Data extracted from this reference:
Inhibitors
2.3.1.148
Zn2+
strong
Rattus norvegicus
KM Value [mM]
2.3.1.148
0.0015
1-hexadecyl-2-lyso-glycerophosphocholine
Oryctolagus cuniculus
2.3.1.148
0.0038
1-acyl-2-lyso-glycerophosphocholine
Oryctolagus cuniculus
2.3.1.148
0.017
1-palmitoyl-2-lyso-glycerophosphocholine
Rattus norvegicus
2.3.1.148
0.076
lyso-phosphatidylserine
Homo sapiens
Localization
2.3.1.148
microsome
Rattus norvegicus
2.3.1.148
microsome
Oryctolagus cuniculus
2.3.1.148
microsome
Canis lupus familiaris
Organism
2.3.1.148
Canis lupus familiaris
2.3.1.148
Oryctolagus cuniculus
2.3.1.148
Rattus norvegicus
Source Tissue
2.3.1.148
alveolar macrophage
Oryctolagus cuniculus
2.3.1.148
heart
Canis lupus familiaris
2.3.1.148
liver
Rattus norvegicus
2.3.1.148
liver
Oryctolagus cuniculus
2.3.1.148
lung
Rattus norvegicus
2.3.1.148
lymphocyte
Mus musculus
2.3.1.148
macrophage
Mus musculus
2.3.1.148
platelet
Homo sapiens
2.3.1.148
platelet
Rattus norvegicus
Substrates and Products (Substrate)
2.3.1.148
1-Acyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
transfer of arachidonate occurs through a bidirectional movement
16278
Mus musculus
1-Acyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
?
2.3.1.148
1-acyl-2-arachidonoyl-sn-glycero-3-phosphoinositol + lyso-phosphatidylcholine
16278
Mus musculus
1-acyl-2-lyso-sn-glycero-3-phosphoinositol + ?
?
2.3.1.148
1-Acyl-2-arachidonoyl-sn-glycero-3-phosphophoinositol + lyso-phosphatidylethanolamine
unidirectional transfer process of arachidonate
16278
Mus musculus
1-Acyl-2-lyso-sn-glycero-3-phosphoinositol + arachidonoylphosphatidylethanolamine
?
2.3.1.148
1-acyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
16278
Oryctolagus cuniculus
1-acyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
r
2.3.1.148
1-Hexadecyl-2-lyso-glycerophosphocholine + phospholipid
16278
Oryctolagus cuniculus
?
?
2.3.1.148
1-palmitoyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
16278
Rattus norvegicus
1-palmitoyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
r
2.3.1.148
lyso-Pasmenylethanolamine + phospholipid
16278
Homo sapiens
?
?
2.3.1.148
lyso-Phosphatidylethanolamine + phospholipid
16278
Homo sapiens
Phosphatidylethanolamine + lyso-phospholipid
?
2.3.1.148
lyso-Phosphatidylinositol + phospholipid
16278
Homo sapiens
Phosphatidylinositol + lyso-phospholipid
?
2.3.1.148
lyso-Phosphatidylserine + phospholipid
16278
Homo sapiens
Phosphatidylserine + lyso-phospholipid
?
2.3.1.148
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
16278
Rattus norvegicus
?
?
2.3.1.148
additional information
more efficient transfer of arachidonate from phosphatidylcholine to the ethanolamine-containing phospholipids than from phosphatidylinositol
16278
Homo sapiens
?
?
2.3.1.148
Phosphatidylcholine + lyso-phosphatidylethanolamine
16278
Mus musculus
lyso-Phosphatidylcholine + phosphatidylethanolamine
?
pH Optimum
2.3.1.148
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
2.3.1.148
7.5
Rattus norvegicus
2.3.1.148
7.5
bimodal pH-optimum, at pH 7.5 and at pH 4.5
Canis lupus familiaris
Cofactor
2.3.1.148
CoA
Canis lupus familiaris
2.3.1.148
CoA
required
Mus musculus
2.3.1.148
CoA
required
Homo sapiens
2.3.1.148
CoA
required
Rattus norvegicus
2.3.1.148
CoA
required
Oryctolagus cuniculus
2.3.1.148
CoA
Km: 0.0015 mM, lung enzyme, with lyso-phosphatidylethanolamine as substrate
Rattus norvegicus
2.3.1.148
CoA
Km: 0.014 mM, liver enzyme, with 2-lyso-sn-phosphatidylinositol as substrate
Rattus norvegicus
2.3.1.148
CoA
Km: 0.0014 mM
Homo sapiens
2.3.1.148
CoA
Km: 0.0014 mM
Oryctolagus cuniculus
Cofactor (protein specific)
2.3.1.148
CoA
Canis lupus familiaris
2.3.1.148
CoA
required
Mus musculus
2.3.1.148
CoA
required
Homo sapiens
2.3.1.148
CoA
required
Rattus norvegicus
2.3.1.148
CoA
required
Oryctolagus cuniculus
2.3.1.148
CoA
Km: 0.0015 mM, lung enzyme, with lyso-phosphatidylethanolamine as substrate
Rattus norvegicus
2.3.1.148
CoA
Km: 0.014 mM, liver enzyme, with 2-lyso-sn-phosphatidylinositol as substrate
Rattus norvegicus
2.3.1.148
CoA
Km: 0.0014 mM
Homo sapiens
2.3.1.148
CoA
Km: 0.0014 mM
Oryctolagus cuniculus
Inhibitors (protein specific)
2.3.1.148
Zn2+
strong
Rattus norvegicus
KM Value [mM] (protein specific)
2.3.1.148
0.0015
1-hexadecyl-2-lyso-glycerophosphocholine
Oryctolagus cuniculus
2.3.1.148
0.0038
1-acyl-2-lyso-glycerophosphocholine
Oryctolagus cuniculus
2.3.1.148
0.017
1-palmitoyl-2-lyso-glycerophosphocholine
Rattus norvegicus
2.3.1.148
0.076
lyso-phosphatidylserine
Homo sapiens
Localization (protein specific)
2.3.1.148
microsome
Rattus norvegicus
2.3.1.148
microsome
Oryctolagus cuniculus
2.3.1.148
microsome
Canis lupus familiaris
Source Tissue (protein specific)
2.3.1.148
alveolar macrophage
Oryctolagus cuniculus
2.3.1.148
heart
Canis lupus familiaris
2.3.1.148
liver
Rattus norvegicus
2.3.1.148
liver
Oryctolagus cuniculus
2.3.1.148
lung
Rattus norvegicus
2.3.1.148
lymphocyte
Mus musculus
2.3.1.148
macrophage
Mus musculus
2.3.1.148
platelet
Homo sapiens
2.3.1.148
platelet
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
2.3.1.148
1-Acyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
transfer of arachidonate occurs through a bidirectional movement
16278
Mus musculus
1-Acyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
?
2.3.1.148
1-acyl-2-arachidonoyl-sn-glycero-3-phosphoinositol + lyso-phosphatidylcholine
16278
Mus musculus
1-acyl-2-lyso-sn-glycero-3-phosphoinositol + ?
?
2.3.1.148
1-Acyl-2-arachidonoyl-sn-glycero-3-phosphophoinositol + lyso-phosphatidylethanolamine
unidirectional transfer process of arachidonate
16278
Mus musculus
1-Acyl-2-lyso-sn-glycero-3-phosphoinositol + arachidonoylphosphatidylethanolamine
?
2.3.1.148
1-acyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
16278
Oryctolagus cuniculus
1-acyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
r
2.3.1.148
1-Hexadecyl-2-lyso-glycerophosphocholine + phospholipid
16278
Oryctolagus cuniculus
?
?
2.3.1.148
1-palmitoyl-2-lyso-glycerophosphocholine + arachidonoylphosphatidylethanolamine
16278
Rattus norvegicus
1-palmitoyl-2-arachidonoyl-glycerophosphocholine + lyso-phosphatidylethanolamine
r
2.3.1.148
lyso-Pasmenylethanolamine + phospholipid
16278
Homo sapiens
?
?
2.3.1.148
lyso-Phosphatidylethanolamine + phospholipid
16278
Homo sapiens
Phosphatidylethanolamine + lyso-phospholipid
?
2.3.1.148
lyso-Phosphatidylinositol + phospholipid
16278
Homo sapiens
Phosphatidylinositol + lyso-phospholipid
?
2.3.1.148
lyso-Phosphatidylserine + phospholipid
16278
Homo sapiens
Phosphatidylserine + lyso-phospholipid
?
2.3.1.148
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
16278
Rattus norvegicus
?
?
2.3.1.148
additional information
more efficient transfer of arachidonate from phosphatidylcholine to the ethanolamine-containing phospholipids than from phosphatidylinositol
16278
Homo sapiens
?
?
2.3.1.148
Phosphatidylcholine + lyso-phosphatidylethanolamine
16278
Mus musculus
lyso-Phosphatidylcholine + phosphatidylethanolamine
?
pH Optimum (protein specific)
2.3.1.148
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
2.3.1.148
7.5
Rattus norvegicus
2.3.1.148
7.5
bimodal pH-optimum, at pH 7.5 and at pH 4.5
Canis lupus familiaris