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Literature summary for 3.1.4.4 extracted from

  • Chen, J.S.; Exton, J.H.
    Regulation of phospholipase D2 activity by protein kinase Calpha (2004), J. Biol. Chem., 279, 22076-22083.
    View publication on PubMed
Search for more literature for 3.1.4.4

Activating Compound

Activating Compound Comment Organism Structure
additional information phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme Chlorocebus aethiops

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Chlorocebus aethiops phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme ?
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Organism

Organism UniProt Comment Textmining
Chlorocebus aethiops
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme Chlorocebus aethiops

Source Tissue

Source Tissue Comment Organism Textmining
COS-7 cell
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 Chlorocebus aethiops
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme Chlorocebus aethiops ?
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 ?

Synonyms

Synonyms Comment Organism
PLD2
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 Chlorocebus aethiops