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Information on EC 3.5.1.23 - ceramidase and Organism(s) Homo sapiens and UniProt Accession Q5QJU3

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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
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q5QJU3 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adipor2, adiponectin receptor, ceramidase, acid ceramidase, asah1, neutral ceramidase, acdase, ncdase, acer2, acer3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid ceramidase
-
alkaline ceramidase
-
alkaline ceramidase 2
ACER2
alkCDase-1
-
alkCDase-2
-
ceramidase
-
Golgi alkaline ceramidase
-
neutral ceramidase
-
phytoalkaline ceramidase
-
phytoCDase
-
(dihydro)ceramidase
-
-
aCDase
ACER type 3
-
ACER-2
-
-
ACER1
ACER2
ACER3
acid ceramidase
acylsphingosine deacylase
-
-
-
-
adiponectin receptor
-
alkaline ceramidase
alkaline ceramidase 1
alkaline ceramidase 2
-
-
alkaline ceramidase 3
ASAH1
ASAH2
ASAH3
gene name of alkaline ceramidase
ceramidase
glycosphingolipid ceramide deacylase
-
-
-
-
intramembrane ceramidase
-
N-acylsphingosine amidohydrolase
-
-
-
-
N-acylsphingosine amidohydrolase 2
-
N-acylsphingosine amidohydrolase-1
-
N-acylsphingosine aminohydrolase
-
N-acylsphingosine deacylase
N-CDase
nCDase
neutral ceramidase
PHP32
-
-
-
-
Putative 32 KDA heart protein
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a ceramide + H2O = a carboxylate + sphingosine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deacylation
-
-
hydrolysis
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
N-acylsphingosine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37289-06-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
show the reaction diagram
-
-
-
?
ceramide + H2O
sphingosine + fatty acid
show the reaction diagram
-
-
-
?
D-erythro-myristoyl-sphingosine + H2O
myristate + sphingosine
show the reaction diagram
-
-
-
?
D-erythro-oleoyl-sphingosine + H2O
oleate + sphingosine
show the reaction diagram
-
-
-
?
D-erythro-palmitoyl-sphingosine + H2O
palmitate + sphingosine
show the reaction diagram
-
-
-
?
D-erythro-tetracosanoyl-sphingosine + H2O
tetracosanoate + sphingosine
show the reaction diagram
i.e. D-e-C24:0-ceramide
-
-
?
(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
?
show the reaction diagram
9.9% hydrolysis
-
-
ir
11-eicosenoyl-ceramide + H2O
sphingosine + 11-eicosenoic acid
show the reaction diagram
-
-
-
-
?
11-eicosenoyl-dihydroceramide + H2O
dihydrosphingosine + 11-eicosenoic acid
show the reaction diagram
-
-
-
-
?
11-eicosenoyl-phytoceramide + H2O
phytosphingosine + 11-eicosenoic acid
show the reaction diagram
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
ir
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
show the reaction diagram
C12:0-ceramide + H2O
laurate + sphingosine
show the reaction diagram
-
-
-
-
?
C14:0-ceramide + H2O
myristate + sphingosine
show the reaction diagram
-
-
-
-
?
C16:0-ceramide + H2O
palmitate + sphingosine
show the reaction diagram
-
-
-
-
?
C18-ceramide + H2O
stearate + sphingosine
show the reaction diagram
preferred substrate, fluorescent C18 ceramide in detergent micelles
-
-
?
C18:0-ceramide + H2O
stearate + sphingosine
show the reaction diagram
-
-
-
-
?
C18:1-ceramide + H2O
oleate + sphingosine
show the reaction diagram
-
-
-
-
?
C20:0-ceramide + H2O
eicosanoic acid + sphingosine
show the reaction diagram
-
-
-
-
?
C20:1-ceramide + H2O
C20:1 fatty acid + sphingosine
show the reaction diagram
-
-
-
-
?
C24-ceramide + H2O
lignocerate + sphingosine
show the reaction diagram
-
-
-
?
C24:0-ceramide + H2O
C24:0 fatty acid + sphingosine
show the reaction diagram
-
-
-
-
?
C24:1-ceramide + H2O
C24:1 fatty acid + sphingosine
show the reaction diagram
-
-
-
-
?
C6-ceramide + H2O
hexanoate + sphingosine
show the reaction diagram
-
-
-
?
C6:0-ceramide + H2O
hexanoate + sphingosine
show the reaction diagram
-
-
-
-
?
ceramide + H2O
?
show the reaction diagram
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
-
-
?
ceramide + H2O
carboxylate + sphingosine
show the reaction diagram
-
-
-
?
ceramide + H2O
fatty acid + sphingosine
show the reaction diagram
ceramide + H2O
sphingosine + a fatty acid
show the reaction diagram
-
-
-
?
ceramide + H2O
sphingosine + fatty acid
show the reaction diagram
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
D-erythro-4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
show the reaction diagram
-
-
-
?
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
D-erythro-sphingosine + ?
show the reaction diagram
-
-
-
?
D-erythro-C24:1-ceramide + H2O
C24:1 fatty acid + D-erythro-sphingosine
show the reaction diagram
-
-
-
-
?
dihydroceramide + H2O
dihydrosphingosine + fatty acid
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
N-acetylsphingosine + H2O
acetic acid + sphingosine
show the reaction diagram
-
-
-
-
?
N-acylsphingosine + H2O
a carboxylate + sphingosine
show the reaction diagram
-
AC catalyzes the hydrolysis of ceramide to sphingosine and fatty acid
-
-
r
N-acylsphingosine + H2O
carboxylate + sphingosine
show the reaction diagram
N-arachidonoyl-ceramide + H2O
sphingosine + arachidonate
show the reaction diagram
-
-
-
-
?
N-arachidonoyl-dihydroceramide + H2O
dihydrosphingosine + arachidonate
show the reaction diagram
-
-
-
-
?
N-arachidonoyl-phytoceramide + H2O
phytosphingosine + arachidonate
show the reaction diagram
-
-
-
-
?
N-hexanoyl-sphingosine + H2O
hexanoate + sphingosine
show the reaction diagram
-
-
-
?
N-hexanoylsphingosine + H2O
hexanoic acid + sphingosine
show the reaction diagram
-
-
-
-
?
N-lauroylsphingosine + H2O
laurate + sphingosine
show the reaction diagram
-
-
-
-
?
N-lauroylsphingosine + H2O
lauric acid + sphingosine
show the reaction diagram
N-octanoylsphinganine + H2O
octanoic acid + sphingosine
show the reaction diagram
-
-
-
-
?
N-octanoylsphingosine + H2O
octanoic acid + sphingosine
show the reaction diagram
N-oleoyl-ceramide + H2O
sphingosine + oleate
show the reaction diagram
-
-
-
-
?
N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
show the reaction diagram
N-oleoyl-D-sphingosine + H2O
oleate + sphingosine
show the reaction diagram
-
-
-
?
N-oleoyl-dihydroceramide + H2O
dihydrosphingosine + oleate
show the reaction diagram
-
-
-
-
?
N-oleoyl-phytoceramide + H2O
phytosphingosine + oleate
show the reaction diagram
-
-
-
-
?
N-oleoylsphingosine + H2O
oleic acid + sphingosine
show the reaction diagram
N-palmitoylsphinganine + H2O
palmitic acid + sphinganine
show the reaction diagram
-
-
-
-
?
N-palmitoylsphingosine + H2O
palmitic acid + sphingosine
show the reaction diagram
-
-
-
-
r
N-stearoylsphinganine + H2O
stearic acid + sphinganine
show the reaction diagram
-
-
-
-
?
N-[(2S,3R,4E)-1,3-dihydroxy-14-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]tetradec-4-en-2-yl]hexadecanamide + H2O
?
show the reaction diagram
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
?
show the reaction diagram
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
?
show the reaction diagram
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
?
show the reaction diagram
fluorescently labelled ceramide analogue, 4.0% hydrolýsis
-
-
ir
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
show the reaction diagram
substrate C12-NBD ceramide
-
-
?
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
show the reaction diagram
-
i.e. D-ribo-C12-NBD-phytoceramide
-
-
?
NBD-C12-ceramide + H2O
?
show the reaction diagram
-
-
-
?
palmitoyl-sphingosine + H2O
palmitate + sphingosine
show the reaction diagram
-
-
-
r
phytoceramide + H2O
phytosphingosine + fatty acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ceramide + H2O
sphingosine + fatty acid
show the reaction diagram
-
-
-
?
D-erythro-myristoyl-sphingosine + H2O
myristate + sphingosine
show the reaction diagram
-
-
-
?
D-erythro-oleoyl-sphingosine + H2O
oleate + sphingosine
show the reaction diagram
-
-
-
?
D-erythro-palmitoyl-sphingosine + H2O
palmitate + sphingosine
show the reaction diagram
-
-
-
?
D-erythro-tetracosanoyl-sphingosine + H2O
tetracosanoate + sphingosine
show the reaction diagram
i.e. D-e-C24:0-ceramide
-
-
?
C12:0-ceramide + H2O
laurate + sphingosine
show the reaction diagram
-
-
-
-
?
C14:0-ceramide + H2O
myristate + sphingosine
show the reaction diagram
-
-
-
-
?
C16:0-ceramide + H2O
palmitate + sphingosine
show the reaction diagram
-
-
-
-
?
C18:0-ceramide + H2O
stearate + sphingosine
show the reaction diagram
-
-
-
-
?
C18:1-ceramide + H2O
oleate + sphingosine
show the reaction diagram
-
-
-
-
?
C20:0-ceramide + H2O
eicosanoic acid + sphingosine
show the reaction diagram
-
-
-
-
?
C20:1-ceramide + H2O
C20:1 fatty acid + sphingosine
show the reaction diagram
-
-
-
-
?
C24:0-ceramide + H2O
C24:0 fatty acid + sphingosine
show the reaction diagram
-
-
-
-
?
C6:0-ceramide + H2O
hexanoate + sphingosine
show the reaction diagram
-
-
-
-
?
ceramide + H2O
carboxylate + sphingosine
show the reaction diagram
-
-
-
?
ceramide + H2O
fatty acid + sphingosine
show the reaction diagram
ceramide + H2O
sphingosine + a fatty acid
show the reaction diagram
-
-
-
?
ceramide + H2O
sphingosine + fatty acid
show the reaction diagram
D-erythro-C24:1-ceramide + H2O
C24:1 fatty acid + D-erythro-sphingosine
show the reaction diagram
-
-
-
-
?
dihydroceramide + H2O
dihydrosphingosine + fatty acid
show the reaction diagram
-
-
-
-
?
N-acylsphingosine + H2O
carboxylate + sphingosine
show the reaction diagram
N-lauroylsphingosine + H2O
laurate + sphingosine
show the reaction diagram
-
-
-
-
?
N-oleoyl-D-erythro-ceramide + H2O
oleate + D-erythro-sphingosine
show the reaction diagram
-
common substrate in erythrocytes
-
-
?
phytoceramide + H2O
phytosphingosine + fatty acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
activates slightly
Mn2+
activates slightly
Na+
activates
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R, 2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
inhibits in vitro
(1R,2R)-2-(N-tetradecanoylamino)-1-(4-nitrophenyl)-1,3-propanediol
(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
(1R,2R)-2-N-myristoylamino-1-(4-nitrophenyl)-1,3-propandiol
-
-
(1S, 2R)-D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
(1S,2R)-2-N-myristoylamino-1-phenyl-1-propanol
-
-
(1S,2R)-D-erythro-2-(N-myristoylamino)-1-phenyl-1-propanol
(2E,4E)-N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]hexa-2,4-dienamide
-
(E)-4-[(2S,3R)-N-1,3-dihydroxyoctadecan-2-ylamino]4-oxo-2-butenoic acid
-
(E)-N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]but-2-enamide
-
1-hexylcarbamoyl-5-fluorouracil
i.e. carmofur
12-amino-N-[(1R,2R)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]dodecanamide
-
1R,2R-(2-N-myristoylamino-1-(4-nitrophenyl)-1,3-dihydroxypropane)
-
-
1S,2S-(2-N-myristoylamino-1-(4-nitrophenyl)-1,3-dihydroxypropane)
-
-
2-bromo-N-[(2S,3R)-1,3-dihydroxynonadecan-2-yl]acetamide
-
2-bromo-N-[(2S,3R,4E)-1,3-dihydroxyoctadec-4-en-2-yl]acetamide
-
2-bromo-N-[(2S,3R,4Z)-1,3-dihydroxyoctadec-4-en-2-yl]acetamide
-
2-chloro-N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]acetamide
-
2-chloro-N-[(2S,3R,4Z)-1,3-dihydroxyoctadec-4-en-2-yl]acetamide
-
2-mercaptoethanol
-
2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
-
5-chloro-N-hexyl-2,4-dioxo-pyrimidine-1-carboxamide
-
5-trifluoromethyl-N-hexyl-2,4-dioxo-pyrimidine-1-carboxamide
-
6-(4-fluorophenyl)-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
-
6-bromo-2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
-
ACER2-specific siRNA
-
-
-
Bodipy-SOBRAC
-
Bodipy-SOCLAC
-
C6-urea-ceramide
an nCDase inhibitor
carmofur
Ceranib-1
-
i.e. 3-(3-(4-methoxyphenyl)acryloyl)-6-methyl-4-phenylquinolin-2(1H)-one
Ceranib-2
-
i.e. 3-[3-(4-methoxyphenyl)acryloyl]-4-phenyl-1H-quinolin-2-one
CHAPS
cholesterol
-
0.08 mM or below, decreases the hydrolysis of ceramide by a maximum of two-thirds
D-NMAPPD
-
-
desipramine
di-isopropyl fluorophosphate
the substrate protects against inhibition
dithiothreitol
-
glycodeoxycholate
LCL385
LCL521
a lysosomotropic prodrug inhibitor of acid ceramidase, inhibition in vivo leads to decreased cell viability
Mg2+
-
5 mM
Mn2+
-
5 mM
N-(2-hydroxy-2-phenylethyl)dodecane-1-sulfonamide
-
N-(2-hydroxy-2-phenylethyl)tetradecanamide
N-hexyl-2,4-dioxo-pyrimidine-1-carboxamide
-
N-hexyl-5-methyl-2,4-dioxo-pyrimidine-1-carboxamide
-
N-oleoylethanolamine
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-(4-methylphenyl)ethyl]tetradecanamide
-
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)-1,3-dihydroxyoctadecan-2-yl]3-methyl-2-butenamide.
-
N-[(2S)-2-hydroxy-2-(4-methylphenyl)ethyl]tetradecanamide
-
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
N-[(2S,3R)-1,3-dihydroxyoctadecan-2-yl]acrylamide
-
N-[(2S,3R,4E)-14-azido-1,3-dihydroxytetradec-4-en-2-yl]-2-bromoacetamide
-
N-[2-(4-butylphenyl)-2-hydroxyethyl]tetradecanamide
-
N-[2-(4-ethylphenyl)-2-hydroxyethyl]tetradecanamide
-
N-[2-(4-fluorophenyl)-2-hydroxyethyl]tetradecanamide
-
N-[2-(4-tert-butylphenyl)-2-hydroxyethyl]tetradecanamide
-
N-[2-hydroxy-2-(3-hydroxyphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(3-methoxyphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(3-methylphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(4-hydroxyphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(4-methoxyphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(4-methylphenyl)ethyl]dodecane-1-sulfonamide
-
N-[2-hydroxy-2-(4-methylphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(4-propylphenyl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(pyridin-3-yl)ethyl]-12-(1-methylhydrazinyl)dodecanamide
-
N-[2-hydroxy-2-(pyridin-3-yl)ethyl]dodecane-1-sulfonamide
-
N-[2-hydroxy-2-(pyridin-3-yl)ethyl]tetradecanamide
-
N-[2-hydroxy-2-(pyridin-4-yl)ethyl]dodecane-1-sulfonamide
-
N-[2-hydroxy-2-(pyridin-4-yl)ethyl]tetradecanamide
oleoylethanolamide
phorbol myristate acetate
-
phorbol myristate acetate, PMA, decreases the expression of ACER2 in HeLa cells
phosphatidylcholine
SABRAC
an acid ceramidase inhibitor
siRNA
-
-
-
taurocholate
taurodeoxycholate
Triton X-100
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
ceramide-1-phosphate
activates neutral ceramidase
N-(4-hydroxyphenyl)retinamide
increases isoform ACER2 activity and mRNA, but not isoforms ACER1 or ACER3
radiation
-
-
-
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
-
sphingosine-1-phosphate
activates neutral ceramidase
Zn2+
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.1338
C12:0-ceramide
-
pH 9.0, 37°C
0.1146
C14:0-ceramide
-
pH 9.0, 37°C
0.0985
C16:0-ceramide
-
pH 9.0, 37°C
0.0156
C18-ceramide
pH and temperature not specified in the publication
0.0948
C18:0-ceramide
-
pH 9.0, 37°C
0.0773
C18:1-ceramide
-
pH 9.0, 37°C
0.0915
C20:0-ceramide
-
pH 9.0, 37°C
0.0721
C20:1-ceramide
-
pH 9.0, 37°C
0.1432
C24:0-ceramide
-
pH 9.0, 37°C
0.2242
C6:0-ceramide
-
pH 9.0, 37°C
0.06
D-erythro-C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide
pH 7.5, 37°C, recombinant enzyme
0.0814
D-erythro-C24:1-ceramide
-
pH 9.0, 37°C
0.149 - 0.4132
N-lauroylsphingosine
0.01302
N-octanoylsphingosine
-
-
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
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
0.033
NBD-C12-ceramide
pH 7.0, 28°C, recombinant enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00049
C18-ceramide
pH and temperature not specified in the publication
0.7
NBD-C12-ceramide
pH 7.0, 28°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031
C18-ceramide
pH and temperature not specified in the publication
21.21
NBD-C12-ceramide
pH 7.0, 28°C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000064
2-oxo-N-(4-phenylbutyl)-1,3-benzoxazole-3(2H)-carboxamide
Homo sapiens
pH 7.4, 37°C
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
0.055
Ceranib-1
Homo sapiens
-
at 37°C, pH not specified in the publication
0.028
Ceranib-2
Homo sapiens
-
at 37°C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00593
-
-
0.0081
-
-
0.0338
-
pH 4.5, 37°C, recombinant AC expressed in CHO cells, hydrolysis of N-lauroylsphingosine
3.647
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7 - 4.2
-
-
3.8 - 4.3
-
-
4
assay at, substrate ceramide
5.5 - 6
-
ceramide synthesis reaction, distinct pH-optima for the degradative and synthetic reaction
6 - 8
-
-
6.8
-
synthesis of N-palmitoylsphingosine
7 - 9
neutral ceramidase
7.4
assay at
7.5 - 8.5
-
7.5 - 9
-
-
8
-
assay at
8.5 - 9.5
alkaline ceramidase
9.4
-
alkaline ceramidase, assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 4.6
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis, distribution of acid and alkaline isozymes, overview
Manually annotated by BRENDA team
of newborn
Manually annotated by BRENDA team
differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis
Manually annotated by BRENDA team
high expression level of CER2
Manually annotated by BRENDA team
-
bladder cancer cell line
Manually annotated by BRENDA team
-
high levels of acid ceramidase
Manually annotated by BRENDA team
alkaline ceramidase
Manually annotated by BRENDA team
a conjunctiva epithelial cell line
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
-
express only alkaline ceramidases
Manually annotated by BRENDA team
a significantly lower level of acid ceramidase expression was detected in gingival tissues from periodontal patients compared to those from healthy subjects
Manually annotated by BRENDA team
-
skin squamous cell carcinoma cells, express very low levels of ACER3
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
alkaline ceramidase
Manually annotated by BRENDA team
immortalized gingival epithelial cell line
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
high expression level of neutral ceramidase
Manually annotated by BRENDA team
alkaline ceramidase
Manually annotated by BRENDA team
-
head and neck cancer cell line
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
high expression level of neutral ceramidase
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane protein
Manually annotated by BRENDA team
-
ACER2 has 7 putative transmembrane domains, ACER2 membrane topology, overview. The N-terminal tail is necessary for both ACER2 activity and Golgi localization
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACER2_HUMAN
275
5
31309
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31300
theoretical value, Western blot analysis shows a molecular mass close to the predicted one
116000
13000
14000
1 * 14000 + 1 * 40000, SDS-PAGE
150000
-
gel filtration
28000
apparent molecular weight, deglycosylated beta subunit
31000
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
monomer
1 * 50000-55000, enzyme precursor , SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C362A
site-directed mutagenesis, inactive enzyme
D19G
site-directed mutagenesis, partial loss of catalytic activity
D331N
naturally occuring disease mutation, the mutation is predicted to affect the folding or stability of the protein
D352A
site-directed mutagenesis, inactive enzyme
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
E22G
site-directed mutagenesis, high loss of catalytic activity
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
N24G
site-directed mutagenesis, high loss of catalytic activity
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
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
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
resistant to trypsin digestion
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, several months, no significant loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4454fold
-
501fold
-
concanavalin A column chromatography, Blue Sepharose column chromatography, and Superose 12 gel filtration
-
recombinant AC expressed in CHO cells from the culture media, 58fold
-
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 enzyme from insect cells
recombinant enzyme partially from SF9 cells
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression analysis of isozymes during keratinocyte differentiation, expression levels in undifferentiated, early-stage and advanced-stage cells, and in whole epidermis by RT-PCR
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
acid ceramidase is expressed in Sf21 insect 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
-
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, genetic structure
expressed in CHO cells
-
expression in Saccharomyces cerevisiae enzyme-deficient doubleknockout strain.ypc1.ydc1 microsomes under control of the Gal1 promoter
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
-
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
-
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, quantitative RT-PCR enzyme expression analysis
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 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
overexpression in CHO cells
-
overexpression in CHO cells and in normal human skin fibroblasts
-
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
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 in Spodoptera frugiperda Sf9 cells
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 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 human ASAH1 promoter is cloned
-
transient expression of FLAG-tagged ACER3 in HSC-1 cells. ACER2 overexpression in HeLa cells, knockdown by RNA interference with ACER2-specific siRNA
-
transient overexpression of FLAG-tagged ACER3 in HSC-1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
A-375 cells are induced by doxycycline to overexpress the enzyme
acid ceramidase expression in gingival cells is suppressed by stimulation with Porphyromonas gingivalis in vitro
acid ceramidase is overexpressed in most prostate tumors
-
ACTH/cAMP signaling stimulates acid ceramidase ASAH1 transcription and activity
ACTH/cAMP signaling stimulates the enzyme transcription and activity
gemcitabine downregulates the neutral ceramidase
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
isoform ACER2 is upregulated in tumors
radiation-induced acid ceramidase upregulation confers resistance to taxane
-
significantly decreased ceramide levels are observed in human colon cancers, gliomas, ovarian cancers, thyroid and gastrointestinal cancers
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
pharmacology
enzyme inhibition may be beneficial in cancer therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levade, T.; Tempesta, M.C.; Moser, H.W.; Fensom, A.H.; Harzer, K.; Moser, A.B.; Salvayre, R.
Sulfatide and sphingomyelin loading of living cells as tools for the study of ceramide turnover by lysosomal ceramidase - implications for the diagnosis of Farber disease
Biochem. Mol. Med.
54
117-125
1995
Homo sapiens
Manually annotated by BRENDA team
Bernardo, K.; Hurwitz, R.; Zenk, T.; Desnick, R.J.; Ferlinz, K.; Schuchman, E.H.; Sandhoff, K.
Purification, characterization, and biosynthesis of human acid ceramidase
J. Biol. Chem.
270
11098-11102
1995
Homo sapiens
Manually annotated by BRENDA team
Linke, T.; Lansmann, S.; Sandhoff, K.
Purification of acid ceramidase from human pacenta
Methods Enzymol.
311
201-207
1999
Homo sapiens
Manually annotated by BRENDA team
Romiti, E.; Vasta, V.; Meacci, E.; Farnararo, M.; Linke, T.; Ferlinz, K.; Sandhoff, K.; Bruni, P.
Characterization of sphingomyelinase activity released by thrombin-stimulated platelets
Mol. Cell. Biochem.
205
75-81
2000
Homo sapiens
Manually annotated by BRENDA team
He, X.; Okino, N.; Dhami, R.; Dagan, A.; Gatt, S.; Schulze, H.; Sandhoff, K.; Schuchman, E.H.
Purification and characterization of recombinant, human acid ceramidase. Catalytic reactions and interactions with acid sphingomyelinase
J. Biol. Chem.
278
32978-32986
2003
Homo sapiens
Manually annotated by BRENDA team
Hwang, Y.H.; Tani, M.; Nakagawa, T.; Okino, N.; Ito, M.
Subcellular localization of human neutral ceramidase expressed in HEK293 cells
Biochem. Biophys. Res. Commun.
331
37-42
2005
Homo sapiens (Q9NR71), Homo sapiens
Manually annotated by BRENDA team
Galadari, S.; Wu, B.X.; Mao, C.; Roddy, P.; El Bawab, S.; Hannun, Y.A.
Identification of a novel amidase motif in neutral ceramidase
Biochem. J.
393
687-695
2006
no activity in Saccharomyces cerevisiae, Rattus norvegicus (Q91XT9), Homo sapiens (Q9NR71), Homo sapiens
Manually annotated by BRENDA team
Xu, R.; Jin, J.; Hu, W.; Sun, W.; Bielawski, J.; Szulc, Z.; Taha, T.; Obeid, L.M.; Mao, C.
Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P
FASEB J.
20
1813-1825
2006
Homo sapiens (Q5QJU3), Homo sapiens
Manually annotated by BRENDA team
Elojeimy, S.; Holman, D.H.; Liu, X.; El-Zawahry, A.; Villani, M.; Cheng, J.C.; Mahdy, A.; Zeidan, Y.; Bielwaska, A.; Hannun, Y.A.; Norris, J.S.
New insights on the use of desipramine as an inhibitor for acid ceramidase
FEBS Lett.
580
4751-4756
2006
Homo sapiens
Manually annotated by BRENDA team
Chavez, J.A.; Holland, W.L.; Baer, J.; Sandhoff, K.; Summers, S.A.
Acid ceramidase overexpression prevents the inhibitory effects of saturated fatty acids on insulin signaling
J. Biol. Chem.
280
20148-20153
2005
Homo sapiens
Manually annotated by BRENDA team
Monick, M.M.; Mallampalli, R.K.; Bradford, M.; McCoy, D.; Gross, T.J.; Flaherty, D.M.; Powers, L.S.; Cameron, K.; Kelly, S.; Merrill, A.H.; Hunninghake, G.W.
Cooperative prosurvival activity by ERK and Akt in human alveolar macrophages is dependent on high levels of acid ceramidase activity
J. Immunol.
173
123-135
2004
Homo sapiens
Manually annotated by BRENDA team
Houben, E.; Holleran, W.M.; Yaginuma, T.; Mao, C.; Obeid, L.M.; Rogiers, V.; Takagi, Y.; Elias, P.M.; Uchida, Y.
Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis
J. Lipid Res.
47
1063-1070
2006
Homo sapiens (Q5QJU3)
Manually annotated by BRENDA team
Duan, R.
Sphingomyelinase and ceramidase in the intestinal tract
Eur. J. Lipid Sci. Technol.
109
987-993
2007
Homo sapiens
-
Manually annotated by BRENDA team
Park, J.; Schuchman, E.H.
Acid ceramidase and human disease
Biochim. Biophys. Acta
1758
2133-2138
2006
Homo sapiens
Manually annotated by BRENDA team
Ohlsson, L.; Palmberg, C.; Duan, R.D.; Olsson, M.; Bergman, T.; Nilsson, A.
Purification and characterization of human intestinal neutral ceramidase
Biochimie
89
950-960
2007
Homo sapiens
Manually annotated by BRENDA team
Saad, A.F.; Meacham, W.D.; Bai, A.; Anelli, V.; Elojeimy, S.; Mahdy, A.E.; Turner, L.S.; Cheng, J.; Bielawska, A.; Bielawski, J.; Keane, T.E.; Obeid, L.M.; Hannun, Y.A.; Norris, J.S.; Liu, X.
The functional effects of acid ceramidase overexpression in prostate cancer progression and resistance to chemotherapy
Cancer Biol. Ther.
6
1455-1460
2007
Homo sapiens
Manually annotated by BRENDA team
Kim, H.L.; Satta, Y.
Population genetic analysis of the N-acylsphingosine amidohydrolase gene associated with mental activity in humans
Genetics
178
1505-1515
2008
Homo sapiens
Manually annotated by BRENDA team
Shtraizent, N.; Eliyahu, E.; Park, J.H.; He, X.; Shalgi, R.; Schuchman, E.H.
Autoproteolytic cleavage and activation of human acid ceramidase
J. Biol. Chem.
283
11253-11259
2008
Homo sapiens
Manually annotated by BRENDA team
Sun, W.; Xu, R.; Hu, W.; Jin, J.; Crellin, H.A.; Bielawski, J.; Szulc, Z.M.; Thiers, B.H.; Obeid, L.M.; Mao, C.
Upregulation of the human alkaline ceramidase 1 and acid ceramidase mediates calcium-induced differentiation of epidermal keratinocytes
J. Invest. Dermatol.
128
389-397
2008
Homo sapiens (Q13510), Homo sapiens (Q8TDN7), Homo sapiens
Manually annotated by BRENDA team
Mao, C.; Obeid, L.M.
Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate
Biochim. Biophys. Acta
1781
424-434
2008
Homo sapiens, Homo sapiens (Q5QJU3), Homo sapiens (Q8TDN7), Homo sapiens (Q9NR71), Homo sapiens (Q9NUN7), Mus musculus (Q8R4X1), Mus musculus (Q8VD53), Mus musculus (Q9D099), Mus musculus (Q9JHE3), Mus musculus (Q9WV54), Mus musculus
Manually annotated by BRENDA team
Lucki, N.; Sewer, M.B.
The cAMP-responsive element binding protein (CREB) regulates the expression of acid ceramidase (ASAH1) in H295R human adrenocortical cells
Biochim. Biophys. Acta
1791
706-713
2009
Homo sapiens
Manually annotated by BRENDA team
Sun, W.; Hu, W.; Xu, R.; Jin, J.; Szulc, Z.M.; Zhang, G.; Galadari, S.H.; Obeid, L.M.; Mao, C.
Alkaline ceramidase 2 regulates beta1 integrin maturation and cell adhesion
FASEB J.
23
656-666
2009
Homo sapiens
Manually annotated by BRENDA team
Mahdy, A.E.; Cheng, J.C.; Li, J.; Elojeimy, S.; Meacham, W.D.; Turner, L.S.; Bai, A.; Gault, C.R.; McPherson, A.S.; Garcia, N.; Beckham, T.H.; Saad, A.; Bielawska, A.; Bielawski, J.; Hannun, Y.A.; Keane, T.E.; Taha, M.I.; Hammouda, H.M.; Norris, J.S.; Liu, X.
Acid ceramidase upregulation in prostate cancer cells confers resistance to radiation: AC inhibition, a potential radiosensitizer
Mol. Ther.
17
430-438
2009
Homo sapiens
Manually annotated by BRENDA team
Claus, R.A.; Dorer, M.J.; Bunck, A.C.; Deigner, H.P.
Inhibition of sphingomyelin hydrolysis: targeting the lipid mediator ceramide as a key regulator of cellular fate
Curr. Med. Chem.
16
1978-2000
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, X.; Cheng, J.C.; Turner, L.S.; Elojeimy, S.; Beckham, T.H.; Bielawska, A.; Keane, T.E.; Hannun, Y.A.; Norris, J.S.
Acid ceramidase upregulation in prostate cancer: role in tumor development and implications for therapy
Expert Opin. Ther. Targets
13
1449-1458
2009
Homo sapiens
Manually annotated by BRENDA team
Eliyahu, E.; Shtraizent, N.; Martinuzzi, K.; Barritt, J.; He, X.; Wei, H.; Chaubal, S.; Copperman, A.B.; Schuchman, E.H.
Acid ceramidase improves the quality of oocytes and embryos and the outcome of in vitro fertilization
FASEB J.
24
1229-1238
2010
Homo sapiens
Manually annotated by BRENDA team
Xu, R.; Sun, W.; Jin, J.; Obeid, L.M.; Mao, C.
Role of alkaline ceramidases in the generation of sphingosine and its phosphate in erythrocytes
FASEB J.
24
2507-2515
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Mao, Z.; Sun, W.; Xu, R.; Novgorodov, S.; Szulc, Z.M.; Bielawski, J.; Obeid, L.M.; Mao, C.
Alkaline ceramidase 2 (ACER2) and its product dihydrosphingosine mediate the cytotoxicity of 4-HPR in tumor cells
J. Biol. Chem.
285
29087-29090
2010
Homo sapiens
Manually annotated by BRENDA team
Hu, W.; Xu, R.; Sun, W.; Szulc, Z.M.; Bielawski, J.; Obeid, L.M.; Mao, C.
Alkaline ceramidase 3 (ACER3) hydrolyzes unsaturated long-chain ceramides, and its down-regulation inhibits both cell proliferation and apoptosis
J. Biol. Chem.
285
7964-7976
2010
Homo sapiens
Manually annotated by BRENDA team
Sun, W.; Jin, J.; Xu, R.; Hu, W.; Szulc, Z.M.; Bielawski, J.; Obeid, L.M.; Mao, C.
Substrate specificity, membrane topology, and activity regulation of human alkaline ceramidase 2 (ACER2)
J. Biol. Chem.
285
8995-9007
2010
Homo sapiens
Manually annotated by BRENDA team
ONeill, S.M.; Houck, K.L.; Yun, J.K.; Fox, T.E.; Kester, M.
AP-1 binding transcriptionally regulates human neutral ceramidase
Arch. Biochem. Biophys.
511
31-39
2011
Homo sapiens
Manually annotated by BRENDA team
Canals, D.; Perry, D.M.; Jenkins, R.W.; Hannun, Y.A.
Drug targeting of sphingolipid metabolism: sphingomyelinases and ceramidases
Br. J. Pharmacol.
163
694-712
2011
Homo sapiens, Homo sapiens (Q13510), Homo sapiens (Q8TDN7), Homo sapiens (Q9NR71)
Manually annotated by BRENDA team
Park, J.; Yoon, S.
Ceramide, a crucial functional lipid, and its metabolic regulation by acid ceramidase
Food Sci. Biotechnol.
19
859-864
2010
Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Beckham, T.H.; Lu, P.; Cheng, J.C.; Zhao, D.; Turner, L.S.; Zhang, X.; Hoffman, S.; Armeson, K.E.; Liu, A.; Marrison, T.; Hannun, Y.A.; Liu, X.
Acid ceramidase-mediated production of sphingosine 1-phosphate promotes prostate cancer invasion through upregulation of cathepsin B
Int. J. Cancer
131
2034-2043
2012
Homo sapiens
Manually annotated by BRENDA team
Jenkins, R.W.; Clarke, C.J.; Canals, D.; Snider, A.J.; Gault, C.R.; Heffernan-Stroud, L.; Wu, B.X.; Simbari, F.; Roddy, P.; Kitatani, K.; Obeid, L.M.; Hannun, Y.A.
Regulation of CC ligand 5/RANTES by acid sphingomyelinase and acid ceramidase
J. Biol. Chem.
286
13292-13303
2011
Homo sapiens
Manually annotated by BRENDA team
Draper, J.M.; Xia, Z.; Smith, R.A.; Zhuang, Y.; Wang, W.; Smith, C.D.
Discovery and evaluation of inhibitors of human ceramidase
Mol. Cancer Ther.
10
2052-2061
2011
Homo sapiens
Manually annotated by BRENDA team
Lucki, N.C.; Bandyopadhyay, S.; Wang, E.; Merrill, A.H.; Sewer, M.B.
Acid ceramidase (ASAH1) is a global regulator of steroidogenic capacity and adrenocortical gene expression
Mol. Endocrinol.
26
228-243
2012
Homo sapiens, Homo sapiens (Q13510)
Manually annotated by BRENDA team
Pizzirani, D.; Bach, A.; Realini, N.; Armirotti, A.; Mengatto, L.; Bauer, I.; Girotto, S.; Pagliuca, C.; De Vivo, M.; Summa, M.; Ribeiro, A.; Piomelli, D.
Benzoxazolone carboxamides: potent and systemically active inhibitors of intracellular acid ceramidase
Angew. Chem. Int. Ed. Engl.
54
485-489
2015
Homo sapiens (Q13510), Mus musculus (Q9WV54)
Manually annotated by BRENDA team
Morad, S.; Levin, J.; Tan, S.; Fox, T.; Feith, D.; Cabot, M.
Novel off-target effect of tamoxifen - inhibition of acid ceramidase activity in cancer cells
Biochim. Biophys. Acta
1831
1657-1664
2013
Homo sapiens (Q13510)
Manually annotated by BRENDA team
Ito, M.; Okino, N.; Tani, M.
New insight into the structure, reaction mechanism, and biological functions of neutral ceramidase
Biochim. Biophys. Acta
1841
682-691
2014
Dictyostelium discoideum, Mycobacterium tuberculosis, Oryza sativa, Pseudomonas aeruginosa, Tribolium castaneum, Dermatophilus congolensis, Triticum aestivum (A9YFM2), Aspergillus oryzae (Q5B5D5), Danio rerio (Q5W7F1), Rattus norvegicus (Q91XT9), Mus musculus (Q9JHE3), Homo sapiens (Q9NR71), Drosophila melanogaster (Q9VA70), Laodelphax striatellus (R4N4U2)
Manually annotated by BRENDA team
Bhabak, K.; Proksch, D.; Redmer, S.; Arenz, C.
Novel fluorescent ceramide derivatives for probing ceramidase substrate specificity
Bioorg. Med. Chem.
20
6154-6161
2012
Homo sapiens (Q13510), Homo sapiens (Q9NR71)
Manually annotated by BRENDA team
Bhabak, K.; Arenz, C.
Novel amide- and sulfonamide-based aromatic ethanolamines: Effects of various substituents on the inhibition of acid and neutral ceramidases
Bioorg. Med. Chem.
20
6162-6170
2012
Homo sapiens (Q13510), Homo sapiens (Q9NR71)
Manually annotated by BRENDA team
Bhabak, K.P.; Kleuser, B.; Huwiler, A.; Arenz, C.
Effective inhibition of acid and neutral ceramidases by novel B-13 and LCL-464 analogues
Bioorg. Med. Chem.
21
874-882
2013
Homo sapiens (Q13510), Homo sapiens (Q9NR71)
Manually annotated by BRENDA team
Bhabak, K.P.; Hauser, A.; Redmer, S.; Banhart, S.; Heuer, D.; Arenz, C.
Development of a novel FRET probe for the real-time determination of ceramidase activity
ChemBioChem
14
1049-1052
2013
Homo sapiens (Q9NR71), Mus musculus (Q9WV54)
Manually annotated by BRENDA team
Cheng, J.; Bai, A.; Beckham, T.; Tucker Marrison, S.; Yount, C.; Young, K.; Lu, P.; Bartlett, A.; Wu, B.; Keane, B.; Armeson, K.; Marshall, D.; Keane, T.; Smith, M.; Ellen Jones, E.; Drake Jr., R.; Bielawska, A.; Norris, J.; Liu, X.
Radiation-induced acid ceramidase confers prostate cancer resistance and tumor relapse
J. Clin. Invest.
123
4344-4358
2013
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Camacho, L.; Meca-Cortes, O.; Abad, J.L.; Garcia, S.; Rubio, N.; Diaz, A.; Celia-Terrassa, T.; Cingolani, F.; Bermudo, R.; Fernandez, P.L.; Blanco, J.; Delgado, A.; Casas, J.; Fabrias, G.; Thomson, T.M.
Acid ceramidase as a therapeutic target in metastatic prostate cancer
J. Lipid Res.
54
1207-1220
2013
Homo sapiens (Q13510)
Manually annotated by BRENDA team
Lucki, N.C.; Li, D.; Bandyopadhyay, S.; Wang, E.; Merrill, A.H.; Sewer, M.B.
Acid ceramidase (ASAH1) represses steroidogenic factor 1-dependent gene transcription in H295R human adrenocortical cells by binding to the receptor
Mol. Cell. Biol.
32
4419-4431
2012
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Alves, M.; Trionnaire, E.; Ribeiro, I.; Carpentier, S.; Harzer, K.; Levade, T.; Ribeiro, M.
Molecular basis of acid ceramidase deficiency in a neonatal form of Farber disease: identification of the first large deletion in ASAH1 gene
Mol. Genet. Metab.
109
276-281
2013
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Beckham, T.H.; Cheng, J.C.; Lu, P.; Marrison, S.T.; Norris, J.S.; Liu, X.
Acid ceramidase promotes nuclear export of PTEN through sphingosine 1-phosphate mediated Akt signaling
PLoS ONE
8
e76593
2013
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Realini, N.; Solorzano, C.; Pagliuca, C.; Pizzirani, D.; Armirotti, A.; Luciani, R.; Costi, M.P.; Bandiera, T.; Piomelli, D.
Discovery of highly potent acid ceramidase inhibitors with in vitro tumor chemosensitizing activity
Sci. Rep.
3
1035
2013
Homo sapiens (Q13510), Homo sapiens, Rattus norvegicus (Q6P7S1)
Manually annotated by BRENDA team
Coant, N.; Hannun, Y.A.
Neutral ceramidase advances in mechanisms, cell regulation, and roles in cancer
Adv. Biol. Regul.
