Cloned (Comment) | Organism |
---|---|
functional overexpression in Rhodococcus erythropolis and secretion to the culture medium | Streptomyces sp. |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Streptomyces sp. | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | slightly activates, Km is 1.40 mM | Streptomyces sp. | |
Co2+ | activates, Km is 1.46 mM | Streptomyces sp. | |
Mg2+ | activates, Km is 1.29 mM | Streptomyces sp. | |
Mn2+ | activates, most effective divalent metal ion, Km is 0.94 mM | Streptomyces sp. | |
additional information | central metal-binding site residues N77, E119, D265, N267, D374, and H375 are completely conserved in the enzyme | Streptomyces sp. | |
Sr2+ | slightly activates, Km is 2.42 mM | Streptomyces sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
34000 | - |
1 * 34000, SDS-PAGE, 1 * 41540, sequence caclualtion | Streptomyces sp. |
37000 | - |
gel filtration | Streptomyces sp. |
41540 | - |
1 * 34000, SDS-PAGE, 1 * 41540, sequence caclualtion | Streptomyces sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a sphingomyelin + H2O | Streptomyces sp. | - |
a ceramide + phosphocholine | a ceramide is an N-acylsphingosine | ? | |
a sphingomyelin + H2O | Streptomyces sp. A9107 | - |
a ceramide + phosphocholine | a ceramide is an N-acylsphingosine | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces sp. | I4DXK5 | - |
- |
Streptomyces sp. A9107 | I4DXK5 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a sphingomyelin + H2O | - |
Streptomyces sp. | a ceramide + phosphocholine | a ceramide is an N-acylsphingosine | ? | |
a sphingomyelin + H2O | - |
Streptomyces sp. A9107 | a ceramide + phosphocholine | a ceramide is an N-acylsphingosine | ? | |
additional information | substrate specificity, the enzyme is highly sphingomyelin-specific, it may not have sphingomyelinase D activity, because it does not hydrolyze the ester linkage between ceramide phosphate and choline. Of the phospholipids tested, the enzyme hydrolyzes only the ester linkage between ceramide and phosphocholine and has no activity toward phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, lysophosphatidylethanolamine and phosphatidylinositol | Streptomyces sp. | ? | - |
? | |
additional information | substrate specificity, the enzyme is highly sphingomyelin-specific, it may not have sphingomyelinase D activity, because it does not hydrolyze the ester linkage between ceramide phosphate and choline. Of the phospholipids tested, the enzyme hydrolyzes only the ester linkage between ceramide and phosphocholine and has no activity toward phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, lysophosphatidylethanolamine and phosphatidylinositol | Streptomyces sp. A9107 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 34000, SDS-PAGE, 1 * 41540, sequence caclualtion | Streptomyces sp. |
Synonyms | Comment | Organism |
---|---|---|
S-SMase | - |
Streptomyces sp. |
SMase | - |
Streptomyces sp. |
sphingomyelinase C | - |
Streptomyces sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Streptomyces sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Streptomyces sp. |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme from Streptomyces seems to be a typical bacterial SMase with a primary structure unusual for known bacterial SMases, primary structure comparisons and phylogenetic analysis | Streptomyces sp. |