Cloned (Comment) | Organism |
---|---|
gene prdx6, functional recombinant enzyme expression in mouse pulmonary microvascular endothelial cells via infection with a lentiviral vector construct | Mus musculus |
gene prdx6, recombinant enzyme expression | Homo sapiens |
gene prdx6, recombinant enzyme expression | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
C47S | site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection. The C47S mutant protein does not express peroxidase activity, but both PLA2 and LPCAT activities are preserved | Mus musculus |
D140A | site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection. The D140A mutant protein retains full peroxidase activity | Mus musculus |
D31A | site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection | Homo sapiens |
D31A | site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection, the mutant loses almost all LPCAT activity, but retains PLA2 activity | Mus musculus |
H26A | site-directed mutagenesis, breeding of H26A Prdx6 knock-in mutant mice, the final targeting construct is linearized, sequence verified, and electroporated into C57Bl/6J ES cells (EAP6 ES cells) for insertion of the mutant sequences into the mouse genome by homologous recombination, positive clones are used for blastocyst injection into CD-1/BALB/c mice, chimeric H26A Prdx6 mice are bred to C57Bl/6J wild-type mice and the resulting heterozygotic mice are bred to homozygosity. The H26A mutant retains the ability to reduce short chain hydroperoxides, but cannot reduce phospholipid hydroperoxides, as they do not bind to the phospholipid substrate | Mus musculus |
H26A | site-directed mutagenesis, construction of mutant endothelial cells via lentivirus transfection | Homo sapiens |
additional information | construction of a LPCAT knockout mutant | Mus musculus |
S32A | site-directed mutagenesis, the S32A mutant retains the ability to reduce short chain hydroperoxides, but cannot reduce phospholipid hydroperoxides, as they do not bind to the phospholipid substrate | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CI-976 | about 50% inhibition at 0.01 mM | Homo sapiens | |
CI-976 | - |
Mus musculus | |
CI-976 | about 50% inhibition at 0.01 mM | Rattus norvegicus | |
additional information | in wild-type lamellar bodies, markedly decreased incorporation of labeled palmitate into phosphatidylcholine is observed in the presence of MJ33, an inhibitor of the PLA2 activity of Prdx6 and, therefore, an inhibitor of LPC generation. This decreased incorporation of palmitate into PC in the presence of MJ33 is reversed by the addition of exogenous LPC to the LB incubation medium. Presence of CI-976 also markedly inhibits the incorporation of palmitoyl CoA into PC, but, unlike the results with MJ33, there is no change in the inhibition with addition of LPC | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | Prdx6 is a unique LPCAT enzyme with demonstrated cytoplasmic localization | Homo sapiens | 5737 | - |
cytoplasm | Prdx6 is a unique LPCAT enzyme with demonstrated cytoplasmic localization | Mus musculus | 5737 | - |
cytoplasm | Prdx6 is a unique LPCAT enzyme with demonstrated cytoplasmic localization | Rattus norvegicus | 5737 | - |
lamellar body | - |
Homo sapiens | 42599 | - |
lamellar body | - |
Mus musculus | 42599 | - |
lamellar body | - |
Rattus norvegicus | 42599 | - |
additional information | the remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane | Homo sapiens | - |
- |
additional information | the remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane | Mus musculus | - |
- |
additional information | the remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane | Rattus norvegicus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | ? | - |
- |
|
additional information | Homo sapiens | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | ? | - |
- |
|
additional information | Rattus norvegicus | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | ? | - |
- |
|
additional information | Mus musculus C57BL/6J | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | ? | - |
- |
|
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | Homo sapiens | - |
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | Mus musculus | - |
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | Rattus norvegicus | - |
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | Mus musculus C57BL/6J | - |
CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P30041 | - |
- |
Mus musculus | O08709 | - |
- |
Mus musculus C57BL/6J | O08709 | - |
- |
Rattus norvegicus | O35244 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | Prdx6 is phosphorylated at amino acid T177 by incubation with the MAPK, Erk 2, in the presence of Mg2+-ATP | Homo sapiens |
Purification (Comment) | Organism |
---|---|
recombinant enzyme hPrdx6 by anion exchange chromatography | Homo sapiens |
recombinant enzyme rPrdx6 by anion exchange chromatography | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
lung | - |
Homo sapiens | - |
lung | - |
Mus musculus | - |
lung | - |
Rattus norvegicus | - |
lung epithelial cell | - |
Homo sapiens | - |
lung epithelial cell | - |
Mus musculus | - |
lung epithelial cell | - |
Rattus norvegicus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
LPCAT activities of wild-type and mutant recombinant Prdx6, lungs isolated from wild-type and mutant mice, and lentiviral vector-infected mouse pulmonary microvascular endothelial cells (MPMVECs), overview | Mus musculus |
0.0004 | - |
purified unphosphorylated recombinant mutant D31A enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Mus musculus |
0.024 | - |
purified unphosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA | Homo sapiens |
0.028 | - |
purified unphosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA | Rattus norvegicus |
0.059 | - |
purified unphosphorylated recombinant mutant C47S enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Mus musculus |
0.064 | - |
purified unphosphorylated recombinant mutant S32A enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Mus musculus |
0.065 | - |
purified unphosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Homo sapiens |
0.065 | - |
purified unphosphorylated recombinant mutant H26A enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Mus musculus |
0.065 | - |
purified unphosphorylated recombinant wild-type enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Mus musculus |
0.066 | - |
purified unphosphorylated recombinant mutant D140A enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Mus musculus |
0.068 | - |
purified unphosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Rattus norvegicus |
0.652 | - |
purified phosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Homo sapiens |
0.661 | - |
purified phosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA | Rattus norvegicus |
0.662 | - |
purified phosphorylated recombinant enzyme, pH 4.0, 30°C, substrates LPC and palmitoyl CoA | Rattus norvegicus |
0.662 | - |
purified phosphorylated recombinant enzyme, pH 7.0, 30°C, substrates LPC and palmitoyl CoA | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | Mus musculus | ? | - |
- |
|
additional information | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | Homo sapiens | ? | - |
- |
|
additional information | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | Rattus norvegicus | ? | - |
- |
|
additional information | the enzyme is highly specific for substrates palmitoyl-CoA and lysophosphatidylcholine. Lysophosphatidylethanolamine, lysophosphatidylglycerol, lysophosphatidylinositol, and lysophosphatidylserine are poor substrates, as well as stearoyl-CoA, acetyl-CoA, oleoyl-CA, and arachidonoyl-CoA | Homo sapiens | ? | - |
- |
|
additional information | a linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction | Mus musculus C57BL/6J | ? | - |
- |
|
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | - |
Homo sapiens | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | - |
Mus musculus | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | - |
Rattus norvegicus | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | quantification of palmitic acid by gas chromatography | Homo sapiens | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | quantification of palmitic acid by gas chromatography | Mus musculus | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | quantification of palmitic acid by gas chromatography | Rattus norvegicus | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | - |
Mus musculus C57BL/6J | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? | |
palmitoyl-CoA + 1-palmitoyl-sn-glycero-3-phosphocholine | quantification of palmitic acid by gas chromatography | Mus musculus C57BL/6J | CoA + 1,2-dipalmitoyl-sn-glycero-3-phosphocholine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
hPrdx6 | - |
Homo sapiens |
LPCAT | - |
Homo sapiens |
LPCAT | - |
Mus musculus |
LPCAT | - |
Rattus norvegicus |
lysophosphatidylcholine acyl transferase | - |
Homo sapiens |
lysophosphatidylcholine acyl transferase | - |
Mus musculus |
lysophosphatidylcholine acyl transferase | - |
Rattus norvegicus |
mPrdx6 | - |
Mus musculus |
rPrdx6 | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Homo sapiens |
30 | - |
assay at | Mus musculus |
30 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Homo sapiens |
7 | - |
assay at | Mus musculus |
7 | - |
assay at | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
additional information | amino acid D31 is crucial for LPCAT activity | Homo sapiens |
additional information | amino acid D31 is crucial for LPCAT activity | Mus musculus |
physiological function | lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6, Prdx6, that shows a strong preference for lysophosphatidylcholine (LPC) as the head group and for palmitoyl CoA in the acylation reaction. The enzyme is a peroxiredoxin-6 (EC 1.11.1.27). Prdx6 also has a phospholipase A 2 (PLA2, EC 3.1.1.4) activity that plays important physiological roles in the synthesis of lung surfactant and in the repair of peroxidized cell membranes. These functions require the activity of a lysophospholipid acyl transferase as a critical component of the phospholipid remodeling pathway. A linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction. Prdx6 is a complete enzyme comprising both PLA2 and LPCAT activities for the remodeling pathway of PC synthesis or for repair of membrane lipid peroxidation. The remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane | Homo sapiens |
physiological function | lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6, Prdx6, that shows a strong preference for lysophosphatidylcholine (LPC) as the head group and for palmitoyl CoA in the acylation reaction. The enzyme is a peroxiredoxin-6 (EC 1.11.1.27). Prdx6 also has a phospholipase A 2 (PLA2, EC 3.1.1.4) activity that plays important physiological roles in the synthesis of lung surfactant and in the repair of peroxidized cell membranes. These functions require the activity of a lysophospholipid acyl transferase as a critical component of the phospholipid remodeling pathway. A linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction. Prdx6 is a complete enzyme comprising both PLA2 and LPCAT activities for the remodeling pathway of PC synthesis or for repair of membrane lipid peroxidation. The remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane | Rattus norvegicus |
physiological function | lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6, Prdx6, that shows a strong preference for lysophosphatidylcholine (LPC) as the head group and for palmitoyl CoA in the acylation reaction. The enzyme is a peroxiredoxin-6 (EC 1.11.1.27). Prdx6 also has a phospholipase A 2 (PLA2, EC 3.1.1.4) activity that plays important physiological roles in the synthesis of lung surfactant and in the repair of peroxidized cell membranes. These functions require the activity of a lysophospholipid acyl transferase as a critical component of the phospholipid remodeling pathway. A linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicates that lysophosphatidylcholine generated by Prdx6 PLA2 activity remains bound to the enzyme for the reacylation reaction. Prdx6 is a complete enzyme comprising both PLA2 and LPCAT activities for the remodeling pathway of PC synthesis or for repair of membrane lipid peroxidation. The remodeling pathway for the repair of peroxidized cell membranes presumably occurs at the cytoplasmic face of the affected cell membrane | Mus musculus |