Detail Information for IndEnz0018001443
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