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Literature summary for 3.1.1.5 extracted from

  • Victoria, E.J.; Korn, E.D.
    Plasma membrane and soluble lysophospholipases of Acanthamoeba castellanii (1975), Arch. Biochem. Biophys., 171, 255-258.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Triton X-100 stimulates membrane-bound enzyme Acanthamoeba castellanii

Inhibitors

Inhibitors Comment Organism Structure
deoxycholate soluble enzyme Acanthamoeba castellanii
glutathione membrane-bound enzyme, no inhibition of the soluble enzyme Acanthamoeba castellanii
Hg2+
-
Acanthamoeba castellanii
NEM soluble enzyme, no inhibition of the membrane-bound enzyme Acanthamoeba castellanii
SDS soluble and membrane-bound enzyme Acanthamoeba castellanii
Triton X-100 soluble enzyme Acanthamoeba castellanii
Zn2+
-
Acanthamoeba castellanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.083
-
lysophosphatidylcholine at low substrate concentrations Acanthamoeba castellanii
0.26
-
lysophosphatidylcholine at high substrate concentrations Acanthamoeba castellanii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Acanthamoeba castellanii 16020
-
plasma membrane
-
Acanthamoeba castellanii 5886
-
soluble
-
Acanthamoeba castellanii
-
-

Organism

Organism UniProt Comment Textmining
Acanthamoeba castellanii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lysophosphatidylcholine + H2O
-
Acanthamoeba castellanii glycerophosphorylcholine + unesterified fatty acid
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
and a second optimum at pH 8.0, membrane-bound enzyme Acanthamoeba castellanii
7
-
and a second optimum at pH 9.5, soluble enzyme Acanthamoeba castellanii
8
-
and a second optimum at pH 6.5, membrane-bound enzyme Acanthamoeba castellanii
9.5
-
and a second optimum at pH 7.0, soluble enzyme Acanthamoeba castellanii