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Literature summary for 3.1.4.4 extracted from

  • Paruch, S.; El-Benna, J.; Djerdjouri, B.; Marullo, S.; Perianin, A.
    A role of p44/42 mitogen-activated protein kinases in formyl-peptide receptor-mediated phospholipase D activity and oxidant production (2006), FASEB J., 20, 142-144.
    View publication on PubMed

Application

Application Comment Organism
medicine the extracellular signal-regulated kinase/PLD2 coupling may provide potential pharmacological targets to control PLD-associated cellular dysfunctions Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens PLD is actived by the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine. PLD2, but not PLD1, contributes to PLD activity mediated by N-formyl-methionyl-leucyl-phenylalanine. Extracellular signal-regulated kinase/PLD2 pathway contributes to N-formyl-methionyl-leucyl-phenylalanine-mediated oxidant production ?
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
HL-60 cell
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Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PLD is actived by the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine. PLD2, but not PLD1, contributes to PLD activity mediated by N-formyl-methionyl-leucyl-phenylalanine. Extracellular signal-regulated kinase/PLD2 pathway contributes to N-formyl-methionyl-leucyl-phenylalanine-mediated oxidant production Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
PLD2
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Homo sapiens