Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diethyldicarbonate | 0.02-0.1 mM, complete inhibition, sphingomyelinase P1; 0.02-0.1 mM, complete inhibitionsphingomyelinase P2 | Loxosceles intermedia |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.064 | - |
sphingomyelin | 37°C, pH 7.4, sphingomyelinase P2 | Loxosceles intermedia | |
0.113 | - |
sphingomyelin | 37°C, pH 7.4, sphingomyelinase P1 | Loxosceles intermedia |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Loxosceles intermedia | - |
recombinant | - |
Loxosceles intermedia | P0CE81 | sphingomyelinase P1 precursor; recombinant | - |
Purification (Comment) | Organism |
---|---|
- |
Loxosceles intermedia |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
venom | - |
Loxosceles intermedia | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Comment | Organism |
---|---|---|
SMase P1 | - |
Loxosceles intermedia |
SMase P2 | - |
Loxosceles intermedia |
sphingomyelinase P1 | - |
Loxosceles intermedia |
sphingomyelinase P2 | - |
Loxosceles intermedia |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.058 | - |
sphingomyelin | 37°C, pH 7.4, sphingomyelinase P1 | Loxosceles intermedia | |
0.118 | - |
sphingomyelin | 37°C, pH 7.4, sphingomyelinase P2 | Loxosceles intermedia |