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Literature summary extracted from

  • Clarke, C.J.; Snook, C.F.; Tani, M.; Matmati, N.; Marchesini, N.; Hannun, Y.A.
    The extended family of neutral sphingomyelinases (2006), Biochemistry, 45, 11247-11256.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.4.12 additional information nSMase1 activity required reducing agents Homo sapiens
3.1.4.12 additional information nSMase2 is activated by anionic phospholipids Homo sapiens
3.1.4.12 phosphatidylglycerol activates nSMase2 Homo sapiens
3.1.4.12 phosphatidylserine activates nSMase2 Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.12 nSMase1, DNA and amino acid sequence determination and analysis Homo sapiens
3.1.4.12 nSMase2, DNA and amino acid sequence determination and analysis, overexpression of nSMase2 in DELTAISC1 yeast cells and in MCF-7 cells Homo sapiens
3.1.4.12 overexpression of nSMase1, the recombinant enzyme shows altered subcellular localization in the endoplasmic reticulum compared to the wild-type nSMase1 localized in the nucleus Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.12 nSMase, crystal structure and structure-function analysis Listeria ivanovii
3.1.4.12 nSMase, crystal structure of nSMase complexed with Ca2+, Co2+, or Mg2+, and structure-function analysis Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.12 additional information construction of SMase knockout mutants, the mutant strain is less virulent for mice than the wild-type strain using an infection model of the mouse mammary gland Listeria ivanovii
3.1.4.12 additional information MCF-7 cells overexpressing nSMase2 exhibit clearly lower sphingomyelin and higher ceramide levels, especially of very long chain ceramides, which correlates with a decrease in the level of C24:0- and C24:1-SM species, than corresponding vector-transfected cells, RNAi inhibitors of nSMase2 inhibit the cytotoxic effects of amyloid-beta peptides Homo sapiens
3.1.4.12 additional information mutation of the two histidines, His134 and His252, abolished enzyme activity Bacillus cereus
3.1.4.12 additional information site-directed mutagenesis indicates that two histidine residues, His136 and His272, are essential for catalysis, overexpression of catalytically inactive nSMase1 has no effect on CD95-induced ceramide production Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.12 BeF2 an unusual phosphate analogue Bacillus cereus
3.1.4.12 Ca2+
-
Bacillus cereus
3.1.4.12 EDTA
-
Bacillus cereus
3.1.4.12 GW4869 specific inhibition Homo sapiens
3.1.4.12 oxidized glutathione reversible inhibition of nSMase1 Homo sapiens
3.1.4.12 peroxynitrite irreversible inhibition of nSMase1 Homo sapiens
3.1.4.12 reactive oxygen species reversible inhibition of nSMase1 Homo sapiens
3.1.4.12 Sr2+
-
Bacillus cereus
3.1.4.12 Zn2+ Zn2+ binding to the high-affinity site activates the enzyme and, conversely, binding to the low-affinity site inhibits the enzyme Bacillus cereus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.12 endoplasmic reticulum recombinant overexpressed nSMase1 Rattus norvegicus 5783
-
3.1.4.12 extracellular nSMase, with a cleavable secretory signal sequence at their N-terminus, is a secretory protein released from cells Staphylococcus aureus
-
-
3.1.4.12 extracellular nSMase, with a cleavable secretory signal sequence at their N-terminus, is a secretory protein released from cells Listeria ivanovii
-
-
3.1.4.12 extracellular nSMase, with a cleavable secretory signal sequence at their N-terminus, is a secretory protein released from cells Bacillus cereus
-
-
3.1.4.12 membrane
-
Rattus norvegicus 16020
-
3.1.4.12 membrane nSMase1 contains two putative transmembrane domains at the C-terminus Homo sapiens 16020
-
3.1.4.12 additional information C-terminal region of nSMase2 harbors several motifs that may play a role in its localization Homo sapiens
-
-
3.1.4.12 nucleus endogenous nSMase1 Rattus norvegicus 5634
-
3.1.4.12 plasma membrane nSMase1 contains two putative transmembrane domains at the C-terminus Homo sapiens 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.12 Mg2+
-
Rattus norvegicus
3.1.4.12 Mg2+ required by N-SMase for activity Staphylococcus aureus
3.1.4.12 Mg2+ required by N-SMase for activity Helicobacter pylori
3.1.4.12 Mg2+ required by N-SMase for activity Homo sapiens
3.1.4.12 Mg2+ required by N-SMase for activity Listeria ivanovii
3.1.4.12 Mg2+ required by N-SMase for activity, residues Glu53, Asp126, Asp295, and His296 are critical for Mg2+ binding and catalytic activity Bacillus cereus
3.1.4.12 Mg2+ required by nSMase1 for activity Homo sapiens
3.1.4.12 additional information metal binding structure, overview Listeria ivanovii
3.1.4.12 additional information metal binding structure, overview Bacillus cereus
3.1.4.12 Zn2+ Zn2+ binding to the high-affinity site activates the enzyme and, conversely, binding to the low-affinity site inhibits the enzyme Bacillus cereus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.12 32000
-
x * 32000, SDS-PAGE Helicobacter pylori
3.1.4.12 47600
-
x * 47600, nSMase1, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.12 additional information Staphylococcus aureus 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 ?
-
?
3.1.4.12 additional information Helicobacter pylori 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 ?
-
?
3.1.4.12 additional information Listeria ivanovii 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 ?
-
?
3.1.4.12 additional information Bacillus cereus 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 ?
-
?
3.1.4.12 additional information Listeria ivanovii nSMase 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 ?
-
?
3.1.4.12 additional information Helicobacter pylori nSMase 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 ?
-
?
3.1.4.12 additional information Bacillus cereus nSMase 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 ?
-
?
3.1.4.12 sphingomyelin + H2O Staphylococcus aureus neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Rattus norvegicus neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Helicobacter pylori neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Homo sapiens neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Listeria ivanovii neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Bacillus cereus neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Homo sapiens neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview, signaling roles of nSMase2 implicated in apoptosis, inflammation, cell growth, and differentiation, and Alzheimer disease, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Listeria ivanovii nSMase neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Helicobacter pylori nSMase neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O Bacillus cereus nSMase neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview N-acylsphingosine + choline phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.12 Bacillus cereus P09599 nSMase
-
3.1.4.12 Bacillus cereus nSMase P09599 nSMase
-
3.1.4.12 Helicobacter pylori
-
nSMase
-
3.1.4.12 Helicobacter pylori nSMase
-
nSMase
-
3.1.4.12 Homo sapiens O60906 nSMase1 or smpd2; nSMase1 or smpd2
-
3.1.4.12 Homo sapiens Q9NY59 nSMase2; nSMase2
-
3.1.4.12 Listeria ivanovii Q9RLV9 nSMase
-
3.1.4.12 Listeria ivanovii nSMase Q9RLV9 nSMase
-
3.1.4.12 Rattus norvegicus
-
-
-
3.1.4.12 Staphylococcus aureus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.12 native enzyme Helicobacter pylori

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.4.12 a sphingomyelin + H2O = a ceramide + phosphocholine catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases Rattus norvegicus
3.1.4.12 a sphingomyelin + H2O = a ceramide + phosphocholine catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases Homo sapiens
3.1.4.12 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 Bacillus cereus
3.1.4.12 a sphingomyelin + H2O = a ceramide + phosphocholine catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases, histidine residues, His136 and His272, are essential for catalysis Homo sapiens
3.1.4.12 a sphingomyelin + H2O = a ceramide + phosphocholine catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases, overview Staphylococcus aureus
3.1.4.12 a sphingomyelin + H2O = a ceramide + phosphocholine catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases, overview Helicobacter pylori
3.1.4.12 a sphingomyelin + H2O = a ceramide + phosphocholine catalytic mechanism, a number of key residues involved in metal binding and catalysis are conserved in neutral sphingomyelinases, structure-function analysis, overview Listeria ivanovii

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.12 brain nSMase1, specific for Homo sapiens
-
3.1.4.12 fibroblast
-
Homo sapiens
-
3.1.4.12 hepatoma cell
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.12 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 Staphylococcus aureus ?
-
?
3.1.4.12 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 Helicobacter pylori ?
-
?
3.1.4.12 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 Listeria ivanovii ?
-
?
3.1.4.12 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 Bacillus cereus ?
-
?
3.1.4.12 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 Listeria ivanovii nSMase ?
-
?
3.1.4.12 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 Helicobacter pylori nSMase ?
-
?
3.1.4.12 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 Bacillus cereus nSMase ?
-
?
3.1.4.12 sphingomyelin + H2O
-
Staphylococcus aureus N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O
-
Rattus norvegicus N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O
-
Helicobacter pylori N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O
-
Homo sapiens N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O
-
Listeria ivanovii N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Staphylococcus aureus N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Rattus norvegicus N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Helicobacter pylori N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Homo sapiens N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Listeria ivanovii N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Bacillus cereus N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview, signaling roles of nSMase2 implicated in apoptosis, inflammation, cell growth, and differentiation, and Alzheimer disease, overview Homo sapiens N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O nSMase2 uses sphingomyelin preferentially as a substrate in vitro with no activity against lyso-PAF Homo sapiens N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O residues Glu53, Asp126, Asp295, and His296 are critical for Mg2+ binding and catalytic activity Bacillus cereus N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O
-
Listeria ivanovii nSMase N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Listeria ivanovii nSMase N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O
-
Helicobacter pylori nSMase N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Helicobacter pylori nSMase N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O neutral sphingomyelinases are considered major candidates for mediating the stress-induced production of ceramide, regulation, physiological, and pathological roles of these proteins, overview Bacillus cereus nSMase N-acylsphingosine + choline phosphate
-
?
3.1.4.12 sphingomyelin + H2O residues Glu53, Asp126, Asp295, and His296 are critical for Mg2+ binding and catalytic activity Bacillus cereus nSMase N-acylsphingosine + choline phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.4.12 ? x * 32000, SDS-PAGE Helicobacter pylori
3.1.4.12 ? x * 47600, nSMase1, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.4.12 N-SMase
-
Staphylococcus aureus
3.1.4.12 N-SMase
-
Rattus norvegicus
3.1.4.12 N-SMase
-
Helicobacter pylori
3.1.4.12 N-SMase
-
Homo sapiens
3.1.4.12 N-SMase
-
Listeria ivanovii
3.1.4.12 N-SMase
-
Bacillus cereus
3.1.4.12 neutral sphingomyelinase
-
Staphylococcus aureus
3.1.4.12 neutral sphingomyelinase
-
Rattus norvegicus
3.1.4.12 neutral sphingomyelinase
-
Helicobacter pylori
3.1.4.12 neutral sphingomyelinase
-
Homo sapiens
3.1.4.12 neutral sphingomyelinase
-
Listeria ivanovii
3.1.4.12 neutral sphingomyelinase
-
Bacillus cereus
3.1.4.12 nSMase1
-
Rattus norvegicus
3.1.4.12 nSMase1
-
Homo sapiens
3.1.4.12 nSMase2
-
Homo sapiens
3.1.4.12 smdp3
-
Homo sapiens
3.1.4.12 smpd2
-
Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.12 7.4
-
N-SMase Staphylococcus aureus
3.1.4.12 7.4
-
N-SMase Rattus norvegicus
3.1.4.12 7.4
-
N-SMase Helicobacter pylori
3.1.4.12 7.4
-
N-SMase Homo sapiens
3.1.4.12 7.4
-
N-SMase Listeria ivanovii
3.1.4.12 7.4
-
N-SMase Bacillus cereus