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Information on EC 3.1.4.12 - sphingomyelin phosphodiesterase and Organism(s) Homo sapiens and UniProt Accession Q9NXE4

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.12 sphingomyelin phosphodiesterase
IUBMB Comments
Has very little activity on phosphatidylcholine.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9NXE4
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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
Synonyms
sphingomyelinase, alpha-toxin, acid sphingomyelinase, smase, neutral sphingomyelinase, asmase, nsmase2, nsmase, n-smase, smpd1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
neutral sphingomyelinase-3
-
acid sphingomyelinase
acid spingomyelinase
-
-
acidic SMase
-
-
acidic sphingomyelinase
-
-
alk-SMase
alkaline SMase
-
-
alkaline sphingomyelinase
aSMase
Beta-hemolysin
-
-
-
-
Beta-toxin
-
-
-
-
hnSMase
-
-
hSMase
-
-
intestinal alkaline sphingomyelinase
-
-
Lyso-PAF-PLC
-
-
-
-
magnesium-dependent neutral sphingomyelinase
-
-
N-SMase
N-SMase2
-
-
neutral SMase
-
-
neutral sphingomyelinase
neutral sphingomyelinase 2
neutral sphingomyelinase-1
-
-
neutral sphingomyelinase-2
-
-
neutral sphingomyelinase-3
-
-
neutral sphingomylinase 2
-
nSMase
nSMase-1
-
-
nSMase1
nSMase2
nSMase3
-
-
phosphodiesterase, sphingomyelin
-
-
-
-
rhASM
-
-
S-SMase
-
-
secretory sphingomyelinase
-
-
SKNY
-
-
SMase
SMPD-1
-
-
SMPD1
Smpd3
-
-
SMPLC
-
-
-
-
sphingomyelin phosphodiesterase
-
-
-
-
sphingomyelin phosphodiesterase 1
sphingomyelin phosphodiesterase like 3a
-
sphingomyelin phosphodiesterase-1
-
-
sphingomyelinase
sphingomyelinase C
-
-
-
-
additional information
-
alk-SMase is a member of the NPP, i.e. nucleotide diphosphatase/phosphodiesterase, family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a sphingomyelin + H2O = a ceramide + phosphocholine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
sphingomyelin cholinephosphohydrolase
Has very little activity on phosphatidylcholine.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-54-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
show the reaction diagram
-
-
-
?
2-(N-hexadecanoylamino)-4-nitrophenylphosphorylcholine + H2O
2-(N-hexadecanoylamino)-4-nitrophenol + choline phosphate
show the reaction diagram
-
-
-
?
2-n-hexadecanoylamino-4-nitrophenylphosphorylcholine + H2O
2-n-hexadecanoylamino-4-nitrophenol + choline phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
show the reaction diagram
-
-
-
?
6-hexadecanoylamino-4-methylumbelliferyl-phosphocholine + H2O
6-hexadecanoylamino-4-methylumbelliferone + choline phosphate
show the reaction diagram
-
-
-
-
?
6-hexadecanoylamino-4-methylumbelliferyl-phosphorylcholine + H2O
6-hexadecanoylamino-4-methylumbelliferone + choline phosphate
show the reaction diagram
-
-
-
-
?
6-hexadecanoylamino-4-methylumbelliferyl-phosphorylcholine + H2O
6-hexadecanoylamino-4-methylumbelliferone + phosphorylcholine
show the reaction diagram
-
-
-
-
?
a sphingomyelin + H2O
a ceramide + choline phosphate
show the reaction diagram
-
-
-
-
?
a sphingomyelin + H2O
a ceramide + phosphocholine
show the reaction diagram
ADP + H2O
?
show the reaction diagram
-
-
-
?
ADP-ribose + H2O
?
show the reaction diagram
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
?
bis(4-methylumbelliferyl)-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
bis(4-nitrophenyl)phosphate + H2O
?
show the reaction diagram
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
BODIPY FL C12-sphingomyelin + H2O
BODIPY FL C12-ceramide + phosphocholine
show the reaction diagram
-
-
-
-
?
CDP-choline + H2O
CMP + phosphocholine
show the reaction diagram
-
-
-
?
CDP-ethanolamine + H2O
CMP + phosphoethanolamine
show the reaction diagram
-
-
-
?
choline-methyl-sphingomyelin + H2O
?
show the reaction diagram
-
-
-
-
?
hexadecanoyl-p-nitrophenylphosphorylcholine + H2O
hexadecanoyl-p-nitrophenol + choline phosphate
show the reaction diagram
-
-
-
-
?
lissamine-rhodamine dodecanoyl sphingosyl phosphocholine + H2O
?
show the reaction diagram
-
neutral sphingomyelinase
-
-
?
lyso-platelet-activating factor + H2O
1-alkylglycerol + choline phosphate
show the reaction diagram
-
103fold higher activity than with sphingomyelin in the absence of detergent
-
?
lyso-platelet-activating factor + H2O
alkylglycerol + choline phosphate
show the reaction diagram
-
55% of activity with sphingomyelin in the absence of detergent
-
?
lysophosphatidylcholine + H2O
acylglycerol + choline phosphate
show the reaction diagram
N-methylsphingomyelin + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
diacylglycerol + choline phosphate
show the reaction diagram
phosphatidylethanolamine + H2O
diacylglycerol + phosphorylethanolamine
show the reaction diagram
-
in the presence of 0.08% sodium taurodeoxycholate
-
-
?
phosphatidylglycerol + H2O
diacylglycerol + glycerolphosphate
show the reaction diagram
platelet-activating factor + H2O
1-O-alkyl-2-acetyl-sn-glycerol + choline phosphate
show the reaction diagram
platelet-inactivating factor + H2O
1-O-alkyl-2-acetyl-sn-glycerol + choline phosphate + ?
show the reaction diagram
sphingomyelin + H2O
ceramide + phosphocholine
show the reaction diagram
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
show the reaction diagram
sphingosylphosphocholine + H2O
sphingosine + choline phosphate
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
a sphingomyelin + H2O
a ceramide + choline phosphate
show the reaction diagram
-
-
-
-
?
a sphingomyelin + H2O
a ceramide + phosphocholine
show the reaction diagram
platelet-activating factor + H2O
1-O-alkyl-2-acetyl-sn-glycerol + choline phosphate
show the reaction diagram
-
the enzyme cleaves the phosphocholine head group from platelet-activating factor. Potential protective effect of the enzyme against inflammatory bowel disease and colon cancer
-
-
?
platelet-inactivating factor + H2O
1-O-alkyl-2-acetyl-sn-glycerol + choline phosphate + ?
show the reaction diagram
-
alk-SMase hydrolyses and inactivates platelet-activating factor by a phospholipase C activity, alk-SMase cleaves the phosphocholine head group from PAF and generates 1-O-alkyl-2-acetyl-sn-glycerol
-
-
?
sphingomyelin + H2O
ceramide + phosphocholine
show the reaction diagram
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
5 mM, stimulates
Mn2+
5 mM, stimulates
Cu2+
-
6fold increase in activity at 0.1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
scyphostatin
-
(1-aminodecane-1,1-diyl)bis(phosphonic acid)
-
a substrate analogue inhibitor of aSMase
1,10-phenanthroline
-
-
2'-AMP
-
mixture with 3'-AMP
27-Hydroxycholesterol
3',5'-cAMP
-
IC50: above 0.5 mM
3'-AMP
-
mixture with 2'-AMP
3-acetyl-11-keto-beta-boswellic acid
-
62% inhibition of acid SMase at 0.1 mM
3-O-methylsphingomyelin
-
-
3-[(3-cholamidopropyl)dimethyl-ammonio]-1-propanesulfonate
3-[benzyl(tert-butyl)amino]-1-(4-nitrophenyl)propan-1-one
-
-
5'-AMP
-
-
5-adenoylimino phosphate
-
IC50: above 0.5 mM
AD2765
-
a substrate analogue inhibitor of aSMase
adenine-9-beta-D-arabinofuranoside 5'-monophosphate
-
-
adeno 5'-diphosphate
-
IC50: above 0.5 mM
adeno-2',3'-cyclic phospho 5'-monophosphate
-
IC50: 0.2 mM
adeno-2',3'-cyclic phospho 5'-phosphosulfate
-
IC50: 0.5 mM
adenosine 3',5'-diphosphate
-
-
adenosine 5'-monophosphate
-
periodate-oxidized and an isomer with arabinose instead of ribose as sugar component
Adenosine 5'-O-thiomonosulfate
-
-
adenosine 5'-phosphosulfate
-
-
ADP
-
IC50: 0.3 mM
alpha-mangostin
-
a xanthone from the bark of Garcinia speciosa
amitriptyline
amlodipine
-
-
AMP
-
IC50: 0.08 mM, non-competitive inhibition
astemizole
-
-
ATP
-
IC50: 0.8 mM
benztropine
-
-
bepridil
-
-
Brij 56
-
-
C11AG
-
inhibits N-SMases in T-cells and macrophages
Ca2+
-
slight
camylofin
-
-
Cetylpyridinium chloride
-
-
CHAPS
-
CHAPS and Triton X-100 that are commonly used in acid and neutral SMase assays, do not stimulate but rather strongly inhibit the bile salt-induced activation of Alk-SMase
chlorprothixene
-
-
cholate
-
-
clomiphene
-
-
cloperastine
-
-
cowanin
-
a xanthone from the bark of Garcinia speciosa
cowanol
-
a xanthone from the bark of Garcinia speciosa
curcumin
-
inhibits acid SMase, but not neutral and alkaline SMase, in Caco-2 cells with an antiproliferative effect, the effect is more potent in monolayers than in polarised cells, metabolis effects, overview
cyclobenzaprine
-
-
cyproheptadine
-
-
D609
-
nonspecific sphingomyelinase inhibitor
desipramine
dichloroisocoumarin
-
-
dithioerythritol
-
-
dithiothreitol
-
-
doxepine
-
-
drofenine
-
-
ES048
-
when tested in splenocyte extracts, ES048 specifically inhibits enzyme activity up to a concentration of 0.002 mM
Fe3+
-
-
fendiline
-
-
fluoxetine
-
-
fluphenazine
-
-
glutathione
-
-
GW4869
imipramine
L-carnitine
-
specific inhibitor
lysophosphatidic acid
-
IC50: 0.04 mM
mannose 6-phosphate
-
Niemann-Pick disease fibroblasts
manumycin A
-
-
maprotiline
-
-
Mn2+
-
above 0.5 mM
N-tosyl-L-phenylalanyl chloromethyl ketone
-
-
NAD+
-
IC50: above 0.5 mM
NADP+
-
IC50: above 0.5 mM
norfluoxetine
-
-
nortriptyline
-
-
oxidized glutathione
reversible inhibition of nSMase1
paroxetine
-
-
peroxynitrite
irreversible inhibition of nSMase1
phosphate
phosphatidyl inositol-3,5-bisphosphate
-
-
phosphatidyl-myo-inositol 3,4,5-triphosphate
-
IC50: 0.003 mM
phosphatidyl-myo-inositol 4,5-diphosphate
-
IC50: 0.25 mM
phosphatidylcholine
-
IC50: 2 mM
phosphatidylinositol
-
-
phosphatidylinositol 4',5'-bisphosphate
-
-
phosphatidylinositol-4,5-bisphosphate
-
-
phosphorylcholine
-
-
pimethixene
-
-
platelet-inactivating factor
-
competitive inhibition of sphingomyelin hydrolysis
-
promazine
-
-
Promethazine
-
-
pronase E
-
reduction of stimulation of the two activator proteins
-
protriptyline
-
-
reactive oxygen species
reversible inhibition of nSMase1
-
scyphostatin
-
isolated from Discomycetes, specifically inhibits N-SMases
sertraline
-
-
sphingomyelin
-
strong competitive inhibition of platelet-inactivating factor hydrolysis
sphingosylphosphocholine
-
-
SR33557
-
the calcium channel inhibitor performs indirect inhibition of aSMase
suloctidil
-
-
sulphydryl reagents
-
-
terfenadine
-
-
triflupromazine
-
-
Triton X-100
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidylserine
enhances activity
Activator proteins
-
from human spleen, two forms of
-
albumin
-
20% activation of enzyme A and B
-
arachidonic acid
-
approx. 3fold activation at 0.5 mM
bile salt
-
dependent on, particularly taurocholate and taurochenodeoxycholate
ceramide
-
-
cholate
-
-
Cutsum
-
-
-
daunorubicin
-
-
deoxycholate
-
-
Detergents
-
-
Diacylglycerols
-
-
dioleoyl-phosphatidylserine
0.05 mM, 4fold activation
galectin-I
-
human, induces apoptosis and initiates the acid SMase-mediated release of ceramide
-
glycocholate
-
-
H2O2
-
reactive oxygen species, e.g. hydrogen peroxide, specifically activate neutral sphingomyelinase 2 to generate ceramide and induce apoptosis in airway epithelial cells, overview
Lipids
-
saturated and unsaturated fatty acids
-
monoacylglycerols
-
-
ONOO-
-
peroxynitrite specifically activates the acidic sphingomyelinase
phorbol 12-myristate 13-acetate/protein kinase Cdelta
-
activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation, which is mediated by phorbol 12-myristate 13-acetate, that induces also membrane translocation of ASMase, formation of a novel PKCdelta-ASMase complex after PMA stimulation, mechanism, overview
-
phosphatidic acid
-
-
phosphatidylethanol
0.05 mM, 2fold activation
phosphatidylglycerol
activates nSMase2
phosphatidylinositol
-
-
phosphatidylserine
protein kinase C-zeta
-
mediates the activation of N-SMase by 1,25-dihydroxyvitamin D3, while protein kinase C-delta inhibits the activation
-
salts
-
trihydroxy- and dihydroxy-bile salt
-
saposin C
-
presence of sphingolipid activator proteins, e. g. saponsins, is not essential for activity. Saposin C increases activity of the P153A mutant enzyme, but does not result in complete restoration of the activity
-
staurosporine
-
activates neutral spingomyelinase in a multiphasic manner
taurochenodeoxycholate
-
-
taurocholate
taurodeoxycholate
-
the enzyme activity is specifically stimulated by about 2.5 mM taurodeoxycholate
TNF-alpha
-
increases N-SMase activity rapidly and transiently both endogenously and in cells overexpressing nSMase2, and induces membrane translocation of nSMase2, regulated by p38-alpha MAPK, the increase in endogenous N-SMase activity is abrogated by p38 MAPK inhibition
-
TNFalpha
-
S-SMase cytokine TNFalpha activation, completely abrogated by desipramine, overview
-
triacylglycerols
-
-
Tripalmitoylglycerol
-
-
Triton X-100
tumor necrosis factor
-
induces N-SMase activity
-
tumor necrosis factor-alpha
-
activates neutral spingomyelinase in a multiphasic manner
-
Tween 20
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01871
sphingomyelin
-
1.7
2-(N-hexadecanoylamino)-4-nitrophenylphosphorylcholine
-
37°C, pH 5.5
0.34
2-n-hexadecanoylamino-4-nitrophenylphosphorylcholine
-
-
0.306
ADP
at pH 5.0 and 37°C
0.348
ADP-ribose
at pH 5.0 and 37°C
0.327
ATP
at pH 5.0 and 37°C
14.5
bis-p-nitrophenyl phosphate
-
-
0.262
CDP-choline
at pH 5.0 and 37°C
0.391
CDP-ethanolamine
at pH 5.0 and 37°C
0.024 - 0.526
sphingomyelin
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.374
ADP
at pH 5.0 and 37°C
2.07
ADP-ribose
at pH 5.0 and 37°C
0.7357
ATP
at pH 5.0 and 37°C
1.29
CDP-choline
at pH 5.0 and 37°C
1.864
CDP-ethanolamine
at pH 5.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.23
ADP
at pH 5.0 and 37°C
5.96
ADP-ribose
at pH 5.0 and 37°C
2.26
ATP
at pH 5.0 and 37°C
4.89
CDP-choline
at pH 5.0 and 37°C
5.71
CDP-ethanolamine
at pH 5.0 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
3',5'-cAMP
Homo sapiens
-
IC50: above 0.5 mM
0.05
3-acetyl-11-keto-beta-boswellic acid
Homo sapiens
-
acid SMase
0.5
5-adenoylimino phosphate
Homo sapiens
-
IC50: above 0.5 mM
0.07
AD2765
Homo sapiens
-
pH and temperature not specified in the publication
0.5
adeno 5'-diphosphate
Homo sapiens
-
IC50: above 0.5 mM
0.2
adeno-2',3'-cyclic phospho 5'-monophosphate
Homo sapiens
-
IC50: 0.2 mM
0.5
adeno-2',3'-cyclic phospho 5'-phosphosulfate
Homo sapiens
-
IC50: 0.5 mM
0.3
ADP
Homo sapiens
-
IC50: 0.3 mM
0.014
alpha-mangostin
Homo sapiens
-
pH and temperature not specified in the publication
0.08
AMP
Homo sapiens
-
IC50: 0.08 mM, non-competitive inhibition
0.8
ATP
Homo sapiens
-
IC50: 0.8 mM
0.0192
cowanin
Homo sapiens
-
pH and temperature not specified in the publication
0.0109
cowanol
Homo sapiens
-
pH and temperature not specified in the publication
0.04
lysophosphatidic acid
Homo sapiens
-
IC50: 0.04 mM
0.5
NAD+
Homo sapiens
-
IC50: above 0.5 mM
0.5
NADP+
Homo sapiens
-
IC50: above 0.5 mM
10
phosphate
Homo sapiens
-
IC50: 10 mM, non-competitive inhibition
0.003
phosphatidyl-myo-inositol 3,4,5-triphosphate
Homo sapiens
-
IC50: 0.003 mM
0.25
phosphatidyl-myo-inositol 4,5-diphosphate
Homo sapiens
-
IC50: 0.25 mM
2
phosphatidylcholine
Homo sapiens
-
IC50: 2 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.007
alkaline sphingomyelinase in liver with steatosis
0.027
-
recombinant human Alk-SMase, in 50 mM Tris
0.047
alkaline sphingomyelinase in liver with sclerosing cholangitis
13.3
-
recombinant haSMase
21.1
-
-
7.33
-
-
92.8
-
5fold higher specific activity of rhASM purified from CHO cell-harvests stored at -20°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5
-
-
4.5 - 5
-
-
4.6 - 4.7
-
-
4.8 - 5
-
bis-4-methylumbelliferyl phosphate and bis-p-nitrophenyl phosphate
5 - 5.5
-
hexadecanoyl-p-nitrophenyl phosphorylcholine
5.2
-
in sodium acetate buffer
5.5 - 7.5
assay at
7
-
neutral SMase assay at
additional information
-
acidic pH optimum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6.5
4.5 - 9
