Detail Information for IndEnz0018000005
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