| IED ID | IndEnz0018001489 |
| Enzyme Type ID | peroxidase001489 |
| Protein Name |
Thiol peroxidase Tpx EC 1.11.1.24 Peroxiredoxin tpx Prx Scavengase p20 Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin |
| Gene Name | tpx yzzJ b1324 JW1317 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSQTVHFQGNPVTVANSIPQAGSKAQTFTLVAKDLSDVTLGQFAGKRKVLNIFPSIDTGVCAASVRKFNQLATEIDNTVVLCISADLPFAQSRFCGAEGLNNVITLSTFRNAEFLQAYGVAIADGPLKGLAARAVVVIDENDNVIFSQLVDEITTEPDYEAALAVLKA |
| Enzyme Length | 168 |
| Uniprot Accession Number | P0A862 |
| Absorption | |
| Active Site | ACT_SITE 61; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:12514184" |
| 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:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:12514184}; |
| 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. Has a preference for alkyl hydroperoxides and acts as lipid peroxidase to inhibit bacterial membrane oxidation. Acts as principal antioxidant during anaerobic growth. {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:12514184, ECO:0000269|PubMed:14676195}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Disulfide bond (1); Domain (1); Helix (6); Initiator methionine (1); Mutagenesis (3); Sequence conflict (1); Turn (1) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Oxidoreductase;Periplasm;Peroxidase;Redox-active center;Reference proteome |
| Interact With | P0A8E1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7499381}. Cytoplasm {ECO:0000269|PubMed:19054092}. Note=Forms a mixed disulfide with cytoplasmic thioredoxin (trx1). {ECO:0000269|PubMed:19054092}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1QXH; 3HVS; 3HVV; 3HVX; 3I43; 4AF2; |
| Mapped Pubmed ID | 15004283; 16606699; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 17,835 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1730 uM for H(2)O(2) {ECO:0000269|PubMed:12514184}; KM=9.1 uM for cumene hydroperoxide {ECO:0000269|PubMed:12514184}; KM=25.5 uM for Trx1 (using H(2)O(2) as substrate) {ECO:0000269|PubMed:12514184}; KM=22.5 uM for Trx1 (using cumene hydroperoxide as substrate) {ECO:0000269|PubMed:12514184}; Note=kcat is 76.0 sec(-1) with H(2)O(2) as substrate and 70.1 sec(-1) with cumene hydroperoxide as substrate. {ECO:0000269|PubMed:12514184}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.7; |