| IED ID | IndEnz0018000157 |
| Enzyme Type ID | peroxidase000157 |
| Protein Name |
Peroxiredoxin Bcp EC 1.11.1.24 Bacterioferritin comigratory protein Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin Bcp |
| Gene Name | bcp b2480 JW2465 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVDVLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKSFMGKTYDGIHRISFLIDADGKIEHVFDDFKTSNHHDVVLNWLKEHA |
| Enzyme Length | 156 |
| Uniprot Accession Number | P0AE52 |
| Absorption | |
| Active Site | ACT_SITE 46; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000269|PubMed:10644761, ECO:0000269|PubMed:19298085" |
| 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:10644761, ECO:0000269|PubMed:21910476}; |
| 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. {ECO:0000269|PubMed:21910476}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1) |
| Keywords | Antioxidant;Direct protein sequencing;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16606699; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 17,634 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76.1 uM for H(2)O(2) (using glutathione Grx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=99.5 uM for cumene hydroperoxide (using glutathione Grx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=6800 uM for tert-butyl hydroperoxide (using glutathione Grx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=14.6 uM for H(2)O(2) (using thioredoxin Trx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=21.6 uM for cumene hydroperoxide (using thioredoxin Trx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=574 uM for tert-butyl hydroperoxide (using thioredoxin Trx1 as electron donor) {ECO:0000269|PubMed:21910476}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |