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Literature summary extracted from
- Role of side-edge site of sphingomyelinase from Bacillus cereus (2012), Biochem. Biophys. Res. Commun., 422, 128-132.
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 |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.4.12 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.4.12 | 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 |
| 3.1.4.12 | E53A | site-directed mutagenesis, inactive mutant | Bacillus cereus |
| 3.1.4.12 | 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 |
| 3.1.4.12 | F55A | site-directed mutagenesis, the mutation in close proximity to Mg2+ at the side-edge does not affect the enzyme | Bacillus cereus |
| 3.1.4.12 | 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
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.4.12 | EDTA | inactivation | Bacillus cereus |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.4.12 | extracellular | - |
Bacillus cereus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.4.12 | Co2+ | activates | Bacillus cereus | |
| 3.1.4.12 | 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)
| 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 | ? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.4.12 | Bc-SMase | - |
Bacillus cereus |
| 3.1.4.12 | neutral sphingomyelinase | - |
Bacillus cereus |
| 3.1.4.12 | nSMase | - |
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 | 37 | - |
assay at | Bacillus cereus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.4.12 | 7.5 | - |
assay at | Bacillus cereus |
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