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

BRENDA support

Literature summary for 2.3.1.67 extracted from

  • Gomez-Cambronero, J.; Nieto, M.L.; Mato, J.M.; Sanchez-Crespo, M.
    Modulation of lyso-platelet-activating factor: acetyl-CoA acetyltransferase from rat splenic microsomes. The role of calcium ions (1985), Biochim. Biophys. Acta, 845, 511-515.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Trifluoperazine
-
Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.274
-
acetyl-CoA Km is induced to 0.118 mM in presence of Ca2+ Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Rattus norvegicus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activation reversed by addition of EGTA in excess of Ca2+, Ca2+ reduces the apparent Km for acetyl-CoA, maximum effect between 0.0001 and 0.01 mM, the action of Ca2+ seems to be independent of the presence of calmodulin or phosphorylation Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
spleen
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + alkyl-sn-glycero-3-phosphocholine
-
Rattus norvegicus CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Rattus norvegicus