Detail Information for IndEnz0018001417
IED ID IndEnz0018001417
Enzyme Type ID peroxidase001417
Protein Name Peroxiredoxin-2
Prx
EC 1.11.1.25
1-Cys D-peroxiredoxin
Glutaredoxin-dependent peroxiredoxin
Peroxiredoxin II
Thioredoxin peroxidase
Gene Name
Organism Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Salicaceae Saliceae Populus (poplars) Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Enzyme Sequence MAPIAVGDVLPDGKLAYFDEQDQLQEVSVHSLVAGKKVILFGVPGAFTPTCSLKHVPGFIEKAGELKSKGVTEILCISVNDPFVMKAWAKSYPENKHVKFLADGSATYTHALGLELNLQEKGLGTRSRRFALLVDDLKVKAANIEGGGEFTVSSADDILKDL
Enzyme Length 162
Uniprot Accession Number A9PCL4
Absorption
Active Site ACT_SITE 51; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000269|PubMed:11832487, ECO:0000305|PubMed:15697201"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.25; Evidence={ECO:0000269|PubMed:11706208, ECO:0000269|PubMed:15032877};
DNA Binding
EC Number 1.11.1.25
Enzyme Function FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000269|PubMed:15032877, ECO:0000269|PubMed:18230180}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (10); Chain (1); Domain (1); Helix (6); Mutagenesis (4); Turn (1)
Keywords 3D-structure;Antioxidant;Oxidoreductase;Peroxidase;Redox-active center
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1TP9;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 17,415
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for phosphatidylcholine hydroperoxide {ECO:0000269|PubMed:15032877};
Metal Binding
Rhea ID RHEA:62624
Cross Reference Brenda 1.11.1.24;1.11.1.25;