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Literature summary extracted from

  • Catalan, A.; Cortes, W.; Munoz, C.; Araya, J.E.
    Tryptophan and aspartic acid residues present in the glycerophosphoryl diester phosphodiesterase (GDPD) domain of the Loxosceles laeta phospholipase D are essential for substrate recognition (2014), Toxicon, 81, 43-47.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.41 D259G site-directed mutagenesis, the mutant shows highly reduced sphingomyelinase and hemolytic activity compared to the wild type enzyme, the interaction with sphingomyelin is strongly reduced Loxosceles laeta
3.1.4.41 D269G site-directed mutagenesis, the mutant shows reduced sphingomyelinase, but unaltered hemolytic activity compared to the wild type enzyme Loxosceles laeta
3.1.4.41 S257A site-directed mutagenesis, the mutant shows reduced sphingomyelinase, but unaltered hemolytic activity compared to the wild type enzyme Loxosceles laeta
3.1.4.41 S262A site-directed mutagenesis, the mutant shows reduced sphingomyelinase and hemolytic activity compared to the wild type enzyme Loxosceles laeta
3.1.4.41 W256S site-directed mutagenesis, the mutant shows reduced sphingomyelinase and hemolytic activity compared to the wild type enzyme, the interaction with sphingomyelin is strongly reduced Loxosceles laeta

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.41 Mg2+ required, residue W256 is capable of coordinating the binding of the Mg2+ ion, along with being one of the negatively charged amino acids which form part of the catalytic pocket Loxosceles laeta

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.41 2-lysophosphatidylcholine + H2O Loxosceles laeta
-
 choline + 2-lysophosphatidate
-
 ?
3.1.4.41 sphingomyelin + H2O Loxosceles laeta
-
 ceramide phosphate + choline
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.41 Loxosceles laeta
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.41 2-lysophosphatidylcholine + H2O
-
 Loxosceles laeta choline + 2-lysophosphatidate
-
 ?
3.1.4.41 sphingomyelin + H2O
-
 Loxosceles laeta ceramide phosphate + choline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.41 GDPD
-
 Loxosceles laeta
3.1.4.41 glycerophosphoryl diester phosphodiesterase
-
 Loxosceles laeta
3.1.4.41 LlPLD1
-
 Loxosceles laeta
3.1.4.41 sphingomyelinase
-
 Loxosceles laeta

General Information

EC Number General Information Comment Organism
3.1.4.41 evolution the enzyme belongs to the the family of phospholipases D, PLD Loxosceles laeta
3.1.4.41 additional information highly conserved amino acids of the glycerophosphoryl diester phosphodiesterase domain of the recombinant enzyme interact with the substrate sphingomyelin and are involved in substrate recognition. Residues D259 and S262 form part of the catalytic pocket, and they have an important role in substrate recognition and maintenance of the electronegative net charge which sustains the interaction with sphingomyelin Loxosceles laeta