EC Number   |
General Information |
Reference |
|---|
    2.3.1.23 | evolution |
enzyme At1g78690 shares high homology (about 40%) with the cardiolipin remodeling enzyme tafazzin, but the cardiolipin remodeling enzyme tafazzin and the lysophospholipid acyltransferase catalyze unique reactions |
755961 |
| 2.3.1.23 | evolution |
LPLATs have been identified in the membrane-bound O-acyltransferase (MBOAT) and 1-acyl-glycerol-3-phosphate O-acyltransferase families. Lysophosphatidylcholine acyltransferases (LPCATs), including isozymes LPCAT1-4, have LPLAT activities other than LPCAT activity. For example, LPCAT4 has lysophosphatidylethanolamine acyltransferase as well as LPCAT activity |
758401 |
| 2.3.1.23 | evolution |
the enzyme belongs to the MBOAT family |
756102 |
| 2.3.1.23 | evolution |
the LPCAT genes are highly conserved, suggesting that the duplicated LPCAT genes were derived from a segmental duplication event. The segmental duplication is the result of a recent whole-genome duplication event in flax |
736477 |
| 2.3.1.23 | malfunction |
despite di-acylate phosphatidylglycerol being a substrate, overexpression of At1g78690 in Escherichia coli leads to the accumulation of acyl-PG. Cardiolipin also accumulates in cells overexpressing At1g78690, cardiolipin is found in the inner mitochondrial membrane in eukaryotes and is critical for mitochondrial function. It serves as a necessary proton trap for oxidative phosphorylation and is a trigger for apoptosis |
755961 |
| 2.3.1.23 | malfunction |
LPCAT1 gene-trapped mice show decreased lung saturated phosphatidylcholine and higher perinatal mortality due to respiratory failure. LPCAT1-KO mice also show decreased lung dipalmitoyl-PC and blood oxygenation levels, and lower survival ratios compared to wild-type mice in a ventilator-induced lung injury model, which is an acute lung inflammatory model. Retinal degeneration and defects in visual function are also reported in a mouse strain containing a mutation in LPCAT1, rd11, reduced retinal dipalmitoyl-PC contents in mutant mice, reproducing the similar observation in the lung |
756102 |
| 2.3.1.23 | malfunction |
LPCAT1 gene-trapped mice show decreased lung saturated phosphatidylcholine and higher perinatal mortality due to respiratory failure. LPCAT1-KO mice also show decreased lung dipalmitoyl-PC and blood oxygenation levels, and lower survival ratios compared to wild-type mice in a ventilator-induced lung injury model, which is an acute lung inflammatory model. Retinal degeneration and defects in visual function are also reported in a mouse strain containing a mutation in LPCAT1, reduced retinal dipalmitoyl-PC contents in mutant mice, reproducing the similar observation in the lung |
756102 |
| 2.3.1.23 | malfunction |
LPCAT1 knockdown enhances polyunsaturated fatty acids (PUFAs)-induced cytotoxicity. In LPCAT1 knockout mice, DPPC level is reduced and UPR is activated in the retina. In a study of rd11 mice in which there is a natural loss-of-function of LPCAT1, the level of DPPC in the retina is decreased, resulting in retinal degeneration |
756687 |
| 2.3.1.23 | malfunction |
LPCAT1 knockdown enhances polyunsaturated fatty acids (PUFAs)-induced cytotoxicity. Transfection of an siRNA against LPCAT1 efficiently reduces protein expression of LPCAT1 in HeLa cells. LPCAT1 knockdown cells show a significant reduction in the amount of DPPC upon eicosapentaenoic acid (EPA; 20:5) treatment compared with siControl-transfected cells, whereas the amounts of EPA-containing species are not affected by LPCAT1 knockdown. Oleic acid treatment has no effect |
756687 |
| 2.3.1.23 | malfunction |
LPCAT3 deficiency decreases arachidonic acid containing PC, PE, and PS and induces neonatal lethality due to triacylglycerol (TG) accumulation and dysfunction in enterocytes. LPCAT3-KO mice show longer and bigger small intestine. In response to high-fat feeding, LPCAT3 deficiency in the intestine increases a gut hormone, GLP-1, and oleoylethanolamide. These results suggest that AA-containing PC is a key molecule in regulating dietary lipid absorption. LPCAT3 deficiency reduces cholesterol efflux in macrophages and intestine. Excess cellular cholesterol by LPCAT3 deficiency increases intestinal stem cell proliferation and promotes tumorigenesis |
756102 |
