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Information on EC 3.1.4.12 - sphingomyelin phosphodiesterase and Organism(s) Mus musculus and UniProt Accession Q9JJY3

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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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This record set is specific for:
Mus musculus
UNIPROT: Q9JJY3
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
-
neutral sphingomyelinase 2
-
neutral sphingomyelinase-2
-
sphingomyelin phosphodiesterase 3
-
acid SMase
-
-
acid sphingomyelinase
acid sphingomyelinase-like phosphodiesterase 3B
-
acid-SMase
-
-
acidic sphingomyelinase
-
-
alk-SMase
-
-
alkaline sphingomyelinase
aSMase
Beta-hemolysin
-
-
-
-
Beta-toxin
-
-
-
-
Lyso-PAF-PLC
-
-
-
-
MA-nSMase
-
magnesium-dependent neutral sphingomyelinase
-
-
mitochondrial-associated neutral sphingomyelinase
-
mnSMase
-
-
N-SMase
neutral SMase
-
-
neutral sphingomyelinase
neutral sphingomyelinase 2
-
-
nSMase
-
-
-
-
phosphodiesterase, sphingomyelin
-
-
-
-
SMase
SMPLC
-
-
-
-
sphingomyelin phosphodiesterase
-
-
-
-
sphingomyelin phosphodiesterase 5
-
sphingomyelinase
sphingomyelinase C
-
-
-
-
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
a sphingomyelin + H2O
a ceramide + phosphocholine
show the reaction diagram
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
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
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
bis(4-nitrophenyl)phosphate + H2O
?
show the reaction diagram
CDP-choline + H2O
CMP + phosphorylcholine
show the reaction diagram
-
-
-
?
sphingomyelin + H2O
?
show the reaction diagram
-
-
-
-
?
sphingomyelin + H2O
ceramide + phosphocholine
show the reaction diagram
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
show the reaction diagram
-
-
-
?
sphingomyelin + H2O
N-acylsphingosine + 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 + phosphocholine
show the reaction diagram
-
a ceramide is an N-acylsphingosine
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
show the reaction diagram
-
-
?
a sphingomyelin + H2O
a ceramide + phosphocholine
show the reaction diagram
-
-
a ceramide is an N-acylsphingosine
-
?
sphingomyelin + H2O
?
show the reaction diagram
-
-
-
-
?
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
Mn2+
can replace Mg2+, maximal activation at 1-2 mM, slight inhibition above
Ca2+
-
-
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
inhibits almost 90% of the activity at 3 mM
GW4869
0.015 mM, 40% inhibition, 0.045 mM, 70% inhibition
hydrogen peroxide
-
Mn2+
slight inhibition above 2 mM
oxidized glutathione
-
Triton X-100
inhibits almost 90% of the activity at 0.1%
1-aminodecylidene bis-phosphonic acid
-
3-O-methylsphingomyelin
-
-
amitriptyline
-
-
Ca2+
-
-
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
glutathione
-
then oxidized
GW4869
-
-
imipramine
Mn2+
-
above 0.5 mM
Ni2+
-
-
scyphostatin
-
isolated from Discomycetes, specifically inhibits N-SMases
Triton X-100
-
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
activates in vivo by severalfold
cardiolipin
0.1 mM, approx. 40fold activation
DTT
activates in vivo by severalfold
glutathione
activates in vivo by severalfold
phosphatidylserine
0.1-0.15 mM, approx. 40fold activation
Triton X-100
required for activity, maximal activation at 0.1%
2-mercaptoethanol
-
-
anionic phospholipids
-
APLs, the enzymatic activity of nSMase2 is dependent on anionic phospholipids, structural requirements for APL-selective binding of nSMase2, overview. nSMase2 interacts specifically and directly with several APLs, including phosphatidylserine and phosphatidic acid. Identification of two discrete APL binding domains in the N terminus of nSMase2, the nSMase2 N-terminal domain is essential for nSMase interaction with APLs
-
arachidonic acid
-
approx. 3fold activation at 0.5 mM
cardiolipin
enzymatic activity is induced 23fold at 0.1 mM
dithiothreitol
-
activation in a dose dependent manner
phosphatidylglycerol
enzymatic activity is induced 8fold at 0.1 mM
phosphatidylserine
enzymatic activity is induced 15fold at 0.1 mM
reduced glutathione
-
activation in a dose dependent manner
sphingomyelin
-
dietary sphingomyelin increases the alk-Smase activity in the colon by 65%, the increased activity is associated with increased protein and mRNA expression
TNFalpha
-
activates the enzyme, which is prevented by pentoxifylline
-
Triton X-100
-
-
tumor necrosis factor
-
there is a significant increase in ASMase activity after treatment of MVEC cells with tmor necrosis factor
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027
sphingomyelin
37°C, pH 7.4, recombinant nSMase2 in yeast microsomes
0.00059
sphingomyelin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7
-
neutral sphingomyelinase
7.5
the MA-nSMase has no acid SMase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
murine macrophage cell line
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
-
alk-SMase
Manually annotated by BRENDA team
-
unchanged A-SMase activity in the outer epidermis of chronologically aged skin, in the lower epidermis the activity is reduced
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
immortalized hippocampal neuron
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
cell line
Manually annotated by BRENDA team
-
isolated from bone marrow or peritoneal lavage of gene-targeted mice lacking Asm and their wild-type littermates
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
acid-SMase activity is comparable in lung and intestine
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
localizes to the lumen of endosomes
Manually annotated by BRENDA team
-
localizes to the lumen of phagosomes
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
neutral sphingomyelinase-2 is the major sphingomyelinase activated in response to proinflammatory cytokines and during oxidative stress. The enzyme may be a novel substrate for thioredoxin
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NSMA2_MOUSE
655
2
71197
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
40000
-
2 * 40000, SDS-PAGE and Western blotting analysis
42000
-
x * 42000, SDS-PAGE
47500
-
x * 47500, deduced from nucleotide sequence
50000
SDS-PAGE
53870
calculated from amino acid sequence
68000
-
gel filtration or gel electrophoresis
90000 - 100000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 74000, SDS-PAGE
monomer
1 * 74000, SDS-PAGE
trimer
3 * 74000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE and Western blotting analysis
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the protein has five sites of N-glycosylation
no glycoprotein
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme and in complex with phosphorylcholine, hanging drop vapor diffusion method, using 0.2 M NH4NO3 and 25% (w/v) PEG 3350
sitting drop vapor diffusion method, using 0.2M lithium acetate and 20% (w/v) PEG 3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C617S
site-directed mutagenesis, gain-of-function mutation associated with a decreased propensity for oligomerization
F388R
the mutant shows reduced activity with sphingomyelin and bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme
H135A
almost inactive
H280A
inactive with sphingomyelin and bis(4-nitrophenyl)phosphate as substrate
H317A
inactive with sphingomyelin as substrate, but active with bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme
K140M
the mutant shows reduced activity compared to the wild type enzyme
K140M/N141A
almost inactive
L391R
the mutant shows about 20% activity with sphingomyelin and about 50% activity with bis(4-nitrophenyl)phosphate as substrate, as compared to the wild type enzyme
N141A
the mutant shows reduced activity compared to the wild type enzyme
N200A
the mutant shows increased activity compared to the wild type enzyme
P321E
the mutant shows reduced activity with sphingomyelin and almost no activity with bis(4-nitrophenyl)phosphate as substrate, compared to the wild type enzyme
V128E
the mutant shows about 20% activity with sphingomyelin and about 70% activity with bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme
V143R
the mutant shows about 5% activity with sphingomyelin and about 65% activity with bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme
W283N
the mutant shows reduced activity with sphingomyelin and bis(4-nitrophenyl)phosphate as substrate as compared to the wild type enzyme
Y198F
the mutant shows reduced activity compared to the wild type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
-
20 min, 40% activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme-2-FLAG-6xHis construct from Escherichia coli by affinity chromatography
10fold
-
64fold
-
affinity purification of recombinant mnSMase
-
Ni-NTA resin column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of nSMase2 in Saccharomyces cerevisiae and MCF7 breast cancer cells
gene SMPD3, expression of GFP-tagged and of N-terminally RFP-tagged enzyme in HEK-293-IL1R cells, recombinant expression of C-terminally FLAG-tagged enzyme and of enzyme-2-FLAG-6xHis construct in wildtype Escherichia coli strain Rosetta-gami2, and the mutated strain lacking endogenous thioredoxin, results in increased oligomer formation and lower enzyme activity, the phenotype can be rescued by with recombinant human thioredoxin
cloning of cDNA, expression in HEK293 kidney cells
-
expressed in HEK-293 cells and MCF-7 cells
expressed in Sf9 cells
expressed in Sf9 cells and RAW264.7 cells
expression in Escherichia coli and HEK293 kidney cells
-
expression of (E)GFP-fused wild-type nSMase2 and of several (E)GFP-fused truncated mutant nSMase2s possessing additional V5- or FLAG-tags in HEK-293 or MCF-7 cells
-
isozymes nSMase1 and nSMase2, overexpression of nSMase2 increases the shpingomyelin metabolism while overexpression of nSMase1 has no effect
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of tumor necrosis factor-alpha, interleukin-1beta, interferon-gamma, and lipopolysaccharide to C2C12 cells elicits significant increases in enzyme activity levels
-
ASM is NFAT2-inducible
-
stimulation of bone marrow-derived mast cells with antigen results in about 2.5fold induction of enzyme activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
-
the enzyme is a potential target in the treatment of allergic reactions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Pentchev, P.G.; Gal, A.E.; Booth, A.D.; Omodeo-Sale, F.; Fouks, J.; Neumeyer, B.A.; Quirk, J.M.; Dawson, G.; Brady, R.O.
A lysosomal storage disorder in mice characterized by a dual deficiency of sphingomyelinase and glucocerebrosidase
Biochim. Biophys. Acta
619
669-679
1980
Mus musculus
Manually annotated by BRENDA team
Fensome, A.C.; Rodrigues-Lima, F.; Josephs, M.; Paterson, H.F.; Katan, M.
A neutral magnesium-dependent sphingomyelinase isoform associated with intracellular membranes and reversibly inhibited by reactive oxygen species
J. Biol. Chem.
275
1128-1136
2000
Mus musculus
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
Marchesini, N.; Luberto, C.; Hannun, Y.A.
Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
J. Biol. Chem.
278
13775-13783
2003
Mus musculus (Q9JJY3), Mus musculus
Manually annotated by BRENDA team
Jensen, J.M.; Forl, M.; Winoto-Morbach, S.; Seite, S.; Schunck, M.; Proksch, E.; Schutze, S.
Acid and neutral sphingomyelinase, ceramide synthase, and acid ceramidase activities in cutaneous aging
Exp. Dermatol.
14
609-618
2005
Mus musculus
Manually annotated by BRENDA team
Albi, E.; Cataldi, S.; Bartoccini, E.; Magni, M.V.; Marini, F.; Mazzoni, F.; Rainaldi, G.; Evangelista, M.; Garcia-Gil, M.
Nuclear sphingomyelin pathway in serum deprivation-induced apoptosis of embryonic hippocampal cells
J. Cell. Physiol.
206
189-195
2006
Mus musculus
Manually annotated by BRENDA team
Soloviev, A.; Schwarz, E.M.; Darowish, M.; O'Keefe, R.J.
Sphingomyelinase mediates macrophage activation by titanium particles independent of phagocytosis: a role for free radicals, NFkappaB, and TNFalpha
J. Orthop. Res.
23
1258-1265
2005
Mus musculus
Manually annotated by BRENDA team
AAubin, I.; Adams, C.P.; Opsahl, S.; Septier, D.; Bishop, C.E.; Auge, N.; Salvayre, R.; Negre-Salvayre, A.; Goldberg, M.; Guenet, J.L.; Poirier, C.
A deletion in the gene encoding sphingomyelin phosphodiesterase 3 (Smpd3) results in osteogenesis and dentinogenesis imperfecta in the mouse
Nat. Genet.
37
803-805
2005
Mus musculus (Q9JJY3), Mus musculus
Manually annotated by BRENDA team
Stoffel, W.; Jenke, B.; Block, B.; Zumbansen, M.; Koebke, J.
Neutral sphingomyelinase 2 (smpd3) in the control of postnatal growth and development
Proc. Natl. Acad. Sci. USA
102
4554-4559
2005
Mus musculus (Q9JJY3), Mus musculus
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
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
Llacuna, L.; Mari, M.; Garcia-Ruiz, C.; Fernandez-Checa, J.C.; Morales, A.
Critical role of acidic sphingomyelinase in murine hepatic ischemia-reperfusion injury
Hepatology
44
561-572
2006
Mus musculus
Manually annotated by BRENDA team
McCollister, B.D.; Myers, J.T.; Jones-Carson, J.; Voelker, D.R.; Vazquez-Torres, A.
Constitutive acid sphingomyelinase enhances early and late macrophage killing of Salmonella enterica serovar Typhimurium
Infect. Immun.
75
5346-5352
2007
Mus musculus
Manually annotated by BRENDA team
Zhang, P.; Li, B.; Gao, S.; Duan, R.D.
Dietary sphingomyelin inhibits colonic tumorigenesis with an up-regulation of alkaline sphingomyelinase expression in ICR mice
Anticancer Res.
28
3631-3635
2009
Mus musculus
Manually annotated by BRENDA team
Schramm, M.; Herz, J.; Haas, A.; Kroenke, M.; Utermoehlen, O.
Acid sphingomyelinase is required for efficient phago-lysosomal fusion
Cell. Microbiol.
10
1839-1853
2008
Mus musculus
Manually annotated by BRENDA team
Bianco, F.; Perrotta, C.; Novellino, L.; Francolini, M.; Riganti, L.; Menna, E.; Saglietti, L.; Schuchman, E.H.; Furlan, R.; Clementi, E.; Matteoli, M.; Verderio, C.
Acid sphingomyelinase activity triggers microparticle release from glial cells
EMBO J.
28
1043-1054
2009
Mus musculus
Manually annotated by BRENDA team
Zhang, Y.; Li, X.; Carpinteiro, A.; Gulbins, E.
Acid sphingomyelinase amplifies redox signaling in Pseudomonas aeruginosa-induced macrophage apoptosis
J. Immunol.
181
4247-4254
2008
Mus musculus
Manually annotated by BRENDA team
Ohlsson, L.; Hjelte, L.; Huehn, M.; Scholte, B.J.; Wilke, M.; Flodstroem-Tullberg, M.; Nilsson, A.
Expression of intestinal and lung alkaline sphingomyelinase and neutral ceramidase in cystic fibrosis f508del transgenic mice
J. Pediatr. Gastroenterol. Nutr.
47
547-554
2008
Mus musculus
Manually annotated by BRENDA team
Henkes, L.E.; Sullivan, B.T.; Lynch, M.P.; Kolesnick, R.; Arsenault, D.; Puder, M.; Davis, J.S.; Rueda, B.R.
Acid sphingomyelinase involvement in tumor necrosis factor alpha-regulated vascular and steroid disruption during luteolysis in vivo
Proc. Natl. Acad. Sci. USA
105
7670-7675
2008
Mus musculus
Manually annotated by BRENDA team
von Bismarck, P.; Wistaedt, C.F.; Klemm, K.; Winoto-Morbach, S.; Uhlig, U.; Schuetze, S.; Adam, D.; Lachmann, B.; Uhlig, S.; Krause, M.F.
Improved pulmonary function by acid sphingomyelinase inhibition in a newborn piglet lavage model
Am. J. Respir. Crit. Care Med.
177
1233-1241
2008
Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Wu, B.X.; Rajagopalan, V.; Roddy, P.L.; Clarke, C.J.; Hannun, Y.A.
Identification and characterization of murine mitochondrial-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5
J. Biol. Chem.
285
17993-18002
2010
Mus musculus (D6MZJ6), Mus musculus
Manually annotated by BRENDA team
Bao, X.; Ogawa, T.; Se, S.; Akiyama, M.; Bahtiar, A.; Takeya, T.; Ishida-Kitagawa, N.
Acid sphingomyelinase regulates osteoclastogenesis by modulating sphingosine kinases downstream of RANKL signaling
Biochem. Biophys. Res. Commun.
405
533-537
2011
Mus musculus
Manually annotated by BRENDA team
Osawa, Y.; Seki, E.; Kodama, Y.; Suetsugu, A.; Miura, K.; Adachi, M.; Ito, H.; Shiratori, Y.; Banno, Y.; Olefsky, J.M.; Nagaki, M.; Moriwaki, H.; Brenner, D.A.; Seishima, M.
Acid sphingomyelinase regulates glucose and lipid metabolism in hepatocytes through AKT activation and AMP-activated protein kinase suppression
FASEB J.
25
1133-1144
2011
Mus musculus, Mus musculus C57/BL6J, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Wu, B.X.; Clarke, C.J.; Matmati, N.; Montefusco, D.; Bartke, N.; Hannun, Y.A.
Identification of novel anionic phospholipid binding domains in neutral sphingomyelinase 2 with selective binding preference
J. Biol. Chem.
286
22362-22371
2011
Mus musculus
Manually annotated by BRENDA team
Dotson Ii, P.P.; Karakashian, A.A.; Nikolova-Karakashian, M.N.
Neutral sphingomyelinase-2 is a redox sensitive enzyme: role of catalytic cysteine residues in regulation of enzymatic activity through changes in oligomeric state
Biochem. J.
465
371-382
2015
Mus musculus (Q9JJY3), Mus musculus
Manually annotated by BRENDA team
Yang, W.; Schmid, E.; Nurbaeva, M.K.; Szteyn, K.; Leibrock, C.; Yan, J.; Schaller, M.; Gulbins, E.; Shumilina, E.; Lang, F.
Role of acid sphingomyelinase in the regulation of mast cell function
Clin. Exp. Allergy
44
79-90
2014
Mus musculus
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
Supinski, G.S.; Alimov, A.P.; Wang, L.; Song, X.H.; Callahan, L.A.
Neutral sphingomyelinase 2 is required for cytokine-induced skeletal muscle calpain activation
Am. J. Physiol. Lung Cell Mol. Physiol.
309
L614-L624
2015
Mus musculus
Manually annotated by BRENDA team
Gorelik, A.; Heinz, L.X.; Illes, K.; Superti-Furga, G.; Nagar, B.
Crystal structure of the acid sphingomyelinase-like phosphodiesterase SMPDL3B provides insights into determinants of substrate specificity
J. Biol. Chem.
291
24054-24064
2016
Mus musculus (P58242), Mus musculus
Manually annotated by BRENDA team
Gorelik, A.; Illes, K.; Heinz, L.X.; Superti-Furga, G.; Nagar, B.
Crystal structure of mammalian acid sphingomyelinase
Nat. Commun.
7
12196
2016
Mus musculus (Q04519)
Manually annotated by BRENDA team