IED ID | IndEnz0018000701 |
Enzyme Type ID | peroxidase000701 |
Protein Name |
Lactoperoxidase LPO EC 1.11.1.7 Salivary peroxidase SPO |
Gene Name | LPO SAPX |
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 | MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAMSSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDENYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN |
Enzyme Length | 712 |
Uniprot Accession Number | P22079 |
Absorption | |
Active Site | ACT_SITE 226; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Activity Regulation | |
Binding Site | BINDING 225; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250"; BINDING 375; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250" |
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: Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN) (By similarity). May contribute to airway host defense against infection. {ECO:0000250|UniProtKB:A5JUY8, ECO:0000269|PubMed:12626341}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (6); Glycosylation (4); Metal binding (6); Modified residue (2); Natural variant (7); Propeptide (1); Sequence conflict (2); Signal peptide (1); Site (1) |
Keywords | Alternative splicing;Antimicrobial;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Nitration;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12626341}. |
Modified Residue | MOD_RES 315; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P80025; MOD_RES 482; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:P11678 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15384204; 15894800; 19423540; 19505917; 20237496; 20406964; 20438785; 23042278; 24049667; 24928513; 24974109; 25309750; 27048452; 28653416; |
Motif | |
Gene Encoded By | |
Mass | 80,288 |
Kinetics | |
Metal Binding | METAL 227; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 301; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 303; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 305; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 307; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 468; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |