ceramidase actively forms glycosphingoid bases in Gaucher and Fabry disease. Molecular basis of the formation of glucosylsphingosine and globotriaosylsphingosine during deficiency of glucocerebrosidase (Gaucher disease) and alpha-galactosidase A (Fabry disease), active role of acid ceramidase in both processes through deacylation of lysosomal glycosphingolipids, overview. Analysis of the potential pathophysiological relevance of elevated glycosphingoid bases generated through this alternative metabolism in patients suffering from lysosomal glycosidase defects. Possibility of broadened substrate specificity of acid ceramidase during lysosomal lipid accumulation
physiological function
acid ceramidase actively forms glycosphingoid bases in Gaucher and Fabry disease. Molecular basis of the formation of glucosylsphingosine and globotriaosylsphingosine during deficiency of glucocerebrosidase (Gaucher disease) and alpha-galactosidase A (Fabry disease), active role of acid ceramidase in both processes through deacylation of lysosomal glycosphingolipids, overview. Possibility of broadened substrate specificity of acid ceramidase during lysosomal lipid accumulation
physiological function
acid ceramidase hydrolyzes ceramides into sphingoid bases and fatty acids
physiological function
acid ceramidase ASAH1 is a key enzyme of sphingolipid metabolism. ASAH1 controls melanoma cell proliferation and motile features. ASAH1 acts as a rheostat of the phenotypic switch in melanoma cells. Low ASAH1 expression is associated with an invasive behavior mediated by activation of the integrin alphavbeta5-FAK signaling cascade. ASAH1 controls the switch between the proliferative and invasive phenotype in melanoma cells
physiological function
acid ceramidase (ASAH1), a lysosomal cysteine amidase, helps metabolize ceramides into sphingosine and free fatty acids. Ceramides promote senescence and apoptosis, while sphingososine-1-phospate (Sph-1P), the immediate metabolite of sphingosine, promotes cell survival, proliferation, inflammation, and angiogenesis. As such, overexpression of ASAH1 confers resistance to apoptosis
physiological function
neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate. Enzyme nCDase regulates the balance of ceramide and sphingosine-1-phosphate
physiological function
neutral ceramidases are key enzymes of sphingolipid metabolism that hydrolyze the fatty acyl/sphingosine amide linkage of ceramide at neutral pH
physiological function
enzyme Dacer regulates expression of oxidative stress proteins
physiological function
alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. They are implicated in human pathophysiology, including progressive leukodystrophy, colon cancer as well as acute myeloid leukemia. ACER3 has a catalytic Zn2+ binding site in its core and a Ca2+ binding site physically and functionally connected to the Zn2+ providing a structural explanation for the known regulatory role of Ca2+ on ACER3 enzymatic activity
physiological function
acid ceramidase (aCDase, ASAH1) hydrolyzes lysosomal membrane ceramide into sphingosine, the backbone of all sphingolipids, to regulate many cellular processes
physiological function
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neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens. The NlnCDase level might be elevated in adult reproductive organs to mediate developmental process. NlnCDase might be involved in the stress response
physiological function
nCDase regulates the levels of bioactive sphingolipid metabolites in the intestinal tract. Role of nCDase in traumatic brain injury. The enzyme is involved in intracellular signaling
physiological function
nCDase regulates the levels of bioactive sphingolipid metabolites in the intestinal tract. CDase may protect against inflammation using a dextran sodium sulfate (DSS) mouse model. Role of nCDase in traumatic brain injury
physiological function
acid ceramidase is critical for transient receptor potential mucolipin 1 (TRPML1) channel-mediated Ca2+ release, which controls lysosome-multivesicular body interaction and exosome release in podocytes
physiological function
role in senescence and apoptosis
physiological function
ASAH1 maintains intralysosomal ceramide homeostasis. Saposin D is a positive modulator of ASAH1
physiological function
the conversion of ceramide to sphingosine is mediated by acid ceramidase (ASAH1) thus maintaining a rheostat between a tumor suppressor and a tumor promoter
physiological function
alkaline ceramidase 2 (ACER2) plays a key role in sustaining the integrity of the placental vasculature by regulating the homeostasis of sphingolipids in mice
physiological function
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NCER is necessary for the development of the female productive system by controlling ceramide homeostasis in the female ovary
physiological function
neutral ceramidase regulates breast cancer progression by metabolic programming of TREM2-associated macrophages
physiological function
enzyme sphingolipid ceramide N-deacylase (SCDase) cleaves the fatty acid chain of the ceramide moiety to produce l-GSLs bearing a free amine
physiological function
ACER2 regulates the cellular levels of sphingolipids dependent on its expression level. ACER2 may act as a tumor promoter in certain cancers, such as hepatocellular carcinoma and breast cancer
physiological function
regulates the conversion of ceramide into sphingosine and sphingosine-1-phosphate. Important for the metabolism of dietary sphingolipids
physiological function
role in digesting dietary sphingolipid to regulate the sphingolipid balance in the human gut
physiological function
ACER1 is predominantly expressed by skin cells and is involved in their differentiation, as well as in the viability of hair follicle stem cells
physiological function
regulates cell proliferation and apoptosis. Key regulator of keratinocyte differentiation, fundamental role in skin barrier formation
physiological function
induces programmed cell death through an sphingosine-dependent pathway
physiological function
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alkaline ceramidase TOD1 is preferentially expressed in pollen tubes and in silique guard cells, where it is required for turgor pressure regulation, it is a key turgor pressure regulator in plant cells, molecular mechanism. Turgor pressure plays pivotal roles in the growth and movement of walled cells
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physiological function
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Dacer plays a role in fly development and longevity by controlling the metabolism of ceramides. Dacer inactivation delays Drosophila pre-adult development, while Dacer inactivation increases Drosophila lifespan
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physiological function
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enzyme sphingolipid ceramide N-deacylase (SCDase) cleaves the fatty acid chain of the ceramide moiety to produce l-GSLs bearing a free amine
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additional information
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in cells, ACER3 overexpression decreases C18:1- and C20:1-ceramides and dihydroceramides, whereas ACER3 knockdown by RNA interference in HeLa cells has the opposite effect. ACER3 knockdown inhibits cell proliferation and up-regulates the cyclin-dependent kinase inhibitor p21CIP1/WAF1. Blocking p21CIP1/WAF1 up-regulation attenuates the inhibitory effect of ACER3 knockdown on cell proliferation, suggesting that ACER3 knockdown inhibits cell proliferation because of p21CIP1/WAF1 up-regulation. ACER3 knockdown inhibits cell apoptosis in response to serum deprivation. ACER3 knockdown up-regulates the expression of ACER2, and the ACER2 up-regulation decreases non-ULC ceramide species while increasing both sphingosine and its phosphate
additional information
-
ceramidase inhibition abolishes contractile effects in cardiomyocytes
additional information
-
human acid ceramidase deficiency is associated with Farber disease. It plays a role in androgen depletion therapy and in resistance to chemotherapy and to radiation therapy, overview
additional information
-
alkaline ceramidase overexpression along with sphingosine 1-phosphate lyase knockdown results in sphingosine 1-phosphate accumulation in cells
additional information
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
-
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence and a mucin box
additional information
enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence and a mucin box
additional information
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence and a mucin box
additional information
enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence and a mucin box
additional information
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
two of the five natural cysteines, Cys27 and Cys219, are essential for enzymatic activity and form a disulfide bridge. Enzyme Ypc1p possesses the Pfam PF05875 ceramidase motif containing seven predicted transmembranes
additional information
two of the five natural cysteines, Cys27 and Cys219, are essential for enzymatic activity and form a disulfide bridge. Enzyme Ypc1p possesses the Pfam PF05875 ceramidase motif containing seven predicted transmembranes
additional information
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two of the five natural cysteines, Cys27 and Cys219, are essential for enzymatic activity and form a disulfide bridge. Enzyme Ypc1p possesses the Pfam PF05875 ceramidase motif containing seven predicted transmembranes
additional information
-
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
-
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
-
enzyme structure-function relationship, overview. The enzyme contains no signal/anchor sequence and no mucin box
additional information
-
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
-
enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box
additional information
treatment of cultured epithelial Chang cells or leukemic T-lymphocytes (Jurkat cells) with purified acid ceramidase results in a dose dependent activation of AKT, p38-kinase and p70S6-kinase, while tyrosine phosphorylation of intracellular proteins remains largely unchanged, determination of intracellular signalling events, proliferation and cell survival, overview. Acid ceramidase treatment does not change expression of tight junction proteins such as ZO-1, ZO-2 and occludin. Cellular viability and proliferation are not affected by acid ceramidase treatment
additional information
-
treatment of cultured epithelial Chang cells or leukemic T-lymphocytes (Jurkat cells) with purified acid ceramidase results in a dose dependent activation of AKT, p38-kinase and p70S6-kinase, while tyrosine phosphorylation of intracellular proteins remains largely unchanged, determination of intracellular signalling events, proliferation and cell survival, overview. Acid ceramidase treatment does not change expression of tight junction proteins such as ZO-1, ZO-2 and occludin. Cellular viability and proliferation are not affected by acid ceramidase treatment
additional information
development of a method for the specific visualization of catalytically active acid ceramidase in intracellular compartments. Development of activity-based probes for the detection of acid ceramidase, fluorescent SABRAC enzyme inhibitor analogues are used for enzyme detection. An azide-substituted analogue allows the unprecedented labeling of active acid ceramidase in living cells. Cys143 is the catalytic residue in the active site
additional information
possible mechanism for the hydrolytic activity of ADIPOR2 using computational approaches. In molecular dynamics simulations, the side chains of residues coordinating the zinc rearrange quickly to promote the nucleophilic attack of a zinc-bound hydroxide ion onto the ceramide amide carbonyl. Enzyme structure analysis, overbiew. An uninterrupted cavity goes through the entire receptor from the domain exposed to the upper lipid bilayer to the domain exposed to the cytoplasm. A tunnel enters the top half of the receptor between TM5 and TM6 and links the upper lipid bilayer to the FFA binding pocket. Some electron density is present in this domain indicating that this large opening might play a key role in modulating the entrance or exit of molecules to or from the receptor. On the intracellular side of ADIPOR2, the cavity splits into two tunnels immediately below the zinc binding domain, one of which is largely exposed to the cytoplasm
additional information
the human enzyme contains a 20 A deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases. Flexible ligand docking and prediction of a binding mode for ceramide. The nCDase uses a distinct catalytic strategy for Zn2+-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl headgroup of ceramide. Docking study with ligand C16-ceramide
additional information
-
the human enzyme contains a 20 A deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases. Flexible ligand docking and prediction of a binding mode for ceramide. The nCDase uses a distinct catalytic strategy for Zn2+-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl headgroup of ceramide. Docking study with ligand C16-ceramide
additional information
analysis of the catalytic mechanism of eukaryotic neutral ceramidase, structurally based explanation for ceramide specificity, comparison to the bacterial neutral ceramidase, overview. A general acid-base catalysis mechanism is proposed for amide bond hydrolysis by nCDase. In this mechanism, the Zn2+ ion functions to activate a water molecule for nucleophilic attack of the amide carbon. His196 serves as a general base for proton extraction from water and subsequently, a general acid to shuttle this proton to the nitrogen of ceramide during amide bond cleavage. The catalytic domain of the human enzyme contains an extra 30-residue subdomain inserted within the loop between beta14 and alpha7. In human nCDase, the 30-residue subdomain insert replacing the 6-residue span of bacterial CDase displays specific mobility. Stabilization of the subdomain conformation is aided by two internal disulfide bridges, formed by four cysteines that are conserved in eukaryotes
additional information
-
analysis of the catalytic mechanism of eukaryotic neutral ceramidase, structurally based explanation for ceramide specificity, comparison to the bacterial neutral ceramidase, overview. A general acid-base catalysis mechanism is proposed for amide bond hydrolysis by nCDase. In this mechanism, the Zn2+ ion functions to activate a water molecule for nucleophilic attack of the amide carbon. His196 serves as a general base for proton extraction from water and subsequently, a general acid to shuttle this proton to the nitrogen of ceramide during amide bond cleavage. The catalytic domain of the human enzyme contains an extra 30-residue subdomain inserted within the loop between beta14 and alpha7. In human nCDase, the 30-residue subdomain insert replacing the 6-residue span of bacterial CDase displays specific mobility. Stabilization of the subdomain conformation is aided by two internal disulfide bridges, formed by four cysteines that are conserved in eukaryotes
additional information
substrate docking and hydrolysis mechanism, molecular dynamics simulation and docking study, overview. Computational docking of N-oleoyl-D-sphingosine
additional information
-
substrate docking and hydrolysis mechanism, molecular dynamics simulation and docking study, overview. Computational docking of N-oleoyl-D-sphingosine
additional information
a hydrophobic surface surrounding the substrate binding channel appears to be a site of membrane attachment where the enzyme accepts substrates facilitated by the accessory protein, saposin-D. The shape of the substrate binding channel appears to be specific for ceramide, as other membrane-resident lipids with bulky head groups, such as sphingomyelin, phospholipids, and cerebrosides, result in steric clashes binding in a manner similar to the modelled ceramide. Catalytic mechanism of substrate hydrolysis, molecular docking and simulation, overview. Uncovering the substrate-binding site upon autocleavage, the concomitant conformational change to the alpha-beta junction causes strand-beta3 containing Cys 143 to shift. This moves Cys143 away from Arg159 breaking their putative hydrogen bond, suggesting that for substrate cleavage Arg159 may not act as the general base. Instead, the general base in the activated state is mostly likely to be the newly formed N-terminus of the beta-subunit. Active site residue N320 stabilizes the N-terminus of Cys143 through hydrogen bonding with its side chain oxygen, whereas its side chain nitrogen provides the oxyanion hole for substrate hydrolysis and stabilizes the position of Glu225, also important for oxyanion hole formation. R333 hydrogen bonds to N320 and based on the substrate modeling above, is predicted to be important for engaging ceramide
additional information
possible mechanism for the catabolism of ceramide by the enzyme. The active site of human neutral ceramidase is a narrow, 20 A deep, hydrophobic pocket with a Zn2+ ion at the base. Hydrophobic residues line the pocket from outside to inside with one side of the active site cavity formed by the ny2-alpha8 helices. His196, Arg257, Tyr579, and Tyr591 were identified as playing critical roles in catalysis and stabilizing the transition state of ceramide hydrolysis, proposed model of ceramide hydrolysis by nCDase in membranes, overview. The membrane-tethered human nCDase involves extracting ceramide from membranes (left) or bile-acid micelles (right) into the deep hydrophobic pocket. The flexible tether allows human nCDase to hydrolyze ceramide in two different physiological forms
additional information
measurement of neutral ceramidase activity both in vitro and in vivo. Three high- and moderate-throughput biochemical assays for human neutral ceramidase are described and characterized, the RBM ceramide, fluorescence resonance energy transfer (FRET) and NBD-ceramide based assays. While the RBM assay is best suited for HTS, the fluorescence interference requires secondary follow-up using the red-shifted FRET assay and/or HPLC based NBDceramide assays. Comparison of assay conditions
additional information
-
the enzyme is a potential target for developing novel pesticides to control Nilaparvata lugens, a highly destructive rice pest
additional information
acid ceramidase is abnormally expressed in various cancers
additional information
glycolipids from mammalian cells contain glycosphingolipids (GSLs) as their major glycolipid component, and these structures vary in the identity of the glycan headgroup as well as the structure of the fatty acid and sphingosine (Sph) tails. Development of a method for analysis of intact GSLs in mammalian cell culture and tissue: digestion of a GSL sample with sphingolipid ceramide N-deacylase (SCDase), followed by labelling with an amine-reactive fluorophore. The sample is then analyzed by HPLC-FLD-MS and quantitated by addition of an external standard. This method is compared to analysis of GSL glycans after cleavage by an endoglycoceramidase (EGCase, EC 3.2.1.123) enzyme and labeling with a fluorophore (2-anthranilic acid, 2AA). The two methods are complementary, with EGCase providing improved signal (due to fewer species) and SCDase providing analysis of lyso-GSL (l-GSL, GSL that retain linkage of the glycan headgroup with the Sph base). Importantly the SCDase method provides Sph composition of GSL species
additional information
-
glycolipids from mammalian cells contain glycosphingolipids (GSLs) as their major glycolipid component, and these structures vary in the identity of the glycan headgroup as well as the structure of the fatty acid and sphingosine (Sph) tails. Development of a method for analysis of intact GSLs in mammalian cell culture and tissue: digestion of a GSL sample with sphingolipid ceramide N-deacylase (SCDase), followed by labelling with an amine-reactive fluorophore. The sample is then analyzed by HPLC-FLD-MS and quantitated by addition of an external standard. This method is compared to analysis of GSL glycans after cleavage by an endoglycoceramidase (EGCase, EC 3.2.1.123) enzyme and labeling with a fluorophore (2-anthranilic acid, 2AA). The two methods are complementary, with EGCase providing improved signal (due to fewer species) and SCDase providing analysis of lyso-GSL (l-GSL, GSL that retain linkage of the glycan headgroup with the Sph base). Importantly the SCDase method provides Sph composition of GSL species
-
Show AA Sequence and Transmembrane Helices (9926 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
x * 100000, about, glycosylated enzyme, SDS-PAGE, x * 80000, about, deglycosylated enzyme, SDS-PAGE
110000
112000
x * 112000, membrane-bound CDase from kidney, SDS-PAGE, x * 83483, CDase from kidney, sequence calculation, x * 113000, endoplasmic reticulum-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE, x * 133000, Golgi-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE
113000
x * 112000, membrane-bound CDase from kidney, SDS-PAGE, x * 83483, CDase from kidney, sequence calculation, x * 113000, endoplasmic reticulum-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE, x * 133000, Golgi-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE
116000
118000
13000
133000
x * 112000, membrane-bound CDase from kidney, SDS-PAGE, x * 83483, CDase from kidney, sequence calculation, x * 113000, endoplasmic reticulum-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE, x * 133000, Golgi-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE
135000
-
determined by SDS-PAGE and Western blot analysis, the multiple band pattern between about 95 and 135 kDa may be due to the complexity of modifications, such as O-glycosylation and N-glycosylation
142000
150000
28000
apparent molecular weight, deglycosylated beta subunit
31000
31300
theoretical value, Western blot analysis shows a molecular mass close to the predicted one
31600
theoretical value, Western blot analysis shows a molecular mass close to the predicted one
40000
50000
53000
54000
synthesized as a polypeptide of 395 amino acids, 53 - 55 kDa
70000
80000
-
x * 100000, about, glycosylated enzyme, SDS-PAGE, x * 80000, about, deglycosylated enzyme, SDS-PAGE
82500
-
x * 110000, glycosylated recombinant enzyme, SDS-PAGE, x * 82500, deglycosylated recombinant enzyme, SDS-PAGE
83483
x * 112000, membrane-bound CDase from kidney, SDS-PAGE, x * 83483, CDase from kidney, sequence calculation, x * 113000, endoplasmic reticulum-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE, x * 133000, Golgi-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE
87000
-
determined by SDS-PAGE and Western blot analysis, signal between 75 and 100 kDa
95000
97000
110000
-
x * 110000, glycosylated recombinant enzyme, SDS-PAGE, x * 82500, deglycosylated recombinant enzyme, SDS-PAGE
118000
synthesized as 118 kDa and 142 kDa isoforms
13000
processed mature heterodimeric enzyme, alpha subunit
13000
-
alpha,beta, 1 * 13000 + 1 * 40000, SDS-PAGE, treatment with beta-mercaptoethanol
13000
-
alpha,beta, 1 * 13000 + 1 * 40000, SDS-PAGE, deglycosylation reduces beta unit weight to 28000 Da
13000
-
x * 13000 + x * 40000, alpha- and beta-subunit, recombinant AC from CHO cells contains two distinct beta-subunits likely due to C-terminal processing, SDS-PAGE
142000
synthesized as 118 kDa and 142 kDa isoforms
40000
processed mature heterodimeric enzyme, beta subunit
40000
-
alpha,beta, 1 * 13000 + 1 * 40000, SDS-PAGE, treatment with beta-mercaptoethanol
40000
-
alpha,beta, 1 * 13000 + 1 * 40000, SDS-PAGE, deglycosylation reduces beta unit weight to 28000 Da
40000
-
x * 13000 + x * 40000, alpha- and beta-subunit, recombinant AC from CHO cells contains two distinct beta-subunits likely due to C-terminal processing, SDS-PAGE
95000
-
determined by SDS-PAGE and Western blot analysis, the multiple band pattern between about 95 and 135 kDa may be due to the complexity of modifications, such as O-glycosylation and N-glycosylation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
additional information
?
-
x * 100000, about, glycosylated enzyme, SDS-PAGE, x * 80000, about, deglycosylated enzyme, SDS-PAGE
?
-
x * 110000, glycosylated recombinant enzyme, SDS-PAGE, x * 82500, deglycosylated recombinant enzyme, SDS-PAGE
?
x * 44000, about, sequence calculation, x * 50000, about, recombinant glycosylated enzyme, SDS-PAGE
?
-
x * 13000 + x * 40000, alpha- and beta-subunit, recombinant AC from CHO cells contains two distinct beta-subunits likely due to C-terminal processing, SDS-PAGE
?
13000 (alpha-subunit) + 30000 (beta-subunit)
?
x * 112000, membrane-bound CDase from kidney, SDS-PAGE, x * 83483, CDase from kidney, sequence calculation, x * 113000, endoplasmic reticulum-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE, x * 133000, Golgi-form of Myc-tagged CDase expressed in HEK-239, SDS-PAGE
dimer
-
alpha,beta, 1 * 13000 + 1 * 40000, SDS-PAGE, treatment with beta-mercaptoethanol
dimer
-
alpha,beta, 1 * 13000 + 1 * 40000, SDS-PAGE, deglycosylation reduces beta unit weight to 28000 Da
dimer
-
the 53 kDa acid ceramidase pre-polypeptide undergoes autocatalytic processing into two subunits of 13 and 40 kDa, respectively
additional information
the enzyme has a transmembrane domain (residues 20-39), and a DUF616 domain (residues 107-409)
additional information
-
the enzyme has a transmembrane domain (residues 20-39), and a DUF616 domain (residues 107-409)
-
additional information
-
the luminal ACER2 N-terminal tail, comprising 36 amino acid residues, is important for ACER2 activity, but the terminal 13 amino acid residues are not required for its activity
additional information
the crystal structures of the two receptor subtypes, ADIPOR1 and ADIPOR2, show a similar overall seven-transmembranedomain architecture with large unoccupied cavities and a zinc binding site within the seven transmembrane domain
additional information
the overall structure showed a catalytic domain (residues 99-626), a short linker (627-641), and an immunoglobulin (IG)-like domain (642-780). In comparison with the distantly homologous bacterial CDase (bCDase), in the human nCDase, a 30-residue subdomain insert replaces a 6-residue span of bCDase. This insertion seems to stabilize two alpha helixes of the active site. This subdomain conformation is aided by two internal disulfide bridges, formed by four cysteines that are conserved in eukaryotes
additional information
-
the C-terminal tail is essential for enzyme activity and correct folding
additional information
-
neutral CDase is composed of two domains: a novel NH2-terminal domain harboring an active site and an immunoglobulin-like COOH-terminal domain. A zinc-binding site is located in the center of the NH2-terminal domain, whereas a calcium/magnesium-binding site is found at the interface between the NH2-terminal and COOH-terminal domains
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
CDase contains a 26 amino acids signal peptide
glycoprotein
-
eight potential N-glycosylation sites, four potential O-glycosylation sites
glycoprotein
the enzyme contains N-glycan and O-glycan, the intestinal enzyme is glycosylated with complex-type N-glycans and O-glycans
glycoprotein
six N-glycosylation sites at amino acid positions 173, 259, 286, 301, 342, and 348, and a single O-glycosylation site at positions 344 present on the beta-subunit are determined in the zebrafish sequence. The alpha-subunit does not have any putative glycosylation site. The recombinant enzyme is glycosylated at the beta-subunit. Deglycosylation by PNGase F
glycoprotein
-
recombinant AC from CHO cells contains mostly high mannose-type oligosaccharides, beta-subunit is glycosylated
glycoprotein
acid ceramidase has six potential N-glycosylation sites
glycoprotein
recombinant CDase expressed in Pichia pastoris GS115
glycoprotein
112 kDa CDase from kidney, highly N-glycosylated, sequence contains 9 putative N-glycosylation sites, the N-glycosylation process is indispensable for enzyme activity
proteolytic modification
the zebrafish enzyme is subjected to proteolytic cleavage during maturation, the enzyme has autoproteolytic activity
proteolytic modification
-
AC is first synthesized as 55 kDa precursor protein that is proteolytically processed
proteolytic modification
-
a highly purified, recombinant human acid ceramidase precursor undergoes self-cleavage into alpha and beta subunits. The following mechanism for acid ceramidase self-cleavage and activation is proposed: Asp162 likely forms a hydrogen bond with Cys143, initiating a conformational change that allows Arg159 to act as a proton acceptor. This, in turn, facilitates an intermediate thioether bond between Cys143 and Ile142, the site of acid ceramidase cleavage. Hydrolysis of this bond is catalyzed by water
proteolytic modification
the enzyme performs autocatalysis. In the proenzyme, the catalytic center is buried and protected from solvent. Autocleavage triggers a conformational change exposing a hydrophobic channel leading to the active site. Substrate modeling suggests distinct catalytic mechanisms for substrate hydrolysis versus autocleavage
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of recombinant truncated enzyme, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant ADIPOR2 complexed with a free fatty acid molecule, X-ray diffraction structure determination and analysis
purified recombinant His6-tagged extracellular domain of nCDase, residues 99-780, in complex with phosphate, hanging drop vapor diffusion, mixing of equal volumes of 3 mg/ml protein in 100 mM NaCl, 10 mM HEPES, pH 7.0, with reservoir solution containing 0.2 M Li2SO4, 10% PEG 1000, and 0.1 M citrate-phosphate, pH 4.6, at 16°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using Pseudomonas aeruginosa bCDase structure, PDB ID 2ZWS, as template
purified recombinant N-glycosylated extracellular region of nCDase in complex with phosphate, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant wild-type and mutant BRIL-fusion ACER3 enzyme reconstituted into 10:1 monoolein:cholesterol at a ratio of 1:1.5 protein:lipid by weight, from precipitant solution consisting of 34-40% PEG 400, 0.1 M HEPES, pH 7.5, 75 mM magnesium sulfate, and 5% DMSO, 5 days, X-ray diffraction structure determination and analysis at 2.70-2.85 A resolution
crystal structure of neutral CDase for the ceramide-free and C2-ceramide-bound forms
-
the crystal structures of neutral CDase from Pseudomonas aeruginosa in the C2-ceramide-bound and -unbound forms are determined at 2.2 and 1.4 A resolutions, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D331N
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
E138V
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
E180K
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
E33G
naturally occuring inactive mutant, the mutation results in the destabilization of the calcium binding site
F136L
naturally occuring disease mutation, F136 is located near the lipid tails of the modeled substrate and at the alpha-beta interface, the F136L mutation can destabilize the heterodimer and substrate interactions, affects the hydrophobic surface of the protein
F328Q/F329Q/L330Q
site-directed mutagenesis, hydrophobic patches mutated near the substrate binding channel, the mutant shows reduced ceramide hydrolysis compared with wild-type in the liposomal assay
F87Q/V88Q/V93Q
site-directed mutagenesis, mutation of a site further from the substrate-binding site, the mutant shows reduced ceramide hydrolysis compared with wild-type in the liposomal assay
G168W
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
G235D
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
G235R
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
L182V
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
L80Q/V165Q/L167Q
site-directed mutagenesis, hydrophobic patches mutated near the substrate binding channel, the mutant shows reduced ceramide hydrolysis compared with wild-type in the liposomal assay
N320D
N320S
N320X
naturally occuring disease mutation, active site residue mutation, inhibits autocleavage and/or substrate hydrolysis
P362R
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
P362T
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
R226P
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
R254G
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
R333G
naturally occuring disease mutation, active site residue mutation, that hinders the R333 function, affects the activation of the proenzyme
R333H
naturally occuring disease mutation, active site residue mutation, that hinders the R333 function, affects the activation of the proenzyme
R333X
naturally occuring disease mutation, active site residue mutation, inhibits autocleavage and/or substrate hydrolysis
S258A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S354A
S374A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S396A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
S595A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S729A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S77A
the mutant enzyme has a low but measurable ceramidase activity of approximately 0.17% of that of wild-type ACER3. The reaction of S77A follows Michaelis-Menten kinetics with a reduced Vmax (0.061 vs. 47 pmol/min/mg) and a slight increase in KM from 0.0155 mM to 0.038 mM
S77C
the point mutant has no measurable alkaline ceramidase activity at pH 9.4. Decreasing the pH to 7.5 shows an increase of S77C activity, equivalent to the S77A mutant
T179I
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
T222K
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
T42A
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
T42M
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
V97D
naturally occuring disease mutation, the mutation inhibit the interaction of aCDase with negatively charged liposomes
V97E
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
V97G
naturally occuring disease mutation, the mutation likely destabilizes helix-alpha2 in the alpha-subunit in which it resides
W169Q/I171Q/W176Q
site-directed mutagenesis, mutation of the L4-6 loop in the beta-subunit, the mutant shows reduced ceramide hydrolysis compared with wild-type in the liposomal assay
W169R
naturally occuring disease mutation, the mutation affects the hydrophobic surface of the protein
Y36C
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
H97A/H99A
mutant, Zn2+-binding site and deprotonation site mutated
E757R
-
mutation has no effect on activity, subcellular localization of mutant CDase expressed in HEK-293 cells
F756D
-
inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells
F756I
-
mutation has little effect on activity, subcellular localization of mutant CDase expressed in HEK-293 cells
F756R
-
inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells
I758D
-
inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells
I758F
-
mutation decreases activity to 20% of wild-type CDase activity, subcellular localization of mutant CDase expressed in HEK-293 cells
I758R
-
inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells
I758V
-
same activity as wild-type CDase, subcellular localization of mutant CDase expressed in HEK-293 cells
additional information
N320D
naturally occuring disease mutation, active site residue mutation, disrupts the functional requirement for an asparagine side chain at this position
N320D
naturally occuring disease mutation, affects the activation of the proenzyme
N320S
naturally occuring disease mutation, active site residue mutation, disrupts the functional requirement for an asparagine side chain at this position
N320S
naturally occuring disease mutation, affects the activation of the proenzyme
additional information
construction of T-DNA insertion mutants harboring the mutation in exn tod1-1 or tod1-2
additional information
construction of an acer-1 T-DNA insertion mutant, the acer-1 allele has a T-DNA insertion in the 50 untranslated region (5'-UTR) of AtACER, phenotype with reduced stature, with smaller, narrower, glossier leaves and smaller flowers than wild-type plants, sphingolipid profiles in acer-1, overview. The AtACER transgene can complement the phenotypes of the acer-1 mutant
additional information
the Arabidopsis thaliana neutral ceramidase DNA insertion mutant ncer1 has no visible phenotype, but accumulates hydroxyceramides, and shows increased sensitivity to oxidative stress induced by methyl viologen. Plants overexpressing AtNCER1 show increased tolerance to oxidative stress. Neutral ceramidase mutants have increased sensitivity to C2-ceramide induced cell death
additional information
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the Arabidopsis thaliana neutral ceramidase DNA insertion mutant ncer1 has no visible phenotype, but accumulates hydroxyceramides, and shows increased sensitivity to oxidative stress induced by methyl viologen. Plants overexpressing AtNCER1 show increased tolerance to oxidative stress. Neutral ceramidase mutants have increased sensitivity to C2-ceramide induced cell death
additional information
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the Arabidopsis thaliana neutral ceramidase DNA insertion mutant ncer1 has no visible phenotype, but accumulates hydroxyceramides, and shows increased sensitivity to oxidative stress induced by methyl viologen. Plants overexpressing AtNCER1 show increased tolerance to oxidative stress. Neutral ceramidase mutants have increased sensitivity to C2-ceramide induced cell death
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additional information
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construction of T-DNA insertion mutants harboring the mutation in exn tod1-1 or tod1-2
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additional information
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enzyme knockout, via antisense construct using three different antisense morpholino oligonucleotides (AMOs 1, 2, and 3) that are designed based on sequences at different sites of the 5'-untranslated region, leads to an increase in the number of zebrafish embryos with severe morphological qand cellular abnormalities such as abnormal morphogenesis inhead and tail, pericardiac edema, defect of blood cell circulation, and an increase in apoptotic cells, phenotype, overview
additional information
insertional mutagenesis leading to enzyme inactivation, transposon location of the dacer mutant, overview. The mutation increases the levels of ceamides in both the pupal and adult stages, and increases pre-adult development time, lifespan, and anti-oxidative stress capacity, overview
additional information
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insertional mutagenesis leading to enzyme inactivation, transposon location of the dacer mutant, overview. The mutation increases the levels of ceamides in both the pupal and adult stages, and increases pre-adult development time, lifespan, and anti-oxidative stress capacity, overview
additional information
targeted expression of neutral CDase can rescue retinal degeneration in a subset of Drosophila phototransduction mutants
additional information
generation of a Dacer-deficient Drosophila melanogaster mutant, which has higher catalase (CAT) activity and CAT transcription level, leading to higher resistance to oxidative stress induced by paraquat, quantitative proteomic analysis of wild-type and mutant cells. Three oxidoreductases, including two cytochrome P450 (CG3050, CG9438) and an oxoglutarate/iron-dependent dioxygenase (CG17807), are most significantly upregulated in the Dacer overexpressing mutant. Altered antioxidative activity in Dacer mutant might be responsible for increased oxidative stress resistance
additional information
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generation of a Dacer-deficient Drosophila melanogaster mutant, which has higher catalase (CAT) activity and CAT transcription level, leading to higher resistance to oxidative stress induced by paraquat, quantitative proteomic analysis of wild-type and mutant cells. Three oxidoreductases, including two cytochrome P450 (CG3050, CG9438) and an oxoglutarate/iron-dependent dioxygenase (CG17807), are most significantly upregulated in the Dacer overexpressing mutant. Altered antioxidative activity in Dacer mutant might be responsible for increased oxidative stress resistance
additional information
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insertional mutagenesis leading to enzyme inactivation, transposon location of the dacer mutant, overview. The mutation increases the levels of ceamides in both the pupal and adult stages, and increases pre-adult development time, lifespan, and anti-oxidative stress capacity, overview
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additional information
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blocking of acid ceramidase but not sphingosine kinase activity in alveolar macrophages leads to decreased ERK and Akt activity and induction of cell death, sphingosine and L-threo-dihydrosphingosine reverse the antisurvival effects of acid ceramidase inhibition in alveolar macrophages
additional information
high ectopic expression of haCER2 causes fragmentation of the Golgi complex and growth arrest in HeLa cells due to sphingosine accumulation, low ectopic expression increases sphingosine 1-phosphate level without sphingosine accumulation, promoting cell proliferation in serum-free medium, this proliferative effect is suppressed by dimethylsphingosine, an inhibitor of the S1P formation, or by RNAi -mediated inhibition of S1P1, a G-protein-coupled receptor for S1P, the RNAi-mediated down-regulation of haCER2 enhances the serum deprivation-induced growth arrest and apoptosis of HeLa cells, which is inhibited by addition of exogenous S1P, serum deprivation up-regulates both haCER2 mRNA and activity in recombinant HeLa cells, haCER2mRNA is also up-regulated in some tumors, overview
additional information
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high ectopic expression of haCER2 causes fragmentation of the Golgi complex and growth arrest in HeLa cells due to sphingosine accumulation, low ectopic expression increases sphingosine 1-phosphate level without sphingosine accumulation, promoting cell proliferation in serum-free medium, this proliferative effect is suppressed by dimethylsphingosine, an inhibitor of the S1P formation, or by RNAi -mediated inhibition of S1P1, a G-protein-coupled receptor for S1P, the RNAi-mediated down-regulation of haCER2 enhances the serum deprivation-induced growth arrest and apoptosis of HeLa cells, which is inhibited by addition of exogenous S1P, serum deprivation up-regulates both haCER2 mRNA and activity in recombinant HeLa cells, haCER2mRNA is also up-regulated in some tumors, overview
additional information
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no accumulation of diacylglycerol occurs due to overexpression of the recombinant enzyme in myoblasts, but the recombinant enzyme prevents the inhibition of insulin signaling by palmitate in C1c12 myotubes, overview
additional information
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ACER2 mutant, ACER2DELTAN36, lacking the N-terminal tail, the first 36 amino acid residues, exhibits undetectable activity and is mislocalized to the endoplasmic reticulum. Overexpression of ACER2, ACER2DELTAN13, but not ACER2DELTAN36 increased the release of sphingosine 1-phosphate from cells, suggesting that its mislocalization does not affect the ability of ACER2 to regulate sphingosine 1-phosphate secretion. However, overexpression of ACER2 but not ACER2DELTAN13 or ACER2DELTAN36 inhibits the glycosylation of integrin beta1 subunit and Lamp1, suggesting that its mistargeting abolishes the ability of ACER2 to regulation protein glycosylation
additional information
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overexpression of ACER2 augments the 4-N-(4-hydroxyphenyl)retinamide-induced generation of dihydrosphingosine, as well as 4-N-(4-hydroxyphenyl)retinamide cytotoxicity and death in tumor cells, whereas knocking down ACER2 had the opposite effects. ACER2 overexpression or GT11, a dihydrosphingosine desaturase inhibitor, treatment alone caused little or no decrease in cell viability, whereas ACER2 overexpression along with GT11 treatment markedly decreased cell viability
additional information
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a germ line single nucleotide polymorphism creates a splice site resulting in alternatively-spliced KLF6 isoforms, termed KLF6 SV1, SV2 and SV3. The splice variants show that SV1 has a counteracting effect on the wild-type KLF6 tumor suppressor activity, thus permitting tumor progression
additional information
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knockdown of ACER1, ACER2, and ACEr3 in K562 cells by siRNA and lentiviral shRNA transduction. Transduction with lentiviral particles expressing an ACER3-specific shRNA decreases ACER3 mRNA but increased ACER2 mRNA in K562 cells, and transduction with lentiviral particles expressing ACER2-specific shRNA decreases ACER2 mRNA but increased ACER1 mRNA and vice versa. Thus knocking down the expression of one alkaline ceramidase up-regulates another
additional information
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generation of a tetracycline-inducible ASAH1 short hairpin RNA H295R human adrenocortical stable cell line
additional information
generation of a tetracycline-inducible ASAH1 short hairpin RNA H295R human adrenocortical stable cell line
additional information
overexpression and knockdown of acid ceramidase via lentiviral transduction in HEK-293T/17 cells
additional information
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overexpression and knockdown of acid ceramidase via lentiviral transduction in HEK-293T/17 cells
additional information
ASAH1 silencing by siRNA. An increase in expression in the cell cycle inhibitor p27 is observed upon MITF inhibition by siRNA, but does not occur in these cells when they are transduced with ASAH1
additional information
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ASAH1 silencing by siRNA. An increase in expression in the cell cycle inhibitor p27 is observed upon MITF inhibition by siRNA, but does not occur in these cells when they are transduced with ASAH1
additional information
ATRA downregulates nCDase expression at the message level results in less protein and activity in SH-SY5Y neuroblastoma cells
additional information
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RNA interference gene silencing of the neutral CDase in mouse B16 cells leading to reduced enzyme activity and reduced levels of sphingosine and sphingosine 1-phosphate
additional information
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construction of disruption mutant of Asah2 by using a targeted ES clone to produce chimeras and subsequently heterozygous mice, interbreeding of the Asah2 heterozygous mice yielded wild-type, heterozygous, and homozygous mutant null offspring, Asah2 null mice are deficient in the intestinal degradation of ceramide, Asah2 null mice have a normal life span and do not show obvious abnormalities or major alterations in total ceramide levels in tissues
additional information
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truncation of six C-terminal amino acids, but not of five, results in complete loss of CDase activity
additional information
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construction of a CDase-null mutant via homologous recombination and gene disruption, CDase-deficient mutants lack any CDase activity, the hemolytic activity by the CDase mutants against human erythrocytes is significantly reduced compared with that by the wild-type
additional information
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construction of a CDase-null mutant via homologous recombination and gene disruption, CDase-deficient mutants lack any CDase activity, the hemolytic activity by the CDase mutants against human erythrocytes is significantly reduced compared with that by the wild-type
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additional information
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truncation of four, but not three, amino acid residues at the C-terminus results in a complete loss of activity as well as surface expression in HEK-293 cells, the truncated enzymes are retained in the endoplasmic reticulum and rapidly degraded without transportation to the Golgi apparatus also leading to an immature/incorrect glycosylation of the protein
additional information
a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells
additional information
comparison of membrane topology of wild-type and mutant enzymes, overview
additional information
comparison of membrane topology of wild-type and mutant enzymes, overview
additional information
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comparison of membrane topology of wild-type and mutant enzymes, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-85°C, 2 months, with 1 mg/ml bovine serum albumin, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
112 kDa-form from kidney: 3604fold, completely insoluble by freeze-thawing in contrast to liver CDase
concanavalin A column chromatography, Blue Sepharose column chromatography, and Superose 12 gel filtration
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native enzyme 20000fold from brain by anion exchange chromatography, affinity and hydrophobic interaction chromatography, and cation exchange chromatography, to homogeneity
native enzyme 2147.1fold from brain to homogeneity by anion exchange and hydrophobic interaction chromtography, gel filtration, and another step of anion exchange chromatography
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native intestinal enzyme over 307fold by acetone precipitation and ion-exchange, hydrophobic-interaction chromatography, and gel filtration, to homogeneity
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Q-Sepharose column chromatography, Superdex 200 gel filtration, heparin-Sepharose column chromatography, phenyl-Sepharose column chromatography, and Mono Q column chromatography
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recombinant BRIL-fusion FLAG-tagged wild-type and mutant enzymes from Spodoptera frugiperda Sf9 cells by immunoaffinity and FLAG-tag affinity chromatography, the FLAG-tag is cleaved off by TEV protease, followed by gel filtration. The purified E33G ACER3 mutant is highly unstable during purification
recombinant C-terminally His-tagged enzyme from Pichia pastoris strain GS115 by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant enzyme from Trichopulsia ni High Five cell membranes
recombinant HA- and His6-tagged AsahA 90fold from Aspergillus oryzae
recombinant His-tagged CDase from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography and gel filtration
recombinant secreted His6-tagged nCDase (residues 99-780) from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography and gel filtration
wild-type CDase from 3-L culture: 217fold, recombinant CDase expressed in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
112 kDa-form from kidney, expression in Escherichia coli BL21(DE3), in CHOP cells and overexpression in HEK-239 cells
acid ceramidase maps to 8p22, the region of chromosome 8 most frequently deleted in prostate cancer. Regulation of gene expression by acid ceramidase in prostate cancer cells, overview
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cloned from a brain cDNA library, stable overexpression of V5/His-tagged enzyme in HEK-293 cells
cloning of human nCDase gene in pLenti6.3/TO/V5 and recombinant expression in HCT-116 cells and in cells transfected with the Golgi-targeted bacterial ceramidase and sphingomyelinase
DNA and amino acid determination, phylogenetic tree
DNA and amino acid determination, phylogenetic tree, genetic structure, the promoter region of mouse brain neutral CDase contains transcriptional response elements for GATA-2, C/EBP, and HNF3beta
DNA and amino acid determination, phylogenetic tree, recombinant expression of myc-tagged or GFP-tagged neutral CDase in HEK293 cells. When expressed in HEK293 or CHOP cells, both wild-type and mutant rat neutral CDase with a deleted mucin box are released into the medium
DNA and amino acid sequence determination and analysis, overexpression of C-terminally myc-tagged enzyme in CHOP cells and zebrafish BRF41 cells in endoplasmic reticulum and Golgi apparatus, as well as in plasma membranes
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DNA and amino acid sequence determination and analysis, recombinant overexpression in Trichopulsia ni High Five cell membranes via baculoviral transfection, expression of GFP-tagged enzyme
expression analysis of isozymes during keratinocyte differentiation, expression levels in undifferentiated, early-stage and advanced-stage cells, and in whole epidermis by RT-PCR
expression in Escherichia coli DH5alpha and BL21, expression at low levels in Pseudomonas putida KT2440 and Pichia pastoris GS115, sequencing
expression in Saccharomyces cerevisiae enzyme-deficient doubleknockout strain.ypc1.ydc1 microsomes under control of the Gal1 promoter
expression in Saccharomyces cerevisiae mutant cells that lack endogenous ceramidase activity
expression of C-terminally myc-tagged enzyme in CHOP cells in endoplasmic reticulum and Golgi apparatus, as well as in plasma membranes
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expression of FLAG-tagged wild-type ACER2 and FLAG-tagged ACER2 mutants in Saccharomyces cerevisiae mutant cell microsomes, DELTAypc1 and DELTAydc1, that lack endogenous ceramidase activity
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expression of His6-tagged CDase in Escherichia coli strain BL21(DE3)
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expression of the N-terminally GFP-tagged enzyme lacking the 19 amino acid N-terminal extension in HEK-293 and MCF7 cells exclusively in mitohcondria, expression of the longer enzyme version cloned from kidney resulted in localization of the recombinant enzyme in the plasma membrane of HEK-293 cells
functional overexpression of N-terminally C-myc-tagged enzyme, residues 1-1218, in 293T cells using a retroviral vector, in cell culture supernatant, recombinant retrovirus from 293T cell supernatant is used to infect C2C12 myoblasts
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gene ASAH1, DNA and amino acid sequence determination and analysis, genotyping, semi-quantitative enzyme expression analysis
gene ASAH1, expression analysis
gene ASAH1, in vitro translation of FLAG-tagged enzyme from the pCMV6-XL5-ASAH1 plasmid and transient expression in H295R cells
gene ASAH1, recombinant overexpression in HEK-293 cells from pLenti6.3/TO/V5-DEST vector
gene ASAH1, recombinant overexpression in HEK-293T/17 cells, quantitative real-time RT-PCR enzyme expression analysis
gene asah1b, DNA and amino acid sequence determination and analysis, recombinant overexpression of C-terminally His-tagged enzyme in Pichia pastoris strain GS115, method optimization, overview
gene Asah2, DNA and amino acid sequence determination and analysis, expression in ES cells
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gene asahA, DNA and amino acid sequence determination and analysis, overexpression of HA- and His6-tagged neutral CDase in Aspergillus oryzae
gene At4G22330 or acer-1, phylogenetic analysis, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana
gene bwa, recombinant expression of His-tagged wild-type and mutant enzymes, the endogenous signal peptide comprising the first 21 residues is replaced by the melittin signal peptide (MKFLVNVALVFMVVYISYIYA) followed by a His6-tag. Constructs encompassed residues 22 to 395 of homologues from human (UniProt Q13510 variant Ile93Val), nmr (Heterocephalus glaber, UniProt A0A0P6JG37 variant Asn348Ser), or cmw (Balaenoptera acutorostrata scammoni, RefSeq XP_007174053). The latter two homologues are codon-optimized
gene bwa, recombinant expression of wild-type and mutant enzymes in Spodoptera frugiperda Sf9 cells via baculovirus transfection system, the enzyme is cloned with C-terminal BRIL soluble module (thermostabilized apocytochrome b562RIL) and an N-terminal Flag epitope followed by a tobacco etch virus protease site
gene cdase, the gene encoding the enzyme is adjacent to that encoding hemolytic phospholipase C, plcH, in the genome of Pseudomonas aeruginosa
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gene ncer1, transient expression of GFP-tagged enzyme in Arabidosis thaliana protoplasts in the endoplasmic reticulum, quantitative real-time PCR enzyme expression analysis
gene NlnCDase, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the enzyme in insect High Five cells in microsomes, quantitative enzyme expression analysis
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gene tod1, DNA and amino acid sequence determination and analysis, genetic structure, phylogenetic tree
into the vector pET23a for expression in Escherichia coli BL21DE3 pLysS cells, in B834DE3 pLysS cells for preparation of selenomethionine-substituted enzyme
maCER1 gene, overexpression in HeLa cells, expression in yeast cells and in COS-1 cells, sequencing
radiation-induced acid ceramidase gene transactivation by activator protein 1 binding on the proximal promoter is sensitive to inhibition of de novo ceramide biosynthesis, as demonstrated by promoter reporter and ChIP-qPCR analyses
recombinant expression in insect cells of active truncated enzyme, consisting of the extracellular region (residues 99-780) and lacking the short intracellular region (residues 1-12), the transmembrane domain (residues 12-34), and the flexible O-glycosylated mucin box (residues 34-99)
recombinant expression of adenoviral vector expressing the human acid ceramidase (Ad-ASAH1) gene in human OBA-9 cells. ASAH1-over-expressing OBA-9 cells show significantly lower mRNA expressions of caspase-3 as well as the percentage of Annexin V-positive cells, when compared to controls. In response to stimulation with Porphyromonas gingivalis, ASAH1-overexpressing OBA-9 cells produce less TNF-alpha, IL-6, and IL1beta pro-inflammatory cytokines than observed in OBA-9 cells transduced with Ad-control vector, quantitative real-time PCR expression analysis
recombinant expression of V5/His-tagged enzyme using vector pEF6-V5/His in HEK-293 cells
recombinant overexpression of C-terminally His6-tagged extracellular region of human nCDase (residues 99-780) lacking the flexible O-glycosylated mucin box in Spodoptera frugiperda Sf9 cells, the enzyme is secreted
the Dacer/brainwashing or BWA gene CG13969 localizes to the 38B2-3 region of the left arm of the second chromosome, DNA and amino acid sequence determination and analysis, functional overexpression in High Five insect cells
the gene encoding CER2 is located on chromosome 9, cloning from a liver cDNA library, functional expression of CER2 in HeLa cells showing 20fold increased enzyme activity in microsomes
transient expression of FLAG-tagged ACER3 in HSC-1 cells. ACER2 overexpression in HeLa cells, knockdown by RNA interference with ACER2-specific siRNA
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
acid ceramidase expression in gingival cells is suppressed by stimulation with Porphyromonas gingivalis in vitro
ACTH/cAMP signaling stimulates acid ceramidase ASAH1 transcription and activity
increased ACER2 mRNA expression in human cancer tissue in the liver and colon when compared to samples of healthy individuals
infection with the rice strip virus or treatment with insecticides significantly increase LsnCer mRNA expression and its enzymatic activity in Laodelphax striatellus, quantitative real time PCR enzyme expression analysis
interleukin-1beta increases the activity, mRNA levels and protein synthesis of acid ceramidase
interleukin-1beta increases the activity, mRNA levels and protein synthesis of neutral ceramidase
ionizing radiation selectively upregulates acid ceramidase in prostate cancer PCa cells, no induction of neutral and alkaline ceraamidases. Radiation-induced acid ceramidase gene transactivation by activator protein 1 binding on the proximal promoter is sensitive to inhibition of de novo ceramide biosynthesis, as demonstrated by promoter reporter and ChIP-qPCR analyses
irradiation induces expression of ASAH1 in glioblastoma multiforme cells, radiation induces oversecretion of ASAH1
significantly decreased ceramide levels are observed in human colon cancers, gliomas, ovarian cancers, thyroid and gastrointestinal cancers
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the microphthalmia-associated transcription factor (MITF) drives expression of ASAH1. MITF is a transcription factor that binds to DNA to control the expression of its targets. MITF stimulates the activity of ASAH1 promoter
the prominent antiestrogen tamoxifen is a pan-effective acid ceramidase inhibitor in the low micromolar range, as demonstrated in a wide spectrum of cancer cell types, prostate, pancreatic, colorectal, and breast. Tamoxifen does not impact cell viability or inhibit the enzyme activity in cell-free assays. Mechanism of action via increases in lysosomal membrane permeability, and time- and dose-dependent downregulation of acid ceramidase protein expression, overview. The downregulation can be blocked by a cathepsin B inhibitor
the retinoid N-(4-hydroxyphenyl)retinamide, i.e. fenretinide, increases the expression of ACER-2 through a retinoic acid receptor-independent and caspase-dependent manner
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transcripts and activity of the NlnCDase are upregulated under abiotic stresses including starvation, abnormal temperature, and insecticides, and biotic stress of resistant rice varieties
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treatment with fetal bovine serum (FBS) induces approximately a 60% increase in nCDase mRNA expression in coronary artery smooth muscle cells after 6 h. FBS elevates nCDase mRNA expression approximately 35% in HEK-293. cells c-Jun/AP-1 signaling in part regulates serum-induced human nCDase gene transcription
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of a method for the specific visualization of catalytically active acid ceramidase in intracellular compartments is crucial for diagnosis and follow-up of therapeutic strategies in diseases linked to altered enzyme activity
drug development
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development of small molecule drugs, that inhibit AC enzyme activity, is a promising approach for improving standard cancer therapy and patient's clinical outcomes
medicine
medicine
CDase from Pseudomonas aeruginosa may be a virulence factor in infections, may be involved in the ceramide deficiency in the horny layer of the epidermis of patients with atopic dermatitis suffering from bacterial infections
medicine
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patients with the lipid storage disorder, the Farber disease, have a marked AC deficiency
medicine
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Farber disease is diagnosed by the demonstration of reduced acid ceramidase activity, abnormally high ceramide levels in cultured cells, biopsy samples or urine, and the presence of Farber bodies, comma-shaped curvilinear tubular structures. The enzyme is likely to continue to be a target for new drug development in cancer and other disorders
medicine
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in human prostate tissues, acid ceramidase and cathepsin B overexpression are strongly associated and may relate to poor outcome
medicine
because of its central role in the ceramide metabolism, the enzyme may offer a novel molecular target in disorders with dysfunctional ceramide-mediated signaling
medicine
because of its central role in the ceramide metabolism, the enzyme may offer a novel molecular target in disorders with dysfunctional ceramide-mediated signaling
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