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Literature summary for 3.1.4.12 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)

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

Protein Variants

Protein Variants Comment Organism
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
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is dependent on divalent metal ions 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 ?
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 ?
-
?
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

Subunits Comment Organism
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

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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