Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Bacillus subtilis strain ISW1214 | Bacillus cereus |
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 | Comment | Organism | Structure |
---|---|---|---|
additional information | neuraminidase from Clostridium perfringens inhibits the binding of the enzyme to mouse peritoneal macrophages | Bacillus cereus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is dependent on divalent metal ions | Bacillus cereus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | - |
- |
- |
Bacillus cereus IAM1029 | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
Bc-SMase | - |
Bacillus cereus |
sphingomyelinase | - |
Bacillus cereus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
membrane binding assay at | Bacillus cereus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
membrane binding assay at | Bacillus cereus |
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 |