| IED ID | IndEnz0018000012 |
| Enzyme Type ID | peroxidase000012 |
| Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Peroxidase/catalase |
| Gene Name | katG Rv1908c MTCY180.10 |
| 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 | MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR |
| Enzyme Length | 740 |
| Uniprot Accession Number | P9WIE5 |
| Absorption | |
| Active Site | ACT_SITE 108; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01961; ACT_SITE 321; /note=Tryptophan radical intermediate; /evidence=ECO:0000269|PubMed:18052167 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9006925}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9006925}; |
| DNA Binding | |
| EC Number | 1.11.1.21 |
| Enzyme Function | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H) (PubMed:9006925, PubMed:18178143). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst (PubMed:8658136, PubMed:15165233). Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages (PubMed:10080924). {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:10080924, ECO:0000269|PubMed:15165233, ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:8658136, ECO:0000269|PubMed:9006925}.; FUNCTION: Might be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC. {ECO:0000269|PubMed:10463167}.; FUNCTION: Catalyzes the oxidative activation of the antitubercular pro-drug isoniazid (INH) to generate an isonicotinoyl radical that then reacts nonenzymatically with NAD to form an isonicotinoyl-NAD adduct which inhibits InhA. {ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:24185282, ECO:0000269|PubMed:9006925, ECO:0000269|PubMed:9634230}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for the catalase activity and 4.5-5.5 for the peroxidase activity (PubMed:9006925). Optimum pH is 4.75 for the peroxidase activity (PubMed:18178143). {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9006925}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (1); Cross-link (2); Helix (50); Metal binding (1); Mutagenesis (6); Natural variant (7); Sequence conflict (2); Site (1); Turn (9) |
| Keywords | 3D-structure;Antibiotic resistance;Heme;Hydrogen peroxide;Iron;Metal-binding;Organic radical;Oxidoreductase;Peroxidase;Reference proteome;Virulence |
| Interact With | |
| Induction | INDUCTION: By treatment with H(2)O(2) (PubMed:8658136). Repressed by FurA (PubMed:11401695). {ECO:0000269|PubMed:11401695, ECO:0000269|PubMed:8658136}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme (By similarity). The formation of the Trp-Tyr-Met cross-link is autocatalytic (PubMed:15840564). {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15840564}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5); Electron microscopy (6) |
| Cross Reference PDB | 1SJ2; 2CCA; 2CCD; 4C50; 4C51; 7A2I; 7A7A; 7A7C; 7A8Z; 7AA3; 7AG8; |
| Mapped Pubmed ID | 33444527; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,605 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for H(2)O(2) in the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143}; KM=225 mM for H(2)O(2) in the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143}; KM=5.18 mM for H(2)O(2) in the catalase reaction (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:9006925}; KM=360 uM for H(2)O(2) in the peroxidase reaction {ECO:0000269|PubMed:18178143}; KM=67 uM for ABTS {ECO:0000269|PubMed:18178143}; KM=192 uM for isoniazid (at pH 7.2) {ECO:0000269|PubMed:24185282}; Vmax=7620 umol/min/mg enzyme for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143}; Vmax=5700 umol/min/mg enzyme for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143}; Vmax=14 umol/min/mg enzyme for the peroxidase reaction with ABTS as substrate {ECO:0000269|PubMed:18178143}; Note=kcat is 10100 sec(-1) for the catalase reaction (at pH 7.0 and 25 degrees Celsius). {ECO:0000269|PubMed:9006925}; |
| Metal Binding | METAL 270; /note="Iron (heme b axial ligand); via tele nitrogen"; /evidence="ECO:0000269|PubMed:15231843, ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:24185282, ECO:0007744|PDB:1SJ2, ECO:0007744|PDB:2CCA, ECO:0007744|PDB:2CCD, ECO:0007744|PDB:4C51" |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda | 1.11.1.21; |