Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.13 4beta-phorbol 12-myristate 13-acetate activates PKCalpha-mediated activation of phospholipase D Homo sapiens
3.1.4.4 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.13 bisindolylmaleimide strong inhibition of PKCalpha Homo sapiens
2.7.11.13 Gö 6976 slight inhibition of PKCalpha Homo sapiens
2.7.11.13 Ro-31-8220 strong inhibition of PKCalpha Homo sapiens
2.7.11.13 rottlerin slight inhibition of PKCalpha Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.11.13 membrane translocation Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.4 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.13 Homo sapiens
-
-
-
3.1.4.4 Chlorocebus aethiops
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.4 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

EC Number Source Tissue Comment Organism Textmining
2.7.11.13 commercial preparation recombinant PKCalpha Homo sapiens
-
3.1.4.4 COS-7 cell
-
 Chlorocebus aethiops
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.13 ATP + phospholipase D1 phosphorylation by PKC Homo sapiens ADP + phosphorylated phospholipase D1
-
 ?
2.7.11.13 ATP + phospholipase D2 phosphorylation by PKCalpha Homo sapiens ADP + phosphorylated phospholipase D2
-
 ?
2.7.11.13 additional information activation of phospholipase D2 by 4beta-phorbol 12-myristate 13-acetate-induced PKCalpha does not require phosphorylation, overview Homo sapiens ?
-
 ?
3.1.4.4 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 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.13 PKCalpha
-
 Homo sapiens
2.7.11.13 protein kinase Calpha
-
 Homo sapiens
3.1.4.4 PLD2
-
 Chlorocebus aethiops

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.13 ATP
-
 Homo sapiens