| IED ID | IndEnz0018001406 |
| Enzyme Type ID | peroxidase001406 |
| Protein Name |
Peroxiredoxin-6 EC 1.11.1.27 1-Cys peroxiredoxin 1-Cys PRX Acidic calcium-independent phospholipase A2 aiPLA2 EC 3.1.1.4 Antioxidant protein 2 Glutathione-dependent peroxiredoxin Lysophosphatidylcholine acyltransferase 5 LPC acyltransferase 5 LPCAT-5 Lyso-PC acyltransferase 5 EC 2.3.1.23 Non-selenium glutathione peroxidase NSGPx Thiol-specific antioxidant protein |
| Gene Name | Prdx6 Aipla2 Aop2 Tsa |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MPGGLLLGDEAPNFEANTTIGHIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHFAWSKDINAYNGAAPTEKLPFPIIDDKDRDLAILLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTASNPVATPVDWKKGESVMVLPTLPEEEAKQLFPKGVFTKELPSGKKYLRYTPQP |
| Enzyme Length | 224 |
| Uniprot Accession Number | O35244 |
| Absorption | |
| Active Site | ACT_SITE 47; /note=Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity; /evidence=ECO:0000269|PubMed:17652308; ACT_SITE 140; /note=For phospholipase activity; /evidence=ECO:0000305|PubMed:17652308 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000269|PubMed:15004285}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:17652308, ECO:0000269|PubMed:8999971}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000269|PubMed:26830860}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P30041}; |
| DNA Binding | |
| EC Number | 1.11.1.27; 3.1.1.4; 2.3.1.23 |
| Enzyme Function | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15004285). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:8999971, PubMed:15004285, PubMed:17652308). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). {ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:15004285, ECO:0000269|PubMed:17652308, ECO:0000269|PubMed:26830860, ECO:0000269|PubMed:8999971}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4 (for phospholipase activity). {ECO:0000269|PubMed:8999971}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Mutagenesis (3); Region (1); Site (1) |
| Keywords | Acetylation;Antioxidant;Cytoplasm;Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Multifunctional enzyme;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Transferase |
| Interact With | P62259 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19700648}. Lysosome {ECO:0000269|PubMed:19700648}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000269|PubMed:19700648}. |
| Modified Residue | MOD_RES 44; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P30041; MOD_RES 63; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P30041; MOD_RES 89; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P30041; MOD_RES 177; /note=Phosphothreonine; by MAPK; /evidence=ECO:0000269|PubMed:19140803; MOD_RES 209; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P30041; MOD_RES 209; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08709 |
| Post Translational Modification | PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (PubMed:19140803). Phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (PubMed:26830860). {ECO:0000269|PubMed:19140803, ECO:0000269|PubMed:26830860}.; PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16396496; 17877381; 21346153; 24687852; 25171874; 8641418; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,819 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for dipalmitoyl phosphatidylcholine {ECO:0000269|PubMed:8999971}; Vmax=1.89 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine {ECO:0000269|PubMed:8999971}; |
| Metal Binding | |
| Rhea ID | RHEA:62632; RHEA:15801; RHEA:12937; RHEA:35983; RHEA:35984; RHEA:41223; RHEA:41224 |
| Cross Reference Brenda | 1.11.1.27;2.3.1.23;3.1.1.4; |