IED ID | IndEnz0018001143 |
Enzyme Type ID | peroxidase001143 |
Protein Name |
Glutathione peroxidase-like peroxiredoxin 2 EC 1.11.1.24 Glutathione peroxidase homolog 2 GPx 2 |
Gene Name | GPX2 YBR244W YBR1632 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Enzyme Sequence | MTTSFYDLECKDKKGESFKFDQLKGKVVLIVNVASKCGFTPQYKELEELYKKYQDKGFVILGFPCNQFGKQEPGSDEQITEFCQLNYGVTFPIMKKIDVNGSNADSVYNYLKSQKAGLLGFKGIKWNFEKFLVDSNGKVVQRFSSLTKPSSLDQEIQSLLSK |
Enzyme Length | 162 |
Uniprot Accession Number | P38143 |
Absorption | |
Active Site | ACT_SITE 37; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000305|PubMed:16251189 |
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:0000269|PubMed:16251189}; |
DNA Binding | |
EC Number | 1.11.1.24 |
Enzyme Function | FUNCTION: Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Plays an important role in the oxidative stress-induced response in the presence of Ca(2+). Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin) (PubMed:16251189). Involved in sporulation (PubMed:21763276). {ECO:0000269|PubMed:10480913, ECO:0000269|PubMed:11445588, ECO:0000269|PubMed:16251189, ECO:0000269|PubMed:21763276}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (1); Mutagenesis (2) |
Keywords | Antioxidant;Cytoplasm;Disulfide bond;Membrane;Mitochondrion;Mitochondrion inner membrane;Mitochondrion outer membrane;Nucleus;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
Interact With | |
Induction | INDUCTION: By oxidative stress, dependent on transcription factor YAP1 (PubMed:10480913). By oleic acid (PubMed:21763276). {ECO:0000269|PubMed:10480913, ECO:0000269|PubMed:21763276}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21763276}. Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:21763276}. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side {ECO:0000269|PubMed:21763276}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10688190; 11018134; 11679167; 11875065; 12702279; 12816519; 14616057; 15133656; 15135069; 15225652; 15875812; 15953550; 16173060; 18021067; 18178164; 18467557; 18562474; 18719252; 18768136; 19424433; 19536198; 19538123; 20370606; 20726779; 20959147; 21549177; 21695049; 22094416; 22102822; 22449970; 22842922; 22970195; 23198979; 23586741; 24410772; 25173844; 25640729; 26261310; 26713447; 26813659; 27693354; 9315326; |
Motif | |
Gene Encoded By | |
Mass | 18,406 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=170 uM for H(2)O(2) (using glutathione as electron donor) {ECO:0000269|PubMed:16251189}; KM=313 uM for tert-butyl hydroperoxide (using glutathione as electron donor) {ECO:0000269|PubMed:16251189}; KM=20 uM for H(2)O(2) (using thioredoxin as electron donor) {ECO:0000269|PubMed:16251189}; KM=62.5 uM for tert-butyl hydroperoxide (using glutathione as electron donor) {ECO:0000269|PubMed:16251189}; Vmax=0.27 umol/min/mg enzyme for H(2)O(2) (using glutathione as electron donor) {ECO:0000269|PubMed:16251189}; Vmax=0.295 umol/min/mg enzyme for tert-butyl hydroperoxide (using glutathione as electron donor) {ECO:0000269|PubMed:16251189}; Vmax=2.6 umol/min/mg enzyme for H(2)O(2) (using thioredoxin as electron donor) {ECO:0000269|PubMed:16251189}; Vmax=1 umol/min/mg enzyme for tert-butyl hydroperoxide (using thioredoxin as electron donor) {ECO:0000269|PubMed:16251189}; |
Metal Binding | |
Rhea ID | RHEA:62620 |
Cross Reference Brenda |