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Literature summary extracted from

  • Murakami, M.T.; Fernandes-Pedrosa, M.F.; Tambourgi, D.V.; Arni, R.K.
    Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D (2005), J. Biol. Chem., 280, 13658-13664.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.41 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

EC Number Metals/Ions Comment Organism Structure
3.1.4.41 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

EC Number Organism UniProt Comment Textmining
3.1.4.41 Loxosceles laeta
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.41 venom
-
 Loxosceles laeta
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.41 sphingomyelin + H2O
-
 Loxosceles laeta choline + ceramide 1-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.41 SMase D
-
 Loxosceles laeta