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Literature summary for 3.1.4.41 extracted from

  • Catalan, A.; Cortes, W.; Sagua, H.; Gonzalez, J.; Araya, J.E.
    Two new phospholipase D isoforms of Loxosceles laeta: Cloning, heterologous expression, functional characterization, and potential biotechnological application (2011), J. Biochem. Mol. Toxicol., 25, 393-403.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
isozymes LIPLD1 and LIPLD2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression in Escherichia coli strain BL21 (DE3) Loxosceles laeta

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Loxosceles laeta
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Loxosceles laeta the recombinant protein rLIPLD1 shows hydrolytic activity on sphingomyelin and in vitro hemolytic activity on human red blood cells, whereas rLIPLD2 is inactive ?
-
 ?

Organism

Organism UniProt Comment Textmining
Loxosceles laeta
-
 isozymes LIPLD1 and LIPLD2
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Loxosceles laeta
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the recombinant protein rLIPLD1 shows hydrolytic activity on sphingomyelin and in vitro hemolytic activity on human red blood cells, whereas rLIPLD2 is inactive Loxosceles laeta ?
-
 ?

Synonyms

Synonyms Comment Organism
LIPLD1
-
 Loxosceles laeta
LIPLD2
-
 Loxosceles laeta

General Information

General Information Comment Organism
physiological function toxin phospholipases-D in the venom of Loxosceles spiders is the main responsible for local and systemic effects observed in the loxoscelism Loxosceles laeta