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Literature summary for 3.1.4.41 extracted from

  • Murakami, M.T.; Fernandes-Pedrosa, M.F.; de Andrade, S.A.; Gabdoulkhakov, A.; Betzel, C.; Tambourgi, D.V.; Arni, R.K.
    Structural insights into the catalytic mechanism of sphingomyelinases D and evolutionary relationship to glycerophosphodiester phosphodiesterases (2006), Biochem. Biophys. Res. Commun., 342, 323-329.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method. Crystal structure of the sulfate free enzyme determined at 1.85 A resolution. The metal ion is tetrahedrally coordinated instead of the trigonal-bipyramidal coordination observed in the sulfate bound form Loxosceles laeta

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+-ion-dependent acid-base mechanism which involves two histidines Loxosceles laeta

Organism

Organism UniProt Comment Textmining
Loxosceles laeta Q8I914 recombinant
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Source Tissue

Source Tissue Comment Organism Textmining
venom
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Loxosceles laeta
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sphingomyelin + H2O Mg2+-ion-dependent acid-base mechanism which involves two histidines Loxosceles laeta choline + ceramide phosphate
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Synonyms

Synonyms Comment Organism
SMase I
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Loxosceles laeta