IED Industry Enzyme Database

Detail Information for IndEnz0018000713
IED ID IndEnz0018000713
Enzyme Type ID peroxidase000713
Protein Name Thyroid peroxidase
TPO
EC 1.11.1.8
Gene Name Tpo
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 MRTLGAMAIMLVVMGTVIFLSFILRSRDILCGKTMKSHVISAVETSQLMVDHAVYNTMKRNLKKREVLSPAQLLSFFKLPESTSGAISRAAEIMETSIQVMKREQSQFSTDALSADILGTIANLSGCLPFMLPPRCPDTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQSTSTAAFWGGVDCQLTCENQNPCFPIQLPSNSSGTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPFATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFPQDFESCEDIPSMDLELWRETFPQDDKCVFPEEVDNGNFVHCEESGKLVLVYSCFHGYKLQGQEQVTCTQKGWDSEPPVCKDVNECADLTHPPCHPSAQCKNTKGSFQCVCTDPYVLGEDEKTCIDSGRLPRASWVSIALGALLIGGLASLTWIVICRWTHADKKATLPITERVTTQSGCRKSQGRGISPHKAAAQDTGQEPASGSRVLLCE
Enzyme Length 914
Uniprot Accession Number P35419
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"; /evidence="ECO:0000250"; BINDING 387; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250"
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48956, Rhea:RHEA-COMP:12274, Rhea:RHEA-COMP:12275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:46858, ChEBI:CHEBI:90870; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48960, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O; Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12277, Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90871, ChEBI:CHEBI:90872, ChEBI:CHEBI:90873; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine + [thyroglobulin]-dehydroalanine + 2 H2O; Xref=Rhea:RHEA:48968, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12278, Rhea:RHEA-COMP:12279, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871, ChEBI:CHEBI:90873, ChEBI:CHEBI:90874; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933};
DNA Binding
EC Number 1.11.1.8
Enzyme Function FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000250|UniProtKB:P09933}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
nucleotide Binding
Features Active site (1); Binding site (2); Chain (1); Disulfide bond (10); Domain (2); Glycosylation (5); Metal binding (6); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords Calcium;Disulfide bond;EGF-like domain;Glycoprotein;Heme;Hydrogen peroxide;Iron;Membrane;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Signal;Sushi;Thyroid hormones biosynthesis;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity). {ECO:0000250}.; PTM: Cleaved in its N-terminal part. {ECO:0000250}.
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10440727; 11687289; 12432093; 12766619; 12815622; 1354596; 14651853; 14681479; 15452344; 15927672; 16150900; 16762971; 20573721; 21149592; 21224471; 21267068; 21677750; 22132122; 23563309; 23707896; 24265449; 24297261; 25127920; 2691880; 28067429; 28898113; 30446499; 4346605; 7759120; 8027236; 8088780; 8088836; 8390965; 8630490; 9590297;
Motif
Gene Encoded By
Mass 101,342
Kinetics
Metal Binding METAL 234; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 313; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 315; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 317; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 319; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 482; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298
Rhea ID RHEA:23336; RHEA:48956; RHEA:48960; RHEA:48964; RHEA:48968
Cross Reference Brenda