approx. 5% of maximal activity at pH 4.5, approx. 15% of maximal activity at pH 9.0
5 - 10
-
-
6 - 10.5
-
-
7 - 10
-
the activity of Alk-SMase expressed from the yeast has a similar pH dependency, being low at acid pH, increasing after 7 and optimal at 9.0
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
up to
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cortical astrocyte, acid SMase
Manually annotated by BRENDA team
-
a secreted, zinc-activated form of ASM is found in the plasma which plays an important role in the development of atherosclerosis
Manually annotated by BRENDA team
-
cerebrospinal fluid contains a detectable level of secretory enzyme, which is unrelated to serum enzyme activity, no influence of sex or age on enzyme activity in cerebrospinal fluid
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
the enzyme is down regulated in human long-standing ulcerative colitis and colonic adenocarcinoma
Manually annotated by BRENDA team
high mRNA levels
Manually annotated by BRENDA team
-
patients with atopic dermatitis show reduced activities of acid and neutral sphingomyelinase. The reduced acid sphingomyelinase activity may be partially responsible for the reduced content of stratum corneum ceramides. Reduced neutral sphingomyelinase activity may lead to changes in signal transduction, thereby regulating differentiation. The resulting reduction in involucrin could cause the reduced number of covalently bound ceramides in atopic dermatitis
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
bronchial epithelial cell line
Manually annotated by BRENDA team
-
a Jurkat cell line derivative lacking caspase 8
Manually annotated by BRENDA team
low mRNA levels
Manually annotated by BRENDA team
-
different variants
Manually annotated by BRENDA team
-
predominant tissue
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
first faeces of an infant
Manually annotated by BRENDA team
-
acid SMase
Manually annotated by BRENDA team
-
from cord blood of infants of 30-40 weeks, of adults from normal healthy volunteers of either sex, from patients with Padgetis disease
Manually annotated by BRENDA team
-
high content of S-SMase, secretion
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the ratio of secreted to intracellular activity is about 8fold greater in I-cells (skin fibroblasts from I-cell disease patients, in which one of the enzymes responsible for mannose phosphorylation, GlcNAc-phosphotransferase, is deficient) than in normal cells
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the metallophosphoesterase enzyme family
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NSMA3_HUMAN
866
1
97810
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
123000
-
gel filtration
150000
-
enzyme A, gel filtration
200000
28300
-
1 * 36800 + 1 * 28300, SDS-PAGE
290000
-
gel filtration
30700
-
1 * 89100 + 1 * 47500 + 1 * 30700, SDS-PAGE
36800
-
1 * 36800 + 1 * 28300, SDS-PAGE
39800
-
1 * 70500 + 1 * 39800, SDS-PAGE
42000
-
x * 42000, SDS-PAGE
45000
47500
-
1 * 89100 + 1 * 47500 + 1 * 30700, SDS-PAGE
47600
56000
x * 56000, about, sequence calculation
57000
-
1 * 70000 + 1 * 57000, SDS-PAGE + western blotting analysis
60000
62000
-
2 * 62000 SDS-PAGE
67000
x * 67000, about, sequence calculation
68000
-
gel filtration or gel electrophoresis
70000
70500
-
1 * 70500 + 1 * 39800, SDS-PAGE
71000
72000
75000
89100
-
1 * 89100 + 1 * 47500 + 1 * 30700, SDS-PAGE
90000
-
1 * 90000 + 1 * 45000
95000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
trimer
-
1 * 89100 + 1 * 47500 + 1 * 30700, SDS-PAGE
additional information
-
structural-functional properties of its carboxyl-terminus, amino acids 462-629, overview, ASM consists of a signal peptide, amino acids 1-46, in the N-terminal region, a small transmembrane domain, amino acids 25-47, a saposin B region, amino acids 87-165, that serves as an activator of various lysosomal lipid-degrading enzymes, a proline-rich region, amino acids 179-197, followed by the metallophosphoesterase catalytic domain, amino acids 199-461
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
lipoprotein
-
neutral sphingomyelinase 2 is palmitoylated on multiple cysteine residues, palmitoylation of nSMase2 via thioester linkage, mutational analysis, overview
no glycoprotein
-
-
phosphoprotein
proteolytic modification
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain in complex with CMP, sitting drop vapor diffusion method, using 2.08 M disodium malonate pH 5, 0.23 M sodium thiocyanate
in complex with phosphocholine, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 as precipitant
vapor diffusion method, using 0.2 M sodium acetate, 20% (w/v) polyethylene glycol 8000, 0.1 M sodium cacodylate, pH 6.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C120S
-
mutant enzyme is almost completely devoid of activity in the detergent-containing micellar assay system as well as in the liposomal assay system in the presence of saposin C
C131S
-
mutant enzyme is almost completely devoid of activity in the detergent-containing micellar assay system as well as in the liposomal assay system in the presence of saposin C
C1A
-
site-directed mutagenesis, the altered residue shows altered palmitoylationin the mutant
C2A
-
site-directed mutagenesis, the altered residue shows altered palmitoylationin the mutant
C3A
-
site-directed mutagenesis, the altered residue shows altered palmitoylationin the mutant
C3A/C392A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C3A/C395A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C3A/C395A/C396A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C3A/C396A C3A/C400A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C3A/C5A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C4A
-
site-directed mutagenesis, the altered residue shows altered palmitoylationin the mutant
C5A
-
site-directed mutagenesis, the altered residue shows altered palmitoylationin the mutant
C5A/C53A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C5A/C53A/C54A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C5A/C53A/C59A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C5A/C54A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C5A/C54A/C59A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C5A/C59A
-
site-directed mutagenesis, the altered residues show altered palmitoylationin the mutant
C617Y
-
the mutation is associated with leukemia
C629S
-
5fold increase in activity, modification or deletion of the thiol group on the C-terminal cysteine leads to activation of rhASM
C78N
-
reduced alk-SMase activity
D194N
-
the mutation is associated with leukemia
D199A
-
mutation of the metal binding site of alk-SMase abolishes the enzyme activity
D278A
inactive
D358G
-
the mutation is associated with leukaemia and causes protein instability
D51N
-
the mutation is associated with leukemia
E499G
-
the mutation is associated with leukemia
E49A
no activity
E49Q
-
complete loss of hnSMase activity
F572L
naturally occuring mutation, reconstructed by site-directed mutagenesis, involved in acid sphingomyelinase deficiency and subsequently in Niemann-Pick disease, marked deficiency of enzyme activity consistent with the disease phenotype in cells homoallelic for the mutation
G195E
-
the mutation is associated with leukemia
G247D
naturally occuring mutation, reconstructed by site-directed mutagenesis, involved in acid sphingomyelinase deficiency and subsequently in Niemann-Pick disease, marked deficiency of enzyme activity consistent with the disease phenotype in cells homoallelic for the mutation
G248S
-
the mutation is associated with leukemia
G508R
-
naturally occuring polymorphisms in the SMPD1 gene, the G1522A and a hexanucleotide repeat sequence within the signal peptide region, are investigated in 118 unrelated individuals of French Canadian descent with low plasma levels of HDL-cholesterol, allele frequency, the two common coding variants at the SMPD1 gene locus are not associated with low HDL-cholesterol levels in the French Canadian population, overview
G577A
-
naturally occuring mutation, the mutant has severely defective enzymatic function
H272A
no activity
H272N
-
complete loss of hnSMase activity
H319Y
inactive
H353A
-
inactive mutant enzyme
H425R
inactive
K104A
-
mutation does not result in any altered activity
K105A
-
intracellular activity is not reduced but zinc-responsive secreted activity is reduced
K118A
-
intracellular activity is not reduced but zinc-responsive secreted activity is reduced
K118E
-
mutant enzyme is almost completely devoid of activity in the detergent-containing micellar assay system as well as in the liposomal assay system in the presence of saposin C
K124A
-
intracellular activity is not reduced but zinc-responsive secreted activity is reduced
K183A
-
intracellular activity is not reduced but zinc-responsive secreted activity is reduced
K187A
-
intracellular activity is reduced but zinc-responsive secreted activity is unchanged
K249A
-
intracellular activity and zinc-responsive secreted activity are both reduced
K305A
-
intracellular activity and zinc-responsive secreted activity are both reduced
K346A
-
intracellular activity is reduced but zinc-responsive secreted activity is unchanged
K419A
-
intracellular activity and zinc-responsive secreted activity are both reduced
K433A
-
intracellular activity and zinc-responsive secreted activity are both reduced
K576A
-
intracellular activity and zinc-responsive secreted activity are both reduced
K93A
-
mutant enzyme has reduced intracellular activity, but enhanced zinc-responsive secreted activity
M74K
-
reduced alk-SMase activity
N180A
no activity
N180H
-
complete loss of hnSMase activity
O153A
-
mutant enzyme still exhibits enzyme activity of approximately 52% of normal in a detergent-containing micellar assay, but only 13% of normal activity in a detergent-free liposomal assay system. Addition of saposin C to the liposomal ass mixture increases activity of the mutant enzyme to 46% of normal. Saposin C does not result in complete restoration of the variant activity
R246C
-
the mutation is associated with leukemia
R336C
-
the mutation is associated with leukemia
R496L
-
naturally occuring mutation, the mutant has severely defective enzymatic function
S248R
naturally occuring mutation, reconstructed by site-directed mutagenesis, involved in acid sphingomyelinase deficiency and subsequently in Niemann-Pick disease, marked deficiency of enzyme activity consistent with the disease phenotype in cells homoallelic for the mutation
S508A
-
site-directed mutagenesis of ASMase, the mutation blocks the ceramide formation after phorbol 12-myristate 13-acetate treatment, the mutant acts dominantly negative
S76F
-
alk-SMase activity is abolished
V131L
-
the mutation is associated with leukemia
V507I
-
the mutation is associated with leukemia
W391G
naturally occuring mutation, reconstructed by site-directed mutagenesis, involved in acid sphingomyelinase deficiency and subsequently in Niemann-Pick disease, marked deficiency of enzyme activity consistent with the disease phenotype in cells homoallelic for the mutation
Y109L
the mutation mutant decreases the hydrolysis rate of sphingomyelin and 4-nitrophenylphosphorylcholine 5-10fold compared to the wild type enzyme
Y166L
the mutation mutant decreases the hydrolysis rate of sphingomyelin and 4-nitrophenylphosphorylcholine 5-10fold compared to the wild type enzyme
Y43H
-
the mutation is associated with leukemia
Y537H
-
naturally occuring mutation, the mutant has severely defective enzymatic function
Y95F
-
the mutation is associated with leukemia
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
highest stability
135149
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
storage of very small volume cerebrospinal fluid aliquots, below 0.02 ml, at room temperature or above lead to the rapid loss of enzyme activity
40
-
enzyme in cerebrospinal fluid, 2 h, stable under acidic conditions
50
-
50% suppression
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
albumin stabilizes
-
detergents, e.g. Nonidet P-40, stabilization
-
glycerol, stabilization
-
reducing agents such as dithiothreitol stablize nSMase2 during preparation
stable with n-octyl-beta-D-glucopyranoside
-
the wild-type SMPD1 protein has a half-life of over 12 h. The half-life for the F572L protein is shorter, between 4 h and 8 h. The G247D mutation dramatically alters the stability of the mutant protein with a half-life of 2 h or less
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM citrate buffer, pH 5.9, 2 mg/ml cutsum, 50% glycerol, 5 mM EDTA, 1 mM dithiothreitol, more than 3 months
-
-20°C, up to 1 year
-
-80°C, 50 mM n-octyl-beta-D-glucopyranoside, more than 4 months
-
10 mM Tris-HCl, pH 7.2, 0. 1% Triton X-100, 10 mM 2-mercaptoethanol, protein 0.1 mg/ml, more than 2 months
-
22°C, storage of very small volume cerebrospinal fluid aliquots, below 0.02 ml, at room temperature or above lead to the rapid loss of enzyme activity
-
4°C, 0.5% Triton X-100, more than 4 months
-
4°C, 50% loss of activity after 3-5 months
-
4°C, stable for at least 3 months
-
4°C, stable for several weeks
-
the enzyme keeps over 80% activity after 8 rounds of freezing and thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10000-140000fold
-
10000fold
-
110000fold
-
134fold
-
1430fold, urinary enzyme
-
1700fold
-
21fold
-
22990fold
-
30fold
-
370fold
-
4475fold
-
affinity purification of recombinant hnSMase
-
ammonium sulfate precipitation, HiTrap phenyl column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
enzyme A 800fold pure, enzyme B 2500fold pure
-
Ni-NTA column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
partial
-
recombinant and native haSMase
-
recombinant haSMase, ammonium sulfate, Con A-Sepharose, Octyl-Sepharose, Matrex Gel Red A, DEAE-650
-
recombinant His-tagged enzyme from CHO cell culture medium by nickel affinity chromatography
recombinant wild-type and mutant alk-Smase from COS-7 cells
-
SE column chromatography, the enzyme is not retained in DEAE-Sepharose column equilibrated with 20 mM Tris-HCl buffer containing 0.075 M NaCl
-
two procedures, with and without added detergents
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Saccharomyces cerevisiae strain JK9-3dDELTAIsc1p, lacking endogenous SMase activity
alk-SMase, expression of wild-type and mutant alk-Smase in COS-7 cells
-
alkaline sphingomyelinase, cloning and DNA and amino acid sequence determination and analysis from Hep-G2 cancer cells, transient expression of mutant alkaline sphingomyelinase forms in COS-7 cells
cloning of cDNA
ectopic overexpression of nSMase-1 gene in HEK293 cells
-
enzyme expressed from cDNA from HT-29 cells in COS-7 cells shows little alk-SMase activity, enzyme expressed from cDNA from Caco-2 cells in COS-7 cells is as active as wild-type enzyme
-
expressed in CHO cells and in Mus musculus
-
expressed in Mus musculus B16-F10 melanoma cells
-
expressed in Mus musculus osteosarcoma cells (F4328)
-
expressed in Pichia pastoris strain GS115
-
expressed in Sf9 insect cells
expression in CHO cells
-
expression in COS-7 cells
-
expression in COS7 and Jurkat T cells
expression in COS7 cells
expression in Escherichia coli
-
expression in Escherichia coli and HEK293 kidney cells
-
expression in insect, Spodoptera frugiperda 21cells
-
expression in MCF7 breast cancer cells
-
expression in SF21 cells
-
expression in Sf9 insect cells
-
expression of nSMase1 in HEK293 kidney cells
-
expression of nSMase2 in HEK293 kidney cells
-
expression of V5-tagged nSMase2 in A-549 cells
-
expression of V5-tagged unprocessed aSMase in MCF-7 and HEK-293 cells
-
gene SMPD1, genotyping, expression of wild-type and mutant enzymes in COS-7 cells
gene SMPD1, quantitative real-time PCR expression analysis, recombinant His-tagged enzyme expression in CHO cells and secretion to the culture medium
gene SMPD1, splicing form ASM-5, genetic organisation of splicing variants, overview. Alternative splicing of the enzyme of functional significance for the cellular stress response, possibly representing a mechanism for maintaining constant levels of cellular ASM enzyme activity. Expression of FLAG-tagged ASM-5 in HeLa cells
gene SMPD1, splicing form ASM-6, genetic organisation of splicing variants, overview. Alternative splicing of the enzyme of functional significance for the cellular stress response, possibly representing a mechanism for maintaining constant levels of cellular ASM enzyme activity. Expression of FLAG-tagged ASM-6 in HeLa cells
gene SMPD1, splicing form ASM-7, genetic organisation of splicing variants, overview. Alternative splicing of the enzyme of functional significance for the cellular stress response, possibly representing a mechanism for maintaining constant levels of cellular ASM enzyme activity. Expression of FLAG-tagged ASM-7 in HeLa cells
gene SMPD1, transient overexpression of wild-type ASMase and mutant S508A in MCF-7 cells
-
isozyme nSMase1
-
nSMase1, DNA and amino acid sequence determination and analysis
nSMase2, DNA and amino acid sequence determination and analysis, overexpression of nSMase2 in DELTAISC1 yeast cells and in MCF-7 cells
overexpressed in chinese hamster ovary cells
-
overexpression of V5-tagged wild-type and mutant nSMases and of GFP-tagged mutant C3A/C5A in MCF-7 cells
-
SMPD1 gene, genotyping
-
splicing forms ASM-1 to ASM-4, genetic organisation of splicing variants, overview. Alternative splicing of the enzyme of functional significance for the cellular stress response, possibly representing a mechanism for maintaining constant levels of cellular ASM enzyme activity. Expression of FLAG-tagged ASM-1 in HeLa cells
transfection of murine and human glioma cell lines Gl-261 and U-373 with acid sphingomyelinase results in a marked sensitization of glioma cells to gemcitabine and doxorubicin, respectively
-
transient transfection of the His/V5-tagged wild-type and mutant recombinant ASM in CHO cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3-acetyl-11-keto-beta-boswellic acid inhibits expression of acid sphingomyelinase in intestinal cells at high concentration 3-acetyl-11-keto-beta-boswellic acid decreases both the mass of acid SMase protein and the mRNA levels of acid SMase in the cells
-
acid SMase protein is decreased by 20% in both Hep-G2 and Caco-2 cells at 0.1 mM ezetimibe
-
all-trans-retinoic acid induces nSMase2
-
electrophilic compounds such as diethyl malate, methyl mercury, and cigarette smoke extracts significantly enhanced the expression of acidic sphingomyelinase 6fold in bladder carcinoma ECV-304 cells
-
ezetimibe up to 0.05 mM has no effects on acid phosphatase activity in both Hep-G2 and Caco-2 cells, no change of alkaline phosphatase activity is identified by ezetimibe
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
drug development
-
acid sphingomyelinase activity and sphingomyelin presence are necessary for efficient infection of cells by ebolavirus,the enzym eis a target for drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Spence, M.W.; Byers, D.M.; Palmer, F.B.St.C.; Cook, H.W.
A new Zn2+-stimulated sphingomyelinase in fetal bovine serum
J. Biol. Chem.
264
5358-5363
1989
Bos taurus, Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Zou, L.; Kojima, N.; Kito, M.; Yagi, K.
Purification to homogeneity of human placental acid sphingomyelinase
Biotechnol. Appl. Biochem.
11
217-225
1989
Homo sapiens
Manually annotated by BRENDA team
Vanha-Perttula, T.
Sphingomyelinases in human, bovine and porcine seminal plasma
FEBS Lett.
233
263-267
1988
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Quintern, L.E.; Weitz, G.; Nehrkorn, H.; Tager, J.M.; Schram, A.W.; Sandhoff, K.
Acid sphingomyelinase from human urine: purification and characterization
Biochim. Biophys. Acta
922
323-336
1987
Homo sapiens
Manually annotated by BRENDA team
Rousson, R.; Bonnet, J.; Louisot, P.; Vanier, M.T.
Presence of immunoreactive material in Niemann-Pick type A placenta using anti-sphingomyelinase rabbit gammaglobulins
Biochim. Biophys. Acta
924
502-508
1987
Homo sapiens
Manually annotated by BRENDA team
Christomanou, H.; Aignesberger, A.; Linke, R.P.
Immunochemical characterization of two activator proteins stimulating enzymic sphingomyelin degradation in vitro. Absence of one of them in a human Gaucher disease variant
Biol. Chem. Hoppe-Seyler
367
879-890
1986
Homo sapiens
Manually annotated by BRENDA team
Christmanou, H.; Kleinschmidt, T.
Isolation of two forms of an activator protein for the enzymic sphingomyelin degradation from human Gaucher spleen
Biol. Chem. Hoppe-Seyler
366
245-256
1985
Homo sapiens
Manually annotated by BRENDA team
Schram, A.W.; Weitz, G.; Driessen, M.; Brouwer-Kelder, E.M.; Sandhoff, K.; Barranger, J.A.; Tager, J.M.
Immunological properties of urinary sphingomyelinase
Biochem. Soc. Trans.
12
1027-1028
1984
Homo sapiens
-
Manually annotated by BRENDA team
Weitz, G.; Lindl, T.; Hinrichs, U.; Sandhoff, K.
Release of sphingomyelin phosphodiesterase (acid sphingomyelinase) by ammonium chloride from CL 1D mouse L-cells and human fibroblasts. Partial purification and characterization of the exported enzymes
Hoppe-Seyler's Z. Physiol. Chem.
364
863-871
1983
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Sakuragawa, N.
Acid sphingomyelinase of human placenta: purification, properties, and 125iodine labeling
J. Biochem.
92
637-646
1982
Homo sapiens
Manually annotated by BRENDA team
Jones, C.S.; Shankaran, P.; Callahan, J.W.
Purification of sphingomyelinase to apparent homogeneity by using hydrophobic chromatography
Biochem. J.
195
373-382
1981
Homo sapiens
Manually annotated by BRENDA team
Yamanaka, T.; Hanada, E.; Suzuki, K.
Acid sphingomyelinase of human brain. Improved purification procedures and characterization
J. Biol. Chem.
256
3884-3889
1981
Homo sapiens
Manually annotated by BRENDA team
Callahan, J.W.; Gerrie, J.; Jones, C.S.; Shankaran, P.
Studies on the hydrophobic properties of sphingomyelinase
Biochem. J.
193
275-283
1981
Homo sapiens
Manually annotated by BRENDA team
Callahan, J.W.; Shankaran, P.; Khalil, M.; Gerrie, J.
Sphingomyelinases in human tissues. IV. Purification of sphingomyelinase from human placenta and effect of Triton X-100
Can. J. Biochem.
56
885-891
1978
Homo sapiens
Manually annotated by BRENDA team
Pentchev, P.G.; Brady, R.O.; Gal, A.E.; Hibbert, S.R.
The isolation and characterization of sphingomyelinase from human placental tissue
Biochim. Biophys. Acta
488
312-321
1977
Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, S.; Suzuki, K.
Purification and characterization of sphingomyelinase from human brain
J. Biol. Chem.
252
3805-3813
1977
Homo sapiens
Manually annotated by BRENDA team
Okazaki, T.; Bielawska, A.; Domae, N.; Bell, R.M.; Hannun, Y.A.
Characteristics and partial purification of a novel cytosolic, magnesium-independent, neutral sphingomyelinase activated in the early signal transduction of 1alpha,25-dihydroxyvitamin D3-induced HL-60 cell differentiation
J. Biol. Chem.
269
4070-4077
1994
Homo sapiens
Manually annotated by BRENDA team
Lansmann, S.; Ferlinz, K.; Hurwitz, R.; Bartelsen, O.; Glombitza, G.; Sandhoff, K.
Purification of acid sphingomyelinase from human placenta: Characterization and N-terminal sequence
FEBS Lett.
399
227-231
1996
Homo sapiens
Manually annotated by BRENDA team
Duan, R.D.; Nilsson, A.
Purification of a newly identified alkaline sphingomyelinase in human bile and effects of bile salts and phosphatidylcholine on enzyme activity
Hepatology
26
823-830
1997
Homo sapiens
Manually annotated by BRENDA team
Mansat, V.; Bettaieb, A.; Levade, T.; Laurent, G.; Jaffrezou, J.P.
Serine protease inhibitors block neutral sphingomyelinase activation, ceramide generation, and apoptosis triggered by daunorubicin
FASEB J.
11
695-702
1997
Homo sapiens
Manually annotated by BRENDA team
Chatterjee, S.; Han, H.; Rollins, S.; Cleveland, T.
Molecular cloning, characterization, and expression of a novel human neutral sphingomyelinase
J. Biol. Chem.
274
37407-37412
1999
Homo sapiens
Manually annotated by BRENDA team
Bartelsen, O.; Lansmann, S.; Nettersheim, M.; Le mM, T.; Ferlinz, K.; Sandhoff, K.
Expression of recombinant human acid sphingomyelinase in insect Sf21 cells: purification, processing and enzymatic characterization
J. Biotechnol.
63
29-40
1998
Homo sapiens
Manually annotated by BRENDA team
He, X.; Miranda, S.R.P.; Xiong, X.; Dagan, A.; Gatt, S.; Schuchman, E.H.
Characterization of human acid sphingomyelinase purified from the media of overexpressing chinese hamster ovary cells
Biochim. Biophys. Acta
1432
251-264
1999
Homo sapiens
Manually annotated by BRENDA team
Samet, D.; Barenholz, Y.
Characterization of acidic and neutral sphingomyelinase activities in crude extracts of HL-60 cells
Chem. Phys. Lipids
102
65-77
1999
Homo sapiens
Manually annotated by BRENDA team
Tepper, A.D.; Ruurs, P.; Borst, J.; van Blitterswijk, W.J.
Effect of overexpression of a neutral sphingomyelinase on CD95-induced ceramide production and apoptosis
Biochem. Biophys. Res. Commun.
280
634-639
2001
Homo sapiens (O60906), Homo sapiens
Manually annotated by BRENDA team
Lansmann, S.; Schuette, C.G.; Bartelsen, O.; Hoernschemeyer, J.; Linke, T.; Weisgerber, J.; Sandhoff, K.
