| IED ID | IndEnz0018000703 |
| Enzyme Type ID | peroxidase000703 |
| Protein Name |
Myeloperoxidase MPO EC 1.11.2.2 Cleaved into: Myeloperoxidase light chain; Myeloperoxidase heavy chain |
| Gene Name | Mpo |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MKLLLALAGLLAPLAMLQTSNGATPALLGEVENSVVLSCMEEAKQLVDRAYKERRESIKRSLQSGSASPTELLFYFKQPVAGTRTAVRAADYLHVALDLLKRKLQPLWPRPFNVTDVLTPAQLNLLSVSSGCAYQDVRVTCPPNDKYRTITGHCNNRRSPTLGASNRAFVRWLPAEYEDGVSMPFGWTPGVNRNGFKVPLARQVSNAIVRFPNDQLTKDQERALMFMQWGQFLDHDITLTPEPATRFSFFTGLNCETSCLQQPPCFPLKIPPNDPRIKNQKDCIPFFRSCPACTRNNITIRNQINALTSFVDASGVYGSEDPLARKLRNLTNQLGLLAINTRFQDNGRALMPFDSLHDDPCLLTNRSARIPCFLAGDMRSSEMPELTSMHTLFVREHNRLATQLKRLNPRWNGEKLYQEARKIVGAMVQIITYRDYLPLVLGPAAMKKYLPQYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLNNQYRPTGPNPRVPLSKVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIVVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPSTVGELGTVLKNLELARKLMAQYGTPNNIDIWMGGVSEPLEPNGRVGQLLACLIGTQFRKLRDGDRFWWENPGVFSKQQRQALASISLPRIICDNTGITTVSKNNIFMSNTYPRDFVSCNTLPKLNLTSWKET |
| Enzyme Length | 718 |
| Uniprot Accession Number | P11247 |
| Absorption | |
| Active Site | ACT_SITE 235; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 234; /note="Heme b; covalent, via 3 links"; /evidence="ECO:0000250"; BINDING 382; /note="Heme b; covalent, via 3 links"; /evidence="ECO:0000250"; BINDING 383; /note="Heme b; covalent, via 3 links"; /evidence="ECO:0000250" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=chloride + H(+) + H2O2 = H2O + hypochlorous acid; Xref=Rhea:RHEA:28218, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17996, ChEBI:CHEBI:24757; EC=1.11.2.2; Evidence={ECO:0000269|PubMed:11593004}; |
| DNA Binding | |
| EC Number | 1.11.2.2 |
| Enzyme Function | FUNCTION: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity (PubMed:11593004). Mediates the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low density lipoprotein particles and limits vascular damage (By similarity). {ECO:0000250|UniProtKB:P05164, ECO:0000269|PubMed:11593004}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (3); Chain (3); Disulfide bond (6); Glycosylation (6); Metal binding (6); Modified residue (1); Propeptide (1); Sequence conflict (10); Signal peptide (1); Site (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lysosome;Metal-binding;Oxidation;Oxidoreductase;Peroxidase;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | MOD_RES 290; /note=Cysteine sulfenic acid (-SOH); /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10085024; 10945472; 10979934; 11108938; 11181641; 11217851; 11410366; 11792727; 11831441; 11980719; 12085336; 12089442; 12359714; 12466851; 12615902; 12755332; 1346798; 14651853; 14657339; 14681479; 15020295; 15159534; 15507755; 15579460; 15661916; 15711547; 15790660; 15850779; 15911707; 15914564; 16266986; 16416089; 16489219; 16517735; 16585600; 1675432; 16914663; 16956579; 17035062; 17108314; 17134831; 17200182; 17316569; 17384464; 17476283; 17660555; 17828273; 17901846; 1794058; 17991873; 18055546; 18272685; 18281288; 18353866; 18424617; 18505433; 18617697; 18619953; 19039769; 19221870; 19305414; 19383970; 19494324; 19778788; 19907415; 20018843; 20035012; 20061576; 20153732; 20156554; 20230750; 20647008; 20980678; 21267068; 21543212; 2164461; 21677750; 21704008; 21930915; 22082678; 22211924; 22241891; 22322369; 22479306; 22955884; 22976954; 23066164; 23268804; 23285030; 23306200; 23384999; 23434459; 23509155; 23532856; 23593274; 23603832; 23665205; 23686858; 23691142; 24062488; 24194600; 24436331; 24757143; 24976018; 24990898; 25024373; 2567264; 25885273; 25922506; 26003521; 26262998; 26358260; 26446156; 26560636; 26573963; 26949091; 27573815; 27626380; 28069522; 28186568; 28314592; 28359218; 28385925; 28404615; 28432145; 28667835; 28796788; 28850023; 28971841; 29368549; 29496995; 29673284; 29724896; 29780806; 29903730; 3029127; 30565999; 30889221; 31123149; 31393790; 31611761; 32035161; 32050431; 33391487; 33486744; 33668735; 34172578; 34568331; 7514570; 7557989; 7557995; 7579889; 7594550; 7601457; 7650394; 7666191; 7789623; 7920656; 8182931; 8188678; 8384306; 8423056; 8449498; 8530103; 8662231; 8683100; 8777716; 8835527; 9001423; 9087431; 9177778; 9434953; 9611252; 9819431; 9864150; |
| Motif | |
| Gene Encoded By | |
| Mass | 81,182 |
| Kinetics | |
| Metal Binding | METAL 236; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 308; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 310; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 312; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 314; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 476; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:28218 |
| Cross Reference Brenda |