IED ID | IndEnz0018000463 |
Enzyme Type ID | peroxidase000463 |
Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Hydroperoxidase I HPI Peroxidase/catalase |
Gene Name | katG cpeA |
Organism | Rhodobacter capsulatus (Rhodopseudomonas capsulata) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodobacterales Rhodobacteraceae Rhodobacter Rhodobacter capsulatus (Rhodopseudomonas capsulata) |
Enzyme Sequence | MDGKDKATGKCPVMHGAMTAAGVSNTSWWPNALNLDILHQHDTKGNPLNGFDYRAAVKGLDVGLRADLHALMTDSQPWWPADWGHYGGLMIRMAWHAAGSYRAADGRGGGNTGKPARFAPLNSWPDNVSLDKARRLLWPIKKKYGNAVSWADLILFAGTVAYESMGLKTFGFGFGREDIWAPEKDVYWGAEKDWLAPSDGRYGDLAKPETMENPLAAVQMGLIYVNPEGVNGQPDPARTALHIRETFARMGMNDEETVALTAGGHTVGKAHGNGDAKALGPDPEAADVTVRALAGRTRIWAARRRRPSPRGSRAPGPRIRRAGTWAISRCSSGHDWELTKSPAGAWQWKPVTIAEEAKPLDATDLTTRHDPLMTDADMAMKVDPSTMRSVRSSWPIRPPSTTLSRAPGSSCCIATWGRRRATSAPMCPPRIWSAGPGAAGPTGWDVAKVKAQIAASGLSVADLVATAWDSARTFRQSDYRGGANGARIRLAPQKDWAGNEPERLAGACGARTDRGGAGASVADVIVLAGNLGVEQAAAGVSRWRCPSPPVAAMRAAMTDGPSLTCWSRCMTASATG |
Enzyme Length | 576 |
Uniprot Accession Number | P37743 |
Absorption | |
Active Site | ACT_SITE 96; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
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|PROSITE-ProRule:PRU00297}; 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; |
DNA Binding | |
EC Number | 1.11.1.21 |
Enzyme Function | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity. Important for stationary phase survival. {ECO:0000269|PubMed:1577703}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0 for the peroxidase reaction and 6-6.5 for the catalase reaction. {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Cross-link (2); Metal binding (1); Site (1) |
Keywords | Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase |
Interact With | |
Induction | |
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. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 61,517 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; KM=3.7 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; KM=830 mM for H(2)O(2) for the peroxidase reaction {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; KM=16 mM for ABTS for the peroxidase reaction {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; Vmax=10510 umol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; Vmax=5100 umol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; Vmax=5.9 umol/min/mg enzyme for ABTS for the peroxidase reaction {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290}; |
Metal Binding | METAL 265; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Rhea ID | RHEA:30275; RHEA:20309 |
Cross Reference Brenda |