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Literature summary extracted from

  • Oda, M.; Fujita, A.; Okui, K.; Miyamoto, K.; Shibutani, M.; Takagishi, T.; Nagahama, M.
    Bacillus cereus sphingomyelinase recognizes ganglioside GM3 (2013), Biochem. Biophys. Res. Commun., 431, 164-168.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.12 F285A site-directed mutagenesis, binding of the mutant enzyme to mouse macrophages decreases markedly in comparison to the binding by wild-type enzyme Bacillus cereus
3.1.4.12 W284A site-directed mutagenesis, binding of the mutant enzyme to mouse macrophages decreases markedly in comparison to the binding by wild-type enzyme Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.12 additional information neuraminidase from Clostridium perfringens inhibits the binding of the enzyme to mouse peritoneal macrophages Bacillus cereus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.12 additional information the enzyme is dependent on divalent metal ions Bacillus cereus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.12 Bacillus cereus
-
-
-
3.1.4.12 Bacillus cereus IAM1029
-
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.1.4.12 More the enzyme contains the central site (catalytic site), side-edge site (membrane binding site), and beta-hairpin region (membrane binding site) Bacillus cereus

Synonyms

EC Number Synonyms Comment Organism
3.1.4.12 Bc-SMase
-
 Bacillus cereus
3.1.4.12 sphingomyelinase
-
 Bacillus cereus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.4.12 25
-
 membrane binding assay at Bacillus cereus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.12 7.4
-
 membrane binding assay at Bacillus cereus

General Information

EC Number General Information Comment Organism
3.1.4.12 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 Bacillus cereus