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Literature summary for 2.3.1.148 extracted from

  • Snyder, F.; Lee, T.C.; Blank, M.L.
    The role of transacylases in the metabolism of arachidonate and platelet activating factor (1992), Prog. Lipid Res., 31, 65-86.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Zn2+ strong Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
1-hexadecyl-2-lyso-glycerophosphocholine
-
Oryctolagus cuniculus
0.0038
-
1-acyl-2-lyso-glycerophosphocholine
-
Oryctolagus cuniculus
0.017
-
1-palmitoyl-2-lyso-glycerophosphocholine
-
Rattus norvegicus
0.076
-
lyso-phosphatidylserine
-
Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Rattus norvegicus
-
-
microsome
-
Oryctolagus cuniculus
-
-
microsome
-
Canis lupus familiaris
-
-

Organism

Organism UniProt Comment Textmining
Canis lupus familiaris
-
-
-
Homo sapiens
-
-
-
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
alveolar macrophage
-
Oryctolagus cuniculus
-
heart
-
Canis lupus familiaris
-
liver
-
Rattus norvegicus
-
liver
-
Oryctolagus cuniculus
-
lung
-
Rattus norvegicus
-
lymphocyte
-
Mus musculus
-
macrophage
-
Mus musculus
-
platelet
-
Homo sapiens
-
platelet
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-Acyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine transfer of arachidonate occurs through a bidirectional movement Mus musculus 1-Acyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
-
?
1-acyl-2-arachidonoyl-sn-glycero-3-phosphoinositol + lyso-phosphatidylcholine
-
Mus musculus 1-acyl-2-lyso-sn-glycero-3-phosphoinositol + ?
-
?
1-Acyl-2-arachidonoyl-sn-glycero-3-phosphophoinositol + lyso-phosphatidylethanolamine unidirectional transfer process of arachidonate Mus musculus 1-Acyl-2-lyso-sn-glycero-3-phosphoinositol + arachidonoylphosphatidylethanolamine
-
?
1-acyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
-
Oryctolagus cuniculus 1-acyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
-
r
1-Hexadecyl-2-lyso-glycerophosphocholine + phospholipid
-
Oryctolagus cuniculus ?
-
?
1-palmitoyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
-
Rattus norvegicus 1-palmitoyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
-
r
lyso-Pasmenylethanolamine + phospholipid
-
Homo sapiens ?
-
?
lyso-Phosphatidylethanolamine + phospholipid
-
Homo sapiens Phosphatidylethanolamine + lyso-phospholipid
-
?
lyso-Phosphatidylinositol + phospholipid
-
Homo sapiens Phosphatidylinositol + lyso-phospholipid
-
?
lyso-Phosphatidylserine + phospholipid
-
Homo sapiens Phosphatidylserine + lyso-phospholipid
-
?
additional information arachidonate and linoleate at the sn-2 position of phosphatidylcholine can be transferred to lyso-phosphatidylethanolamine. The transfer of 16:0, 18:0, and 18:1 acyl moieties at the sn-2-position of phosphatidylcholine is negligible Rattus norvegicus ?
-
?
additional information more efficient transfer of arachidonate from phosphatidylcholine to the ethanolamine-containing phospholipids than from phosphatidylinositol Homo sapiens ?
-
?
Phosphatidylcholine + lyso-phosphatidylethanolamine
-
Mus musculus lyso-Phosphatidylcholine + phosphatidylethanolamine
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
bimodal pH-optimum, at pH 4.5 and at pH 7.5. The activity is 4-5times higher at pH 4.5 than at pH 7.5 Canis lupus familiaris
7.5
-
-
Rattus norvegicus
7.5
-
bimodal pH-optimum, at pH 7.5 and at pH 4.5 Canis lupus familiaris

Cofactor

Cofactor Comment Organism Structure
CoA
-
Canis lupus familiaris
CoA required Mus musculus
CoA required Homo sapiens
CoA required Rattus norvegicus
CoA required Oryctolagus cuniculus
CoA Km: 0.0015 mM, lung enzyme, with lyso-phosphatidylethanolamine as substrate Rattus norvegicus
CoA Km: 0.014 mM, liver enzyme, with 2-lyso-sn-phosphatidylinositol as substrate Rattus norvegicus
CoA Km: 0.0014 mM Homo sapiens
CoA Km: 0.0014 mM Oryctolagus cuniculus