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Literature summary for 3.1.4.4 extracted from

  • Yoon, S.H.; Min, d.o..S.; Bae, Y.S.
    Over-expression of phospholipase D isozymes down-regulates protein kinase CKII activity via proteasome-dependent CKIIbeta degradation in NIH3T3 cells (2009), Mol. Cells, 27, 299-305.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of isozymes PLD1 and PLD2 in NIH3T3 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
K758R catalytically inactive mutant of PLD2 Mus musculus
K898R catalytically inactive mutant of PLD1 Mus musculus
additional information overexpression of phospholipase D isozymes, leads to downregulation of protein kinase CKII activity via proteasome-dependent CKIIbeta degradation in NIH3T3 cells. Co-localization of CKIIbeta and PLD isozymes in NIH3T3 cells Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
1-butanol inhibits PLD hydrolytic activity Mus musculus
additional information no inhibition by 2-butanol Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
isozymes PLD1 and PLD2
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
PLD transphosphatidylation activity, overview Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor Mus musculus ?
-
?
additional information the catalytic activity of PLD is not required for PLD-mediated CKII inhibition, possible inhibition mechanism, overview Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
PLD
-
Mus musculus