Literature summary for 3.1.4.41 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.

Search for more literature for 3.1.4.41

Inhibitors

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 [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

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

Purification (Commentary)

Purification (Comment)	Organism
-	Loxosceles intermedia

Source Tissue

Source Tissue	Comment	Organism	Textmining
venom	-	Loxosceles intermedia	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
SMase P1	-	Loxosceles intermedia
SMase P2	-	Loxosceles intermedia
sphingomyelinase P1	-	Loxosceles intermedia
sphingomyelinase P2	-	Loxosceles intermedia

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)