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Literature summary for 3.1.4.41 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
Search for more literature for 3.1.4.41

Protein Variants

Protein Variants Comment Organism
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
D269G site-directed mutagenesis, the mutant shows reduced sphingomyelinase, but unaltered hemolytic activity compared to the wild type enzyme Loxosceles laeta
S257A site-directed mutagenesis, the mutant shows reduced sphingomyelinase, but unaltered hemolytic activity compared to the wild type enzyme Loxosceles laeta
S262A site-directed mutagenesis, the mutant shows reduced sphingomyelinase and hemolytic activity compared to the wild type enzyme Loxosceles laeta
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

Metals/Ions Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Loxosceles laeta
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

General Information

General Information Comment Organism
evolution the enzyme belongs to the the family of phospholipases D, PLD Loxosceles laeta
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