71
141-146
2019
Nilaparvata lugens, Amorphophallus muelleri (A0A2D1WBF2), Rattus norvegicus (Q91XT9), Mus musculus (Q9JHE3), Homo sapiens (Q9NR71)
Manually annotated by BRENDA team
Azuma, M.M.; Balani, P.; Boisvert, H.; Gil, M.; Egashira, K.; Yamaguchi, T.; Hasturk, H.; Duncan, M.; Kawai, T.; Movila, A.
Endogenous acid ceramidase protects epithelial cells from Porphyromonas gingivalis-induced inflammation in vitro
Biochem. Biophys. Res. Commun.
495
2383-2389
2018
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Bai, A.; Bielawska, A.; Rahmaniyan, M.; Kraveka, J.M.; Bielawski, J.; Hannun, Y.A.
Dose dependent actions of LCL521 on acid ceramidase and key sphingolipid metabolites
Bioorg. Med. Chem.
26
6067-6075
2018
Homo sapiens (Q13510)
Manually annotated by BRENDA team
Baduva, K.; Buechter, L.; Kreyenkamp, K.; Westphal, L.; Wilker, B.; Kohnen, M.; Schuchman, E.H.; Edwards, M.J.; Becker, K.A.; Gulbins, E.; Carpinteiro, A.
Signalling effects induced by acid ceramidase in human epithelial or leukemic cell lines
Cell. Physiol. Biochem.
52
1092-1102
2019
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Ferraz, M.J.; Marques, A.R.; Appelman, M.D.; Verhoek, M.; Strijland, A.; Mirzaian, M.; Scheij, S.; Ouairy, C.M.; Lahav, D.; Wisse, P.; Overkleeft, H.S.; Boot, R.G.; Aerts, J.M.
Lysosomal glycosphingolipid catabolism by acid ceramidase formation of glycosphingoid bases during deficiency of glycosidases
FEBS Lett.
590
716-725
2016
Homo sapiens (Q13510), Homo sapiens, Mus musculus (Q9WV54)
Manually annotated by BRENDA team
Ordonez, Y.F.; Abad, J.L.; Aseeri, M.; Casas, J.; Garcia, V.; Casasampere, M.; Schuchman, E.H.; Levade, T.; Delgado, A.; Triola, G.; Fabrias, G.
Activity-based imaging of acid ceramidase in living cells
J. Am. Chem. Soc.
141
7736-7742
2019
Homo sapiens (Q13510)
Manually annotated by BRENDA team
Sakamoto, W.; Coant, N.; Canals, D.; Obeid, L.M.; Hannun, Y.A.
Functions of neutral ceramidase in the Golgi apparatus
J. Lipid Res.
59
2116-2125
2018
Homo sapiens (Q9NR71)
Manually annotated by BRENDA team
Tan, S.F.; Dunton, W.; Liu, X.; Fox, T.E.; Morad, S.A.F.; Desai, D.; Doi, K.; Conaway, M.R.; Amin, S.; Claxton, D.F.; Wang, H.G.; Kester, M.; Cabot, M.C.; Feith, D.J.; Loughran, T.P.
Acid ceramidase promotes drug resistance in acute myeloid leukemia through NF-kappaB-dependent P-glycoprotein upregulation
J. Lipid Res.
60
1078-1086
2019
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Gebai, A.; Gorelik, A.; Li, Z.; Illes, K.; Nagar, B.
Structural basis for the activation of acid ceramidase
Nat. Commun.
9
1621
2018
Homo sapiens (Q9NUN7)
Manually annotated by BRENDA team
Vasiliauskaite-Brooks, I.; Healey, R.D.; Rochaix, P.; Saint-Paul, J.; Sounier, R.; Grison, C.; Waltrich-Augusto, T.; Fortier, M.; Hoh, F.; Saied, E.M.; Arenz, C.; Basu, S.; Leyrat, C.; Granier, S.
Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
Nat. Commun.
9
5437
2018
Homo sapiens (Q9NUN7), Homo sapiens
Manually annotated by BRENDA team
Vasiliauskaite-Brooks, I.; Sounier, R.; Rochaix, P.; Bellot, G.; Fortier, M.; Hoh, F.; De Colibus, L.; Bechara, C.; Saied, E.M.; Arenz, C.; Leyrat, C.; Granier, S.
Structural insights into adiponectin receptors suggest ceramidase activity
Nature
544
120-123
2017
Homo sapiens (Q86V24)
Manually annotated by BRENDA team
Leclerc, J.; Garandeau, D.; Pandiani, C.; Gaudel, C.; Bille, K.; Nottet, N.; Garcia, V.; Colosetti, P.; Pagnotta, S.; Bahadoran, P.; Tondeur, G.; Mograbi, B.; Dalle, S.; Caramel, J.; Levade, T.; Ballotti, R.; Andrieu-Abadie, N.; Bertolotto, C.
Lysosomal acid ceramidase ASAH1 controls the transition between invasive and proliferative phenotype in melanoma cells
Oncogene
38
1282-1295
2019
Homo sapiens (Q13510), Homo sapiens
Manually annotated by BRENDA team
Doan, N.B.; Nguyen, H.S.; Al-Gizawiy, M.M.; Mueller, W.M.; Sabbadini, R.A.; Rand, S.D.; Connelly, J.M.; Chitambar, C.R.; Schmainda, K.M.; Mirza, S.P.
Acid ceramidase confers radioresistance to glioblastoma cells
Oncol. Rep.
38
1932-1940
2017
Homo sapiens (Q13510)
Manually annotated by BRENDA team
Malinina, L.; Brown, R.E.
Catalytic mechanism of eukaryotic neutral ceramidase
Structure
23
1371-1372
2015
Homo sapiens (Q9NR71), Homo sapiens
Manually annotated by BRENDA team
Airola, M.V.; Allen, W.J.; Pulkoski-Gross, M.J.; Obeid, L.M.; Rizzo, R.C.; Hannun, Y.A.
Structural basis for ceramide recognition and hydrolysis by human neutral ceramidase
Structure
23
1482-1491
2015
Homo sapiens (Q9NR71), Homo sapiens
Manually annotated by BRENDA team