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Literature summary extracted from

  • de Andrade, S.A.; Murakami, M.T.; Cavalcante, D.P.; Arni, R.K.; Tambourgi, D.V.
    Kinetic and mechanistic characterization of the sphingomyelinases D from Loxosceles intermedia spider venom (2006), Toxicon, 47, 380-386.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.41 diethyldicarbonate 0.02-0.1 mM, complete inhibition, sphingomyelinase P1; 0.02-0.1 mM, complete inhibitionsphingomyelinase P2 Loxosceles intermedia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.41 0.064
-
 sphingomyelin 37°C, pH 7.4, sphingomyelinase P2 Loxosceles intermedia
3.1.4.41 0.113
-
 sphingomyelin 37°C, pH 7.4, sphingomyelinase P1 Loxosceles intermedia

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.41 Loxosceles intermedia
-
 recombinant
-
3.1.4.41 Loxosceles intermedia P0CE81 sphingomyelinase P1 precursor; recombinant
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.41
-
 Loxosceles intermedia

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.41 sphingomyelin + H2O sphingomyelinase P1 hydrolyzes sphingomyelin less efficiently than sphingomyelinase P2, which can be attributed to a substitution at position 203 (Pro-Leu) and local amino acid substitutions in the hydrophobic channel that can probably play a role in the substrate recognition and binding Loxosceles intermedia choline + ceramide phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.41 SMase P1
-
 Loxosceles intermedia
3.1.4.41 SMase P2
-
 Loxosceles intermedia
3.1.4.41 sphingomyelinase P1
-
 Loxosceles intermedia
3.1.4.41 sphingomyelinase P2
-
 Loxosceles intermedia

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.4.41 0.058
-
 sphingomyelin 37°C, pH 7.4, sphingomyelinase P1 Loxosceles intermedia
3.1.4.41 0.118
-
 sphingomyelin 37°C, pH 7.4, sphingomyelinase P2 Loxosceles intermedia