Detail Information for IndEnz0018001344
IED ID IndEnz0018001344
Enzyme Type ID peroxidase001344
Protein Name Peroxiredoxin-2
EC 1.11.1.24
Thiol-specific antioxidant protein
TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Thioredoxin-dependent peroxiredoxin 2
Gene Name Prdx2 Tdpx1 Tpx
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MASGNAQIGKSAPDFTATAVVDGAFKEIKLSDYRGKYVVLFFYPLDFTFVCPTEIIAFSDHAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTKSLSQNYGVLKNDEGIAYRGLFIIDAKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN
Enzyme Length 198
Uniprot Accession Number Q61171
Absorption
Active Site ACT_SITE 51; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P32119
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:P32119};
DNA Binding
EC Number 1.11.1.24
Enzyme Function FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). {ECO:0000250|UniProtKB:P32119}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (9)
Keywords Acetylation;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000269|Ref.7; MOD_RES 11; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 112; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P32119; MOD_RES 182; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P32119
Post Translational Modification PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:P32119, ECO:0000250|UniProtKB:Q06830}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10501973; 10632718; 11217851; 12107731; 12466851; 12520002; 12586629; 12904583; 14610273; 14651920; 14681479; 15226823; 15259009; 15627969; 15858817; 15902258; 16109412; 16290204; 16565519; 16615898; 16635246; 16785024; 17050172; 17229725; 17325201; 17610816; 17634366; 17697936; 17967808; 17990289; 18369441; 18426799; 18442801; 18544346; 18614015; 18758163; 18799693; 19030911; 19208552; 19423573; 19455133; 19577336; 19766572; 19834914; 19899112; 19969073; 20208180; 20488244; 20978343; 21248284; 21267068; 21328451; 21677750; 21814176; 21835911; 21902453; 22099303; 22254090; 22356734; 22707207; 22749995; 22960070; 23055551; 23101509; 23142655; 23215741; 23429506; 23820076; 23909438; 24048895; 24715692; 25074339; 25092340; 25151118; 25802339; 25975898; 26058667; 26079888; 26500057; 26601956; 26797130; 27261193; 27689697; 28323129; 28659575; 28793778; 28801243; 29503398; 29605633; 29720484; 29778464; 30097850; 30395970; 30504831; 31026770; 31160554; 31882472; 32389179; 32705184; 32929220; 33254076; 33535382; 33587325; 33727589; 34030134; 9792801;
Motif
Gene Encoded By
Mass 21,779
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda