IED ID | IndEnz0018001443 |
Enzyme Type ID | peroxidase001443 |
Protein Name |
Lactoperoxidase LPO EC 1.11.1.7 Lacrimal gland peroxidase |
Gene Name | LPO |
Organism | Mesocricetus auratus (Golden hamster) |
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 Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster) |
Enzyme Sequence | MKVLLRLPALLASLTLLQMAASTRNATRTATIRETVDEVKVQVNKAFLDSRDRLKTDMSNLAPTVRHLSGYLKQAKGRTRTAIRVGQVWEQSLKRLRRMVPLTNVTGQGLDLTSLSWEVGCGHPAPTVTCNISNPYRTITGDCNNRKNPELGSANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPQPRDVSNQVLDYLNEEEILDQNRSLLFMQWGQIVDHDLDFAPETEMGSDNYSKAQCDELCIQGDNCFPIMFPKGDPKLKTQGKCLPFFRAGFVCPTSPYQSLAREQINALTSFMDASMVYGSEPSLANRLRNLSSPLGLMAVNEEVSDHGRPLLPFVNVKPSPCEVINRTAGVPCFLAGDSRASEQILLATSHTLFLREHNRLARELSRLNPQWDGEKLYQEARRIMGALIQIITFRDYLPILLGDELQKWIPPYQGYKETVDPRISNVFTFAFRFGHLEVPSTVSRLDENYQPWGSEPELPLHKLFFNTWRVVKDGGIDPLVRGLLAKKAKLAHQDKMMTGELRNMLFQPNHTVHGFDLAAINIQRCRDHGQPGYNSWRAFCGLSQPKTLEELSAVLRNEVLAKKLMDLYGTPDNIDIWLGAIAEPLVRRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRDSLQKMSFSRLVCDNTGINKVPLNPFQPNSYPHSFVDCSAIEKLDLTPWASVKK |
Enzyme Length | 710 |
Uniprot Accession Number | Q8R481 |
Absorption | |
Active Site | ACT_SITE 224; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Activity Regulation | |
Binding Site | BINDING 223; /note=Heme b; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; BINDING 373; /note=Heme b; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
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; Evidence={ECO:0000250|UniProtKB:A5JUY8}; |
DNA Binding | |
EC Number | 1.11.1.7 |
Enzyme Function | FUNCTION: Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN). {ECO:0000250|UniProtKB:A5JUY8}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (2); Chain (1); Disulfide bond (6); Glycosylation (5); Metal binding (6); Modified residue (2); Propeptide (1); Signal peptide (1); Site (1) |
Keywords | Antimicrobial;Calcium;Disulfide bond;Glycoprotein;Heme;Iron;Metal-binding;Nitration;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Repressed by the androgen dihydrotestosterone (DHT) and the estrogen estradiol (E2) (at protein level). {ECO:0000269|PubMed:16469299}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16469299}. Note=Secreted by the lacrimal gland into tears. {ECO:0000269|PubMed:16469299}. |
Modified Residue | MOD_RES 313; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P80025; MOD_RES 480; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:P11678 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 80,219 |
Kinetics | |
Metal Binding | METAL 225; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 299; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 301; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 303; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 305; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 466; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |