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Literature summary for 3.1.4.41 extracted from
- Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D (2005), J. Biol. Chem., 280, 13658-13664.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop vapor diffusion method. crystal structure determined ar 1.75 A resolution using the quick cryo-soaking technique. The enzyme folds as an (alpha/beta)8 barrel, the interfacial and catalytic sites encompass hydrophobic loops and a negatively charged surface | Loxosceles laeta |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | substrate binding and/or transition state are stabilized by a Mg2+ ion, which is coordinated by Glu32, Asp34, Asp91 and solvent molecules | Loxosceles laeta |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Loxosceles laeta | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| venom | - |
Loxosceles laeta | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| sphingomyelin + H2O | - |
Loxosceles laeta | choline + ceramide 1-phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SMase D | - |
Loxosceles laeta |
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Release 2023.1 (January 2023)
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