| IED ID | IndEnz0018001659 |
| Enzyme Type ID | peroxidase001659 |
| Protein Name |
Thiol peroxidase Tpx EC 1.11.1.24 Peroxiredoxin tpx Prx Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin |
| Gene Name | tpx Rv1932 MTCY09F9.32c |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MAQITLRGNAINTVGELPAVGSPAPAFTLTGGDLGVISSDQFRGKSVLLNIFPSVDTPVCATSVRTFDERAAASGATVLCVSKDLPFAQKRFCGAEGTENVMPASAFRDSFGEDYGVTIADGPMAGLLARAIVVIGADGNVAYTELVPEIAQEPNYEAALAALGA |
| Enzyme Length | 165 |
| Uniprot Accession Number | P9WG35 |
| Absorption | |
| Active Site | ACT_SITE 60; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000250|UniProtKB:P0A862, ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000305|PubMed:16884737" |
| 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:14871480}; |
| 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. {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:14871480}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Helix (5); Mutagenesis (3); Turn (1) |
| Keywords | 3D-structure;Antioxidant;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1XVQ; 1Y25; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,896 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.5 uM for tert-butyl hydroperoxide (using thioredoxin TrxB as electron donor) {ECO:0000269|PubMed:14871480}; KM=184.5 uM for tert-butyl hydroperoxide (using thioredoxin TrxC as electron donor) {ECO:0000269|PubMed:14871480}; KM=2.0 uM for TrxB (using tert-butyl hydroperoxide as substrate) {ECO:0000269|PubMed:14871480}; KM=120.7 uM for TrxC (using tert-butyl hydroperoxide as substrate) {ECO:0000269|PubMed:14871480}; Note=kcat is 0.70 sec(-1) with tert-butyl hydroperoxide as substrate and TrxB as reductant and 11.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant. {ECO:0000269|PubMed:14871480}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |