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Literature summary for 3.1.4.12 extracted from

  • Oda, M.; Takahashi, M.; Tsuge, H.; Nagahama, M.; Sakurai, J.
    Role of side-edge site of sphingomyelinase from Bacillus cereus (2012), Biochem. Biophys. Res. Commun., 422, 128-132.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Bacillus subtilis strain ISW1214 Bacillus cereus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Bacillus cereus

Protein Variants

Protein Variants Comment Organism
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 Bacillus cereus
E53A site-directed mutagenesis, inactive mutant Bacillus cereus
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 Bacillus cereus
F55A site-directed mutagenesis, the mutation in close proximity to Mg2+ at the side-edge does not affect the enzyme Bacillus cereus
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 Bacillus cereus

Inhibitors

Inhibitors Comment Organism Structure
EDTA inactivation Bacillus cereus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Bacillus cereus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Bacillus cereus
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 Bacillus cereus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a sphingomyelin + H2O Bacillus cereus
-
a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?
a sphingomyelin + H2O Bacillus cereus IAM1029
-
a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-
Bacillus cereus IAM1029
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a sphingomyelin + H2O
-
Bacillus cereus a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?
a sphingomyelin + H2O
-
Bacillus cereus IAM1029 a ceramide + phosphocholine a ceramide is an N-acylsphingosine ?

Synonyms

Synonyms Comment Organism
Bc-SMase
-
Bacillus cereus
neutral sphingomyelinase
-
Bacillus cereus
nSMase
-
Bacillus cereus
sphingomyelinase
-
Bacillus cereus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Bacillus cereus