Human acid sphingomyelinase: Assignment of the disulfide bond pattern
Eur. J. Biochem.
270
1076-1088
2003
Homo sapiens
Manually annotated by BRENDA team
Miura, Y.; Gotoh, E.; Nara, F.; Nishijima, M.; Hanada, K.
Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases
FEBS Lett.
557
288-292
2004
Bacillus cereus, Homo sapiens
Manually annotated by BRENDA team
Tomiuk, S.; Zumbansen, M.; Stoffel, W.
Characterization and subcellular localization of murine and human magnesium-dependent neutral sphingomyelinase
J. Biol. Chem.
275
5710-5717
2000
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Qiu, H.; Edmunds, T.; Baker-Malcolm, J.; Karey, K.P.; Estes, S.; Schwarz, C.; Hughes, H.; Van Patten, S.M.
Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine
J. Biol. Chem.
278
32744-32752
2003
Homo sapiens
Manually annotated by BRENDA team
Duan, R.D.; Bergman, T.; Xu, N.; Wu, J.; Cheng, Y.; Duan, J.; Nelander, S.; Palmberg, C.; Nilsson, A.
Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family
J. Biol. Chem.
278
38528-38536
2003
Homo sapiens (Q6UWV6), Homo sapiens
Manually annotated by BRENDA team
Marchesini, N.; Osta, W.; Bielawski, J.; Luberto, C.; Obeid, L.M.; Hannun, Y.A.
Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells
J. Biol. Chem.
279
25101-25111
2004
Homo sapiens
Manually annotated by BRENDA team
Lansmann, S.; Bartelsen, O.; Sandhoff, K.
Purification and characterization of recombinant human acid sphingomyelinase expressed in insect Sf21 cells
Methods Enzymol.
311
149-156
2000
Homo sapiens
Manually annotated by BRENDA team
Hofmann, K.; Tomiuk, S.; Wolff, G.; Stoffel, W.
Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase
Proc. Natl. Acad. Sci. USA
97
5895-5900
2000
Homo sapiens (Q9NY59)
Manually annotated by BRENDA team
Oeoerni, K.; Posio, P.; Ala-Korpela, M.; Jauhiainen, M.; Kovanen, P.T.
Sphingomyelinase induces aggregation and fusion of small very low-density lipoprotein and intermediate-density lipoprotein particles and increases their retention to human arterial proteoglycans
Arterioscler. Thromb. Vasc. Biol.
25
1678-1683
2005
Homo sapiens
Manually annotated by BRENDA team
Wu, J.; Hansen, G.H.; Nilsson, A.; Duan, R.D.
Functional studies of human intestinal alkaline sphingomyelinase by deglycosylation and mutagenesis
Biochem. J.
386
153-160
2005
Homo sapiens
Manually annotated by BRENDA team
Wu, J.; Nilsson, A.; Jonsson, B.A.; Stenstad, H.; Agace, W.; Cheng, Y.; Duan, R.D.
Intestinal alkaline sphingomyelinase hydrolyses and inactivates platelet-activating factor by a phospholipase C activity
Biochem. J.
394
299-308
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Duan, R.D.
Alkaline sphingomyelinase: An old enzyme with novel implications
Biochim. Biophys. Acta
1761
281-291
2006
Homo sapiens
Manually annotated by BRENDA team
Koelzer, M.; Ferlinz, K.; Bartelsen, O.; Hoops, S.L.; Lang, F.; Sandhoff, K.
Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase
Biol. Chem.
385
1193-1195
2004
Homo sapiens
Manually annotated by BRENDA team
Di Marzio, L.; Di Leo, A.; Cinque, B.; Fanini, D.; Agnifili, A.; Berloco, P.; Linsalata, M.; Lorusso, D.; Barone, M.; De Simone, C.; Cifone, M.G.
Detection of alkaline sphingomyelinase activity in human stool: Proposed role as a new diagnostic and prognostic marker of colorectal cancer
Cancer Epidemiol. Biomarkers Prev.
14
856-862
2005
Homo sapiens
Manually annotated by BRENDA team
Liu, F.; Cheng, Y.; Wu, J.; Tauschel, H.D.; Duan, R.D.
Ursodeoxycholic acid differentially affects three types of sphingomyelinase in human colon cancer Caco 2 cells
Cancer Lett.
235
141-146
2006
Homo sapiens
Manually annotated by BRENDA team
Wu, J.; Cheng, Y.; Nilsson, A.; Duan, R.D.
Identification of one exon deletion of intestinal alkaline sphingomyelinase in colon cancer HT-29 cells and a differentiation-related expression of the wild-type enzyme in Caco-2 cells
Carcinogenesis
25
1327-1333
2004
Homo sapiens
Manually annotated by BRENDA team
Koelzer, M.; Werth, N.; Sandhoff, K.
Interactions of acid sphingomyelinase and lipid bilayers in the presence of the tricyclic antidepressant desipramine
FEBS Lett.
559
96-98
2004
Homo sapiens
Manually annotated by BRENDA team
Knapp, P.; Dobrzyn, A.; Gorski, J.
Ceramides, sphinganine, sphingosine and acid sphingomyelinases in the human umbilical cord blood
Horm. Metab. Res.
37
433-437
2005
Homo sapiens
Manually annotated by BRENDA team
Pittis, M.G.; Ricci, V.; Guerci, V.I.; Marcais, C.; Ciana, G.; Dardis, A.; Gerin, F.; Stroppiano, M.; Vanier, M.T.; Filocamo, M.; Bembi, B.
Acid sphingomyelinase: identification of nine novel mutations among Italian Niemann pick type B patients and characterization of in vivo functional in-frame start codon
Hum. Mutat.
24
186-187
2004
Homo sapiens
Manually annotated by BRENDA team
Kashkar, H.; Wiegmann, K.; Yazdanpanah, B.; Haubert, D.; Kroenke, M.
Acid sphingomyelinase is indispensable for UV light-induced Bax conformational change at the mitochondrial membrane
J. Biol. Chem.
280
20804-20813
2005
Homo sapiens
Manually annotated by BRENDA team
Krut, O.; Wiegmann, K.; Kashkar, H.; Yazdanpanah, B.; Kronke, M.
Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein
J. Biol. Chem.
281
13784-13793
2006
Homo sapiens (Q9NXE4), Homo sapiens
Manually annotated by BRENDA team
Mari, M.; Colell, A.; Morales, A.; Paneda, C.; Varela-Nieto, I.; Garcia-Ruiz, C.; Fernandez-Checa, J.C.
Acidic sphingomyelinase downregulates the liver-specific methionine adenosyltransferase 1A, contributing to tumor necrosis factor-induced lethal hepatitis
J. Clin. Invest.
113
895-904
2004
Homo sapiens
Manually annotated by BRENDA team
Jensen, J.M.; Folster-Holst, R.; Baranowsky, A.; Schunck, M.; Winoto-Morbach, S.; Neumann, C.; Schutze, S.; Proksch, E.
Impaired sphingomyelinase activity and epidermal differentiation in atopic dermatitis
J. Invest. Dermatol.
122
1423-1431
2004
Homo sapiens
Manually annotated by BRENDA team
Testai, F.D.; Landek, M.A.; Goswami, R.; Ahmed, M.; Dawson, G.
Acid sphingomyelinase and inhibition by phosphate ion: role of inhibition by phosphatidyl-myo-inositol 3,4,5-triphosphate in oligodendrocyte cell signaling
J. Neurochem.
89
636-644
2004
Homo sapiens
Manually annotated by BRENDA team
Testai, F.D.; Landek, M.A.; Dawson, G.
Regulation of sphingomyelinases in cells of the oligodendrocyte lineage
J. Neurosci. Res.
75
66-74
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Zhou, Q.; Band, M.R.; Hernandez, A.; Liu, Z.L.; Kummerow, F.A.
27-Hydroxycholesterol inhibits neutral sphingomyelinase in cultured human endothelial cells
Life Sci.
75
1567-1577
2004
Homo sapiens (O60906), Homo sapiens
Manually annotated by BRENDA team
Takahashi, I.; Takahashi, T.; Mikami, T.; Komatsu, M.; Ohura, T.; Schuchman, E.H.; Takada, G.
Acid sphingomyelinase: Relation of 93Lysine residue on the ratio of intracellular to secreted enzyme activity
Tohoku J. Exp. Med.
206
333-340
2005
Homo sapiens
Manually annotated by BRENDA team
Grammatikos, G.; Teichgraeber, V.; Carpinteiro, A.; Trarbach, T.; Weller, M.; Hengge, U.R.; Gulbins, E.
Overexpression of acid sphingomyelinase sensitizes glioma cells to chemotherapy
Antioxid. Redox Signal.
9
1449-1456
2007
Homo sapiens
Manually annotated by BRENDA team
Martin, S.F.; Sawai, H.; Villalba, J.M.; Hannun, Y.A.
Redox regulation of neutral sphingomyelinase-1 activity in HEK293 cells through a GSH-dependent mechanism
Arch. Biochem. Biophys.
459
295-300
2007
Homo sapiens
Manually annotated by BRENDA team
De Palma, C.; Meacci, E.; Perrotta, C.; Bruni, P.; Clementi, E.
Endothelial nitric oxide synthase activation by tumor necrosis factor alpha through neutral sphingomyelinase 2, sphingosine kinase 1, and sphingosine 1 phosphate receptors
Arterioscler. Thromb. Vasc. Biol.
26
99-105
2006
Homo sapiens
Manually annotated by BRENDA team
Clarke, C.J.; Snook, C.F.; Tani, M.; Matmati, N.; Marchesini, N.; Hannun, Y.A.
The extended family of neutral sphingomyelinases
Biochemistry
45
11247-11256
2006
Helicobacter pylori, Staphylococcus aureus, Rattus norvegicus, Homo sapiens (O60906), Homo sapiens (Q9NY59), Bacillus cereus (P09599), Listeria ivanovii (Q9RLV9), Listeria ivanovii nSMase (Q9RLV9), Helicobacter pylori nSMase, Bacillus cereus nSMase (P09599)
Manually annotated by BRENDA team
Lee, C.Y.; Tamura, T.; Rabah, N.; Lee, D.Y.; Ruel, I.; Hafiane, A.; Iatan, I.; Nyholt, D.; Laporte, F.; Lazure, C.; Wada, I.; Krimbou, L.; Genest, J.
Carboxyl-terminal disulfide bond of acid sphingomyelinase is critical for its secretion and enzymatic function
Biochemistry
46
14969-14978
2007
Homo sapiens
Manually annotated by BRENDA team
Clarke, C.J.; Hannun, Y.A.
Neutral sphingomyelinases and nSMase2: bridging the gaps
Biochim. Biophys. Acta
1758
1893-1901
2006
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Dastani, Z.; Ruel, I.L.; Engert, J.C.; Genest, J.; Marcil, M.
Sphingomyelin phosphodiesterase-1 (SMPD1) coding variants do not contribute to low levels of high-density lipoprotein cholesterol
BMC Med. genet.
8
79
2007
Homo sapiens
Manually annotated by BRENDA team
Cheng, Y.; Wu, J.; Hertervig, E.; Lindgren, S.; Duan, D.; Nilsson, A.; Duan, R.D.
Identification of aberrant forms of alkaline sphingomyelinase (NPP7) associated with human liver tumorigenesis
Br. J. Cancer
97
1441-1448
2007
Homo sapiens (Q6UWV6), Homo sapiens
Manually annotated by BRENDA team
Ion, G.; Fajka-Boja, R.; Kovacs, F.; Szebeni, G.; Gombos, I.; Czibula, A.; Matko, J.; Monostori, E.
Acid sphingomyelinase mediated release of ceramide is essential to trigger the mitochondrial pathway of apoptosis by galectin-1
Cell. Signal.
18
1887-1896
2006
Homo sapiens
Manually annotated by BRENDA team
Doehner, W.; Bunck, A.C.; Rauchhaus, M.; von Haehling, S.; Brunkhorst, F.M.; Cicoira, M.; Tschope, C.; Ponikowski, P.; Claus, R.A.; Anker, S.D.
Secretory sphingomyelinase is upregulated in chronic heart failure: a second messenger system of immune activation relates to body composition, muscular functional capacity, and peripheral blood flow
Eur. Heart J.
28
821-828
2007
Homo sapiens
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, Mus musculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Castillo, S.S.; Levy, M.; Thaikoottathil, J.V.; Goldkorn, T.
Reactive nitrogen and oxygen species activate different sphingomyelinases to induce apoptosis in airway epithelial cells
Exp. Cell Res.
313
2680-2686
2007
Homo sapiens
Manually annotated by BRENDA team
Castillo, S.S.; Levy, M.; Wang, C.; Thaikoottathil, J.V.; Khan, E.; Goldkorn, T.
Nitric oxide-enhanced caspase-3 and acidic sphingomyelinase interaction: a novel mechanism by which airway epithelial cells escape ceramide-induced apoptosis
Exp. Cell Res.
313
816-823
2007
Homo sapiens
Manually annotated by BRENDA team
Tani, M.; Hannun, Y.A.
Neutral sphingomyelinase 2 is palmitoylated on multiple cysteine residues. Role of palmitoylation in subcellular localization
J. Biol. Chem.
282
10047-10056
2007
Homo sapiens
Manually annotated by BRENDA team
Zeidan, Y.H.; Hannun, Y.A.
Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation
J. Biol. Chem.
282
11549-11561
2007
Homo sapiens
Manually annotated by BRENDA team
Clarke, C.J.; Truong, T.G.; Hannun, Y.A.
Role for neutral sphingomyelinase-2 in tumor necrosis factor alpha-stimulated expression of vascular cell adhesion molecule-1 (VCAM) and intercellular adhesion molecule-1 (ICAM) in lung epithelial cells: p38 MAPK is an upstream regulator of nSMase2
J. Biol. Chem.
282
1384-1396
2007
Homo sapiens
Manually annotated by BRENDA team
Walton, K.A.; Gugiu, B.G.; Thomas, M.; Basseri, R.J.; Eliav, D.R.; Salomon, R.G.; Berliner, J.A.
A role for neutral sphingomyelinase activation in the inhibition of LPS action by phospholipid oxidation products
J. Lipid Res.
47
1967-1974
2006
Homo sapiens
Manually annotated by BRENDA team
Coll, O.; Morales, A.; Fernandez-Checa, J.C.; Garcia-Ruiz, C.
Neutral sphingomyelinase-induced ceramide triggers germinal vesicle breakdown and oxidant-dependent apoptosis in Xenopus laevis oocytes
J. Lipid Res.
48
1924-1935
2007
Bacillus cereus, Homo sapiens
Manually annotated by BRENDA team
Kornhuber, J.; Tripal, P.; Reichel, M.; Terfloth, L.; Bleich, S.; Wiltfang, J.; Gulbins, E.
Identification of new functional inhibitors of acid sphingomyelinase using a structure-property-activity relation model
J. Med. Chem.
51
219-237
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Adamy, C.; Mulder, P.; Khouzami, L.; Andrieu-abadie, N.; Defer, N.; Candiani, G.; Pavoine, C.; Caramelle, P.; Souktani, R.; Le Corvoisier, P.; Perier, M.; Kirsch, M.; Damy, T.; Berdeaux, A.; Levade, T.; Thuillez, C.; Hittinger, L.; Pecker, F.
Neutral sphingomyelinase inhibition participates to the benefits of N-acetylcysteine treatment in post-myocardial infarction failing heart rats
J. Mol. Cell. Cardiol.
43
344-353
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Duan, R.; Cheng, Y.; Joensson, B.A.; Ohlsson, L.; Herbst, A.; Hellstroem-Westas, L.; Nilsson, A.
Human meconium contains significant amounts of alkaline sphingomyelinase, neutral ceramidase, and sphingolipid metabolites
Pediatr. Res.
61
61-66
2006
Homo sapiens
Manually annotated by BRENDA team
Cheng, Y.; Kozubek, A.; Ohlsson, L.; Sternby, B.; Duan, R.D.
Curcumin decreases acid sphingomyelinase activity in colon cancer Caco-2 cells
Planta Med.
73
725-730
2007
Homo sapiens
Manually annotated by BRENDA team
Bock, J.; Liebisch, G.; Schweimer, J.; Schmitz, G.; Rogler, G.
Exogenous sphingomyelinase causes impaired intestinal epithelial barrier function
World J. Gastroenterol.
13
5217-5225
2007
Homo sapiens
Manually annotated by BRENDA team
Jafurulla, M.; Pucadyil, T.J.; Chattopadhyay, A.
Effect of sphingomyelinase treatment on ligand binding activity of human serotonin1A receptors
Biochim. Biophys. Acta
1778
2022-2025
2008
Homo sapiens
Manually annotated by BRENDA team
Kim, W.J.; Okimoto, R.A.; Purton, L.E.; Goodwin, M.; Haserlat, S.M.; Dayyani, F.; Sweetser, D.A.; McClatchey, A.I.; Bernard, O.A.; Look, A.T.; Bell, D.W.; Scadden, D.T.; Haber, D.A.
Mutations in the neutral sphingomyelinase gene SMPD3 implicate the ceramide pathway in human leukemias
Blood
111
4716-4722
2008
Homo sapiens
Manually annotated by BRENDA team
Andersson, D.; Kotarsky, K.; Wu, J.; Agace, W.; Duan, R.D.
Expression of alkaline sphingomyelinase in yeast cells and anti-inflammatory effects of the expressed enzyme in a rat colitis model
Digest. Dis. Sci.
54
1440-1448
2008
Homo sapiens
Manually annotated by BRENDA team
Dodge, J.C.; Clarke, J.; Treleaven, C.M.; Taksir, T.V.; Griffiths, D.A.; Yang, W.; Fidler, J.A.; Passini, M.A.; Karey, K.P.; Schuchman, E.H.; Cheng, S.H.; Shihabuddin, L.S.
Intracerebroventricular infusion of acid sphingomyelinase corrects CNS manifestations in a mouse model of Niemann-Pick A disease
Exp. Neurol.
215
349-357
2009
Homo sapiens
Manually annotated by BRENDA team
Smith, E.L.; Schuchman, E.H.
The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases
FASEB J.
22
3419-3431
2008
Homo sapiens
Manually annotated by BRENDA team
Corcoran, C.A.; He, Q.; Ponnusamy, S.; Ogretmen, B.; Huang, Y.; Sheikh, M.S.
Neutral sphingomyelinase-3 is a DNA damage and nongenotoxic stress-regulated gene that is deregulated in human malignancies
Mol. Cancer Res.
6
795-807
2008
Homo sapiens
Manually annotated by BRENDA team
Ziegler, R.J.; Brown, C.; Barbon, C.M.; DAngona, A.M.; Schuchman, E.H.; Andrews, L.; Thurberg, B.L.; McPherson, J.M.; Karey, K.P.; Cheng, S.H.
Pulmonary delivery of recombinant acid sphingomyelinase improves clearance of lysosomal sphingomyelin from the lungs of a murine model of Niemann-Pick disease
Mol. Genet. Metab.
97
35-42
2009
Homo sapiens
Manually annotated by BRENDA team
Clarke, C.J.; Guthrie, J.M.; Hannun, Y.A.
Regulation of neutral sphingomyelinase-2 (nSMase2) by tumor necrosis factor-alpha involves protein kinase C-delta in lung epithelial cells
Mol. Pharmacol.
74
1022-1032
2008
Homo sapiens
Manually annotated by BRENDA team
Smith, E.L.; Schuchman, E.H.
Acid sphingomyelinase overexpression enhances the antineoplastic effects of irradiation in vitro and in vivo
Mol. Ther.
16
1565-1571
2008
Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Duan, R.D.
Boswellic acid inhibits expression of acid sphingomyelinase in intestinal cells
Lipids Health Dis.
8
51
2009
Homo sapiens
Manually annotated by BRENDA team
Cheng, Y.; Liu, F.; Wu, J.; Zhang, Y.; Nilsson, A.; Duan, R.D.
Ezetimibe inhibits expression of acid sphingomyelinase in liver and intestine
Lipids
44
897-906
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Arenz, C.
Small molecule inhibitors of acid sphingomyelinase
Cell. Physiol. Biochem.
26
1-8
2010
Homo sapiens
Manually annotated by BRENDA team
Clarke, C.J.; Mediwala, K.; Jenkins, R.W.; Sutton, C.A.; Tholanikunnel, B.G.; Hannun, Y.A.
Neutral sphingomyelinase-2 mediates growth arrest by retinoic acid through modulation of ribosomal S6 kinase
J. Biol. Chem.
286
21565-21576
2011
Homo sapiens
Manually annotated by BRENDA team
Jenkins, R.W.; Idkowiak-Baldys, J.; Simbari, F.; Canals, D.; Roddy, P.; Riner, C.D.; Clarke, C.J.; Hannun, Y.A.
A novel mechanism of lysosomal acid sphingomyelinase maturation: requirement for carboxyl-terminal proteolytic processing
J. Biol. Chem.
286
3777-3788
2011
Homo sapiens
Manually annotated by BRENDA team
Perrotta, C.; Clementi, E.
Biological roles of Acid and neutral sphingomyelinases and their regulation by nitric oxide
Physiology
25
64-71
2010
Homo sapiens
Manually annotated by BRENDA team
Kumagai, T.; Ishino, T.; Nakagawa, Y.
Acidic sphingomyelinase induced by electrophiles promotes proinflammatory cytokine production in human bladder carcinoma ECV-304 cells
Arch. Biochem. Biophys.
519
8-16
2012
Homo sapiens
Manually annotated by BRENDA team
Traini, M.; Quinn, C.M.; Sandoval, C.; Johansson, E.; Schroder, K.; Kockx, M.; Meikle, P.J.; Jessup, W.; Kritharides, L.
Sphingomyelin phosphodiesterase-like 3A (SMPDL3A) is a novel nucleotide phosphodiesterase regulated by cholesterol in human macrophages
J. Biol. Chem.
289
32895-32913
2014
Homo sapiens (Q8IUN0), Homo sapiens
Manually annotated by BRENDA team
Miller, M.E.; Adhikary, S.; Kolokoltsov, A.A.; Davey, R.A.
Ebolavirus requires acid sphingomyelinase activity and plasma membrane sphingomyelin for infection
J. Virol.
86
7473-7483
2012
Homo sapiens
Manually annotated by BRENDA team
Toth, B.; Erdoes, M.; Szekely, A.; Ritli, L.; Bagossi, P.; Suemegi, J.; Marodi, L.
Molecular genetic characterization of novel sphingomyelin phosphodiesterase 1 mutations causing Niemann-Pick disease
JIMD Rep.
3
125-129
2012
Homo sapiens (P17405), Homo sapiens
Manually annotated by BRENDA team
He, Q.; Wang, G.; Wakade, S.; Dasgupta, S.; Dinkins, M.; Kong, J.N.; Spassieva, S.D.; Bieberich, E.
Primary cilia in stem cells and neural progenitors are regulated by neutral sphingomyelinase 2 and ceramide
Mol. Biol. Cell
25
1715-1729
2014
Homo sapiens
Manually annotated by BRENDA team
Rhein, C.; Tripal, P.; Seebahn, A.; Konrad, A.; Kramer, M.; Nagel, C.; Kemper, J.; Bode, J.; Muehle, C.; Gulbins, E.; Reichel, M.; Becker, C.M.; Kornhuber, J.
Functional implications of novel human acid sphingomyelinase splice variants
PLoS ONE
7
e35467
2012
Homo sapiens (E9LUE7), Homo sapiens (E9LUE8), Homo sapiens (E9LUE9), Homo sapiens (P17405), Homo sapiens
Manually annotated by BRENDA team
Muehle, C.; Huttner, H.B.; Walter, S.; Reichel, M.; Canneva, F.; Lewczuk, P.; Gulbins, E.; Kornhuber, J.
Characterization of acid sphingomyelinase activity in human cerebrospinal fluid
PLoS ONE
8
e62912
2013
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Bai, A.; Kokkotou, E.; Zheng, Y.; Robson, S.C.
Role of acid sphingomyelinase bioactivity in human CD4+ T-cell activation and immune responses
Cell Death Dis.
6
e1828
2015
Homo sapiens
Manually annotated by BRENDA team
Klutzny, S.; Lesche, R.; Keck, M.; Kaulfuss, S.; Schlicker, A.; Christian, S.; Sperl, C.; Neuhaus, R.; Mowat, J.; Steckel, M.; Riefke, B.; Prechtl, S.; Parczyk, K.; Steigemann, P.
Functional inhibition of acid sphingomyelinase by fluphenazine triggers hypoxia-specific tumor cell death
Cell Death Dis.
8
e2709
2017
Homo sapiens
Manually annotated by BRENDA team
Lim, S.M.; Yeung, K.; Tresaugues, L.; Ling, T.H.; Nordlund, P.
The structure and catalytic mechanism of human sphingomyelin phosphodiesterase like 3a--an acid sphingomyelinase homologue with a novel nucleotide hydrolase activity
FEBS J.
283
1107-1123
2016
Homo sapiens (Q92484), Homo sapiens
Manually annotated by BRENDA team
Collenburg, L.; Beyersdorf, N.; Wiese, T.; Arenz, C.; Saied, E.M.; Becker-Flegler, K.A.; Schneider-Schaulies, S.; Avota, E.
The activity of the neutral sphingomyelinase is important in T cell recruitment and directional migration
Front. Immunol.
8
1007
2017
Homo sapiens
Manually annotated by BRENDA team
Gorelik, A.; Liu, F.; Illes, K.; Nagar, B.
Crystal structure of the human alkaline sphingomyelinase provides insights into substrate recognition
J. Biol. Chem.
292
7087-7094
2017
Homo sapiens (Q6UWV6), Homo sapiens
Manually annotated by BRENDA team
Xiong, Z.J.; Huang, J.; Poda, G.; Pomes, R.; Prive, G.G.
Structure of human acid sphingomyelinase reveals the role of the saposin domain in activating substrate hydrolysis
J. Mol. Biol.
428
3026-3042
2016
Homo sapiens (P17405), Homo sapiens
Manually annotated by BRENDA team