Detail