| IED ID | IndEnz0018000136 |
| Enzyme Type ID | peroxidase000136 |
| Protein Name |
Alkyl hydroperoxide reductase C MtAhpC EC 1.11.1.28 Peroxiredoxin Thioredoxin peroxidase |
| Gene Name | ahpC Rv2428 |
| 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 | MPLLTIGDQFPAYQLTALIGGDLSKVDAKQPGDYFTTITSDEHPGKWRVVFFWPKDFTFVCPTEIAAFSKLNDEFEDRDAQILGVSIDSEFAHFQWRAQHNDLKTLPFPMLSDIKRELSQAAGVLNADGVADRVTFIVDPNNEIQFVSATAGSVGRNVDEVLRVLDALQSDELCACNWRKGDPTLDAGELLKASA |
| Enzyme Length | 195 |
| Uniprot Accession Number | P9WQB7 |
| Absorption | |
| Active Site | ACT_SITE 61; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000305|PubMed:10766746, ECO:0000305|PubMed:12084012, ECO:0000305|PubMed:15178486" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + an alcohol + H2O; Xref=Rhea:RHEA:62636, Rhea:RHEA-COMP:10502, Rhea:RHEA-COMP:16355, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.11.1.28; Evidence={ECO:0000269|PubMed:12084012, ECO:0000269|PubMed:14871480}; |
| DNA Binding | |
| EC Number | 1.11.1.28 |
| 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. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. Does not however seem to play a role in detoxification of isoniazid. {ECO:0000269|PubMed:10766746, ECO:0000269|PubMed:11799204, ECO:0000269|PubMed:12084012}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Disulfide bond (3); Domain (1); Helix (9); Initiator methionine (1); Mutagenesis (6); Turn (1) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome;Stress response |
| Interact With | |
| Induction | INDUCTION: Induced in isoniazid (INH)-resistant, KatG-deficient strains as well as in INH-sensitive strains when challenged with the drug. Increased expression in these strains probably compensates for loss of katG activity in detoxification of organic peroxides. A possible member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. {ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:8658136}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2BMX; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,566 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.38 mM for tert-butyl hydroperoxide {ECO:0000269|PubMed:12084012}; KM=0.2 uM for tert-butyl hydroperoxide (using AhpD as electron donor) {ECO:0000269|PubMed:14871480}; KM=5.1 uM for tert-butyl hydroperoxide (using thioredoxin TrxC as electron donor) {ECO:0000269|PubMed:14871480}; KM=65.7 uM for AhpD (using tert-butyl hydroperoxide as substrate) {ECO:0000269|PubMed:14871480}; KM=5.6 uM for TrxC (using tert-butyl hydroperoxide as substrate) {ECO:0000269|PubMed:14871480}; Note=kcat is 0.6 sec(-1) with tert-butyl hydroperoxide as substrate and AhpD as reductant and 0.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant. {ECO:0000269|PubMed:14871480}; |
| Metal Binding | |
| Rhea ID | RHEA:62636 |
| Cross Reference Brenda | 1.11.1.28; |