IED ID | IndEnz0018000005 |
Enzyme Type ID | peroxidase000005 |
Protein Name |
Eosinophil peroxidase EPO EC 1.11.1.7 Cleaved into: Eosinophil peroxidase light chain; Eosinophil peroxidase heavy chain |
Gene Name | EPX EPER EPO EPP |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARKIMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPFMFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDELRDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLARKFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTKRQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT |
Enzyme Length | 715 |
Uniprot Accession Number | P11678 |
Absorption | |
Active Site | ACT_SITE 233; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Activity Regulation | |
Binding Site | BINDING 232; /note="Heme b; covalent, via 2 links; partial"; BINDING 380; /note="Heme b; covalent, via 2 links" |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; |
DNA Binding | |
EC Number | 1.11.1.7 |
Enzyme Function | FUNCTION: Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis. {ECO:0000269|PubMed:12540536, ECO:0000269|PubMed:18694936}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (2); Chain (2); Disulfide bond (6); Glycosylation (6); Metal binding (6); Modified residue (1); Natural variant (16); Propeptide (1); Sequence conflict (5); Signal peptide (1); Site (1) |
Keywords | Calcium;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Nitration;Oxidoreductase;Peroxidase;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of eosinophils. |
Modified Residue | MOD_RES 488; /note=3'-nitrotyrosine; /evidence=ECO:0000269|PubMed:18694936 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15316147; 15894800; 16336215; 17474147; 19014520; 19439985; 20237496; 20453000; 20501663; 21454806; 22702502; 22750539; 23197886; 23650620; 23931643; 24738159; 24814827; 24937179; 26386352; 26645423; 27519953; 27587397; 27836774; 28260049; |
Motif | |
Gene Encoded By | |
Mass | 81,040 |
Kinetics | |
Metal Binding | METAL 234; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 306; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 308; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 310; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 312; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 474; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |