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Information on EC 3.1.4.12 - sphingomyelin phosphodiesterase and Organism(s) Bacillus cereus and UniProt Accession P09599
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3.1.4.12 sphingomyelin phosphodiesteraseIUBMB Comments
Has very little activity on phosphatidylcholine.
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Word Map
- 3.1.4.12
- aureus
- lysosomal
- sphingolipids
- niemann-pick
- cholesterol
-
staphylococcal
- necrosis
- clostridium
- phospholipid
- endothelial
- sphingosine
- perfringens
- phosphatidylcholine
- erythrocyte
-
permeabilized
- ceramidase
-
raft
-
hemolytic
- tnf-alpha
- c2-ceramide
-
bilayer
-
pore-forming
- sphingosine-1-phosphate
- venom
-
cell-permeable
- phosphatidylserine
- desipramine
- scorpion
- glucosylceramide
-
microdomains
- enterotoxin
-
ceramide-induced
- phospholipases
- fumonisin
- phosphorylcholine
-
hepatosplenomegaly
- amitriptyline
- imipramine
- gangrene
-
cytolysin
-
dermonecrosis
- glucocerebrosidase
- pc-plc
- gaucher
-
phosphatidylcholine-specific
-
leukocidins
- lecithinase
- coagulase
- pharmacology
-
nonhemolytic
- drug development
- diagnostics
- medicine
-
transbilayer
The taxonomic range for the selected organisms is: Bacillus cereus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid sphingomyelinase
alkaline sphingomyelinase
-
-
-
-
aSMase
Bc-SMase
Beta-hemolysin
-
-
-
-
Beta-toxin
-
-
-
-
Lyso-PAF-PLC
-
-
-
-
N-SMase
-
-
-
-
neutral sphingomyelinase
nSMase
phosphodiesterase, sphingomyelin
-
-
-
-
SMase
SMPLC
-
-
-
-
sphingomyelin phosphodiesterase
-
-
-
-
sphingomyelinase
sphingomyelinase C
acid sphingomyelinase
-
-
-
-
aSMase
-
-
-
-
neutral sphingomyelinase
-
-
-
-
nSMase
-
-
-
-
SMase
-
-
-
-
sphingomyelinase
-
-
-
-
sphingomyelinase
-
-
sphingomyelinase C
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a sphingomyelin + H2O = a ceramide + phosphocholine
catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases, e.g. Glu53, Asp126, Asp295, and His296 are essential, structure-function analysis, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
additional information
-
SMase belongs to the family of interfacial enzymes that carry out processive catalytic turnover at the interface, SMase binds rapidly and avidly to sphingomyelin vesicles and it is fully active as a monomer at the interface
SYSTEMATIC NAME
IUBMB Comments
sphingomyelin cholinephosphohydrolase
Has very little activity on phosphatidylcholine.
CAS REGISTRY NUMBER
COMMENTARY
9031-54-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hexadecanoylamino-4-nitrophenylphosphocholine + H2O
2-hexadecanoylamino-4-nitrophenol + choline phosphate
2-n-hexadecanoylamino-4-nitrophenylphosphorylcholine + H2O
2-n-hexadecanoylamino-4-nitrophenol + choline phosphate
-
-
-
-
?
4-nitrophenyl phosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
-
-
-
-
?
a sphingomyelin + H2O
a ceramide + phosphocholine
-
-
a ceramide is an N-acylsphingosine
-
?
hexadecanoyl-p-nitrophenylphosphorylcholine + H2O
hexadecanoyl-p-nitrophenol + choline phosphate
-
-
-
-
?
lysophosphatidylcholine + H2O
acylglycerol + choline phosphate
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
choline phosphate + p-nitrophenol
-
-
-
-
?
sphingosylphosphocholine + H2O
sphingosine + choline phosphate
-
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
residues Glu53, Asp126, Asp295, and His296 are critical for Mg2+ binding and catalytic activity
-
-
?
2-hexadecanoylamino-4-nitrophenylphosphocholine + H2O
2-hexadecanoylamino-4-nitrophenol + choline phosphate
-
-
-
?
2-hexadecanoylamino-4-nitrophenylphosphocholine + H2O
2-hexadecanoylamino-4-nitrophenol + choline phosphate
-
-
-
?
lysophosphatidylcholine + H2O
1-acylglycerol + choline phosphate
-
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
-
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
cholesterol activation of sphingomyelinase and the strong affinity of cholesterol for sphingomyelin allows the rapid, localized and self-contained production of the metabolic signal ceramide in specific microdomains
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
the rapid insect toxicity of sphingomyelinase C results from its phospholipid degrading activity
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
hydrolysis of sphingomyelin dispersed in diheptanoylphosphatidyl-choline. Premicellar complexes of sphingomyelinase mediate enzyme exchange for the stationary phase turnover
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
changes in the initial composition and topography of mixed monolayers of sphingomyelin and ceramide modulate the sphingomyelin degradation by the enzyme, overview, the enzyme in an extracellular toxin that exhibits potent hemolytic activity against sphingomyelin-rich erythrocytes in mammals
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
Smase cleaves sphingomyelin at the outer leaflet of the plasma membrane, generating phosphocholine and ceramide
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
SMase shows very low activity against condensed sphingomyelin, but is active on loosely organized sphingomyelin in bilayers and monolayers, overview
-
-
?
additional information
?
-
cytotoxic action of bacterial SMases by their hemolytic activity to human erythrocytes, occuring through hydrolysis of the erythrocyte cell surface sphingomyelin, the hemolytic activity of bacterial SMases is increased by cooperative and synergistic interactions among virulence factors secreted by the same bacteria, cytotoxic mechanism, overview
-
-
?
additional information
?
-
-
exogenous neutral sphingomyelinase-induced ceramide triggers germinal vesicle breakdown and oxidant-dependent apoptosis in Xenopus laevis oocytes, which can be prevented by pre-incubation of the cells with GSH-ethyl ester, overview
-
-
?
additional information
?
-
-
sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion at a step in the fusion process after CD4 engagement, but sphingomyelinase treatment of cells does not influence gp120 binding, HIV-1 attachment, or fluid-phase and receptor-mediated endocytosis, and furthermore, sphingomyelinase treatment does not affect the membrane disposition of the HIV receptor proteins CD4, CXCR4, and CCR5, Smase treatment does not influence Triton X-100 extraction of HIV-1 receptor proteins, overview
-
-
?
additional information
?
-
-
Smase mediates ceramide formation from low density lipoprotein-sphingomyelin
-
-
?
additional information
?
-
-
the enzyme's beta-hairpin site directly binds to gangliosides, especially ganglioside GM3, i,e, NeuAca2-3Galbeta1-4Glcbeta1-1ceramide through a carbohydrate moiety. Binding response of the enzyme to liposomes containing GM3 is about 15fold higher than that to liposomes lacking GM3. Residues Trp-284 and Phe-285 in the beta-hairpin play an important role in the interaction with GM3
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview
-
-
?
a sphingomyelin + H2O
a ceramide + phosphocholine
-
-
a ceramide is an N-acylsphingosine
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
cholesterol activation of sphingomyelinase and the strong affinity of cholesterol for sphingomyelin allows the rapid, localized and self-contained production of the metabolic signal ceramide in specific microdomains
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
the rapid insect toxicity of sphingomyelinase C results from its phospholipid degrading activity
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
changes in the initial composition and topography of mixed monolayers of sphingomyelin and ceramide modulate the sphingomyelin degradation by the enzyme, overview, the enzyme in an extracellular toxin that exhibits potent hemolytic activity against sphingomyelin-rich erythrocytes in mammals
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
Smase cleaves sphingomyelin at the outer leaflet of the plasma membrane, generating phosphocholine and ceramide
-
-
?
additional information
?
-
cytotoxic action of bacterial SMases by their hemolytic activity to human erythrocytes, occuring through hydrolysis of the erythrocyte cell surface sphingomyelin, the hemolytic activity of bacterial SMases is increased by cooperative and synergistic interactions among virulence factors secreted by the same bacteria, cytotoxic mechanism, overview
-
-
?
additional information
?
-
-
exogenous neutral sphingomyelinase-induced ceramide triggers germinal vesicle breakdown and oxidant-dependent apoptosis in Xenopus laevis oocytes, which can be prevented by pre-incubation of the cells with GSH-ethyl ester, overview
-
-
?
additional information
?
-
-
sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion at a step in the fusion process after CD4 engagement, but sphingomyelinase treatment of cells does not influence gp120 binding, HIV-1 attachment, or fluid-phase and receptor-mediated endocytosis, and furthermore, sphingomyelinase treatment does not affect the membrane disposition of the HIV receptor proteins CD4, CXCR4, and CCR5, Smase treatment does not influence Triton X-100 extraction of HIV-1 receptor proteins, overview
-
-
?
additional information
?
-
-
Smase mediates ceramide formation from low density lipoprotein-sphingomyelin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
required by N-SMase for activity, residues Glu53, Asp126, Asp295, and His296 are critical for Mg2+ binding and catalytic activity
Zn2+
Zn2+ binding to the high-affinity site activates the enzyme and, conversely, binding to the low-affinity site inhibits the enzyme
Ca2+
Co2+
Mg2+
Mn2+
Sr2+
Km: 0.018 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+
Zn2+
additional information
Ca2+
Km: 0.0191 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+
Co2+
Km: 0.142 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+. There are three distinct metal ion-binding sites in a long horizontal cleft across the bc-SMase molecule
Co2+
-
rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
Mg2+
-
two-step activation, high-affinity binding site with 50% saturation at 0.0041 mM, low-affinity-binding site with 50% saturation at 20 mM, approx. 5fold activation at 20 mM
Mg2+
Km: 0.0161 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+
Mg2+
-
rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
Mg2+
-
the enzyme is a Mg2+-dependent neutral sphingomyelinase with two metal ion-binding sites in a long horizontal cleft across the molecule, with one Mg2+ in the central region of the cleft and one divalent metal ion at the side-edge of the cleft. The Mg2+ at the side-edge of the enzyme plays an important role in the binding to membranes
Mn2+
Km: 0.0149 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+
Mn2+
-
rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
Zn2+
-
rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
Zn2+
-
the enzyme possesses at least two different binding sites for Zn2+. Zn2+ binding to the high affinity site can activate the enzyme, whereas the Zn2+ binding to the low-affinity site can activate the enzyme. Binding of the substrate to the enzyme is independent of the Zn2+ binding to the high-affinity site, but is competitively inhibited by the Zn2+ binding to the low-affinity site. Rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
Zn2+ binding to the high-affinity site activates the enzyme and, conversely, binding to the low-affinity site inhibits the enzyme
N-[(2S,3R,4E)-1-(2,2'-bipyridin-6-ylmethoxy)-3-hydroxyoctadec-4-en-2-yl]hexanamide [Mg2+]
-
i.e. RY221B-a, synthesis, binding simulations and docking study, overview
N-[(2S,3R,4E)-3-(2,2'-bipyridin-6-ylmethoxy)-1-hydroxyoctadec-4-en-2-yl]hexanamide
-
i.e. RY221B-b, synthesis, binding simulations and docking study, overview
Triton X-100
-
slight inhibition with 2-hexadecynoylamino-4-nitrophenylphosphorylcholine
Ca2+
-
when sphingomyelin as substrate with Triton X-100 is used, competitive inhibitor against Mg2+
Zn2+
-
0.0042 mM, 50% inhibitiion, higher concentrations of Mg2+ slighty restore activity
Zn2+
-
the enzyme possesses at least two different binding sites for Zn2+. Zn2+ binding to the high affinity site can activate the enzyme, whereas the Zn2+ binding to the low-affinity site can activate the enzyme. Binding of the substrate to the enzyme is independent of the Zn2+ binding to the high-affinity site, but is competitively inhibited by the Zn2+ binding to the low-affinity site. Rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule
additional information
-
neuraminidase from Clostridium perfringens inhibits the binding of the enzyme to mouse peritoneal macrophages
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cholesterol
-
sphingomyelinase activity is higher in the cholesterol-induced liquid-ordered phase than in the gel phase
additional information
-
the topography of the lipid monolayer surface, through phase connection-disconnection of substrate-enriched or substrate-depleted domains, can dynamically regulate SMase activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.034
2-n-hexadecanoylamino-4-nitrophenylphosphorylcholine
-
in presence of Mg2+
additional information
additional information
-
different SMase kinetic steps are differentially regulated by non-substrate lipids, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0052
N-[(2S,3R,4E)-1-(2,2'-bipyridin-6-ylmethoxy)-3-hydroxyoctadec-4-en-2-yl]hexanamide [Mg2+]
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
N-[(2S,3R,4E)-1-(2,2'-bipyridin-6-ylmethoxy)-3-hydroxyoctadec-4-en-2-yl]hexanamide [Mg2+]
Bacillus cereus
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
nSMase, with a cleavable secretory signal sequence at their N-terminus, is a secretory protein released from cells
-
-
extracellular soluble toxin that induces hemolysis by acting on sphingomyelin-rich erythrocytes of mammals such as ruminants
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme knockdown reduces Clostridium botulinum C2 toxin-induced cell rounding
physiological function
physiological function
-
in HepG2 cells SMase treatment significantly enhances the esterification of cholesterol by a 50% with respect to control cells
physiological function
-
the enzyme is a virulence factor for septicemia. Ganglioside GM3 is the primary cellular receptor for the enzyme, and the beta-hairpin region is the tethering region for gangliosides
physiological function
-
Clostridium botulinum C2 toxin requires acid sphingomyelinase activity during internalization into cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme structure and topology influences the enzyme activity, overview
additional information
-
the enzyme contains the central site (catalytic site), side-edge site (membrane binding site), and beta-hairpin region (membrane binding site)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nSMase, crystal structure of nSMase complexed with Ca2+, Co2+, or Mg2+, and structure-function analysis
hanging drop vapor diffusion method, crystal structures of Bc-SMase complexed to the functional metal ions Mg2+, Co2+, or Ca2+ are determined at 1.8 A, 1.8 A, and 1.4 A resolution, respectively
purified recombinant mutant N57A enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH7.0, with 0.002 ml of reservoir solution containing 18% w/v PEG 8000, 0.2 M MgCl2, and 0.1 M sodium cacodylate, pH 6.5, 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D100A
-
site-directed mutagenesis, mutation in close proximity to Mg2+ at the side-edge, the mutant shows reduced binding to and hydrolysis of sphingomyelin in membranes of sheep erythrocytes or SM-liposomes, similar catalytic activity compared to the wild-type enzyme
E53A
E53D
-
5% of wild-type sphingomyelin hydrolyzing activity, E53 acts as an indespensable ligand of Mg2+ essential for catalytic activity
E53Q
-
no sphingomyelin hydrolyzing and no hemolytic activity, E53 acts as an indespensable ligand of Mg2+ essential for catalytic activity
E99A
-
site-directed mutagenesis, mutation in close proximity to Mg2+ at the side-edge, the mutant shows reduced binding to and hydrolysis of sphingomyelin in membranes of sheep erythrocytes or SM-liposomes, similar catalytic activity compared to the wild-type enzyme
F285A
F55A
-
site-directed mutagenesis, the mutation in close proximity to Mg2+ at the side-edge does not affect the enzyme
H151A
N57A
-
site-directed mutagenesis, mutation in close proximity to Mg2+ at the side-edge, the mutant shows reduced binding to and hydrolysis of sphingomyelin in membranes of sheep erythrocytes or SM-liposomes, mutant N57A loses the metal ion at the side-edge, similar catalytic activity compared to the wild-type enzyme
W284A
additional information
E53A
-
no sphingomyelin hydrolyzing and no hemolytic activity, E53 acts as an indespensable ligand of Mg2+ essential for catalytic activity
F285A
catalytic activity of the mutant enzyme is below the detection limit, affinity of mutant enzyme to sphingomyelin liposomes are much weaker than the wild-type enzyme
F285A
-
site-directed mutagenesis, binding of the mutant enzyme to mouse macrophages decreases markedly in comparison to the binding by wild-type enzyme
H151A
-
mutation inactivates the sphingomyelinase activity and also abolishes the insecticidal activity
W284A
catalytic activity of the mutant enzyme is below the detection limit, affinity of mutant enzyme to sphingomyelin liposomes are much weaker than the wild-type enzyme
W284A
-
site-directed mutagenesis, binding of the mutant enzyme to mouse macrophages decreases markedly in comparison to the binding by wild-type enzyme
additional information
mutation of the two histidines, His134 and His252, abolished enzyme activity
additional information
-
microinjection of the Bacillus cereus neutral sphingomyelinase in Xenopus laevis oocytes results in increased ceramide levels and triggered germinal vesicle breakdown and oxidant-dependent apoptosis, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Bacillus subtilis strain ISW1214
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tomita, M.; Taguchi, R.; Ikezawa, H.
Molecular properties and kinetic studies on sphingomyelinase of Bacillus cereus
Biochim. Biophys. Acta
704
90-99
1982
Bacillus cereus
Ikezawa, H.; Mori, M.; Ohyabu, T.; Taguchi, R.
Studies on sphingomyelinase of Bacillus cereus. I. Purification and properties
Biochim. Biophys. Acta
528
247-256
1978
Bacillus cereus
Yu, B.Z.; Zakim, D.; Jain, M.K.
Processive interfacial catalytic turnover by Bacillus cereus sphingomyelinase on sphingomyelin vesicles
Biochim. Biophys. Acta
1583
122-132
2002
Bacillus cereus
Obama, T.; Fujii, S.; Ikezawa, H.; Ikeda, K.; Imagawa, M.; Tsukamoto, K.
His151 and His296 are the acid-base catalytic residues of Bacillus cereus sphingomyelinase in sphingomyelin hydrolysis
Biol. Pharm. Bull.
26
920-926
2003
Bacillus cereus
Fanani, M.L.; Hartel, S.; Oliveira, R.G.; Maggio, B.
Bidirectional control of sphingomyelinase activity and surface topography in lipid monolayers
Biophys. J.
83
3416-3424
2002
Bacillus cereus
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
Obama, T.; Kan, Y.; Ikezawa, H.; Imagawa, M.; Tsukamoto, K.
Glu-53 of Bacillus cereus sphingomyelinase acts as an indispensable ligand of Mg2+ essential for catalytic activity
J. Biochem.
133
279-286
2003
Bacillus cereus
Fanani, M.L.; Maggio, B.
Kinetic steps for the hydrolysis of sphingomyelin by Bacillus cereus sphingomyelinase in lipid monolayers
J. Lipid Res.
41
1832-1840
2000
Bacillus cereus
Itoh, F.S.; Yoshida, A.; Higashi, S.; Ikezawa, H.; Ikeda, K.
Activation of sphingomyelinase from Bacillus cereus by Zn2+ hitherto accepted as a strong inhibitor
Arch. Biochem. Biophys.
43
227-236
2005
Bacillus cereus
-
Yu, B.Z.; Polenova, T.; Jain, M.K.; Berg, O.G.
Premicellar complexes of sphingomyelinase mediate enzyme exchange for the stationary phase turnover
Biochim. Biophys. Acta
1712
137-151
2005
Bacillus cereus
Contreras, F.X.; Sot, J.; Ruiz-Arguello, M.B.; Alonso, A.; Goni, F.M.
Cholesterol modulation of sphingomyelinase activity at physiological temperatures
Chem. Phys. Lipids
130
127-134
2004
Bacillus cereus
Nishiwaki, H.; Ito, K.; Otsuki, K.; Yamamoto, H.; Komai, K.; Matsuda, K.
Purification and functional characterization of insecticidal sphingomyelinase C produced by Bacillus cereus
Eur. J. Biochem.
271
601-606
2004
Bacillus cereus
Ago, H.; Oda, M.; Takahashi, M.; Tsuge, H.; Ochi, S.; Katunuma, N.; Miyano, M.; Sakurai, J.
Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from bacillus cereus
J. Biol. Chem.
281
16157-16167
2006
Bacillus cereus (P11889), Bacillus cereus
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)
De Tullio, L.; Maggio, B.; Hartel, S.; Jara, J.; Fanani, M.L.
The initial surface composition and topography modulate sphingomyelinase-driven sphingomyelin to ceramide conversion in lipid monolayers
Cell Biochem. Biophys.
47
169-177
2007
Bacillus cereus
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
Finnegan, C.M.; Rawat, S.S.; Cho, E.H.; Guiffre, D.L.; Lockett, S.; Merrill, A.H.; Blumenthal, R.
Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion
J. Virol.
81
5294-5304
2007
Bacillus cereus
Walters, M.J.; Wrenn, S.P.
Effect of sphingomyelinase-mediated generation of ceramide on aggregation of low-density lipoprotein
Langmuir
24
9642-9647
2008
Bacillus cereus
Marco, C.; Jimenez-Lopez, J.M.; Rios-Marco, P.; Segovia, J.L.; Carrasco, M.P.
Hexadecylphosphocholine alters nonvesicular cholesterol traffic from the plasma membrane to the endoplasmic reticulum and inhibits the synthesis of sphingomyelin in HepG2 cells
Int. J. Biochem. Cell Biol.
41
1296-1303
2009
Bacillus cereus
Imagawa, H.; Oda, M.; Takemoto, T.; Yamauchi, R.; Yoshikawa, T.; Yamamoto, H.; Nishizawa, M.; Takahashi, H.; Hashimoto, M.; Yabiku, K.; Nagahama, M.; Sakurai, J.
Synthesis and evaluation of novel phosphate ester analogs as neutral sphingomyelinase inhibitors
Bioorg. Med. Chem. Lett.
20
3868-3871
2010
Bacillus cereus
Oda, M.; Takahashi, M.; Tsuge, H.; Nagahama, M.; Sakurai, J.
Role of side-edge site of sphingomyelinase from Bacillus cereus
Biochem. Biophys. Res. Commun.
422
128-132
2012
Bacillus cereus, Bacillus cereus IAM1029
Oda, M.; Fujita, A.; Okui, K.; Miyamoto, K.; Shibutani, M.; Takagishi, T.; Nagahama, M.
Bacillus cereus sphingomyelinase recognizes ganglioside GM3
Biochem. Biophys. Res. Commun.
431
164-168
2013
Bacillus cereus, Bacillus cereus IAM1029
Caro, C.A.; Lillo, L.; Valenzuela, F.J.; Cabello, G.
Mechanistic characterization and inhibition of sphingomyelinase C over substituted Iron Schiff bases of chitosan adsorbed on glassy carbon electrode
Chem. Biol. Interact.
263
81-87
2017
Bacillus cereus
EXTERNAL LINKS (specific for EC-Number 3.1.4.12)
Transporter Classification Database (TCDB): 1.B.79.1.1, 1.C.67.1.2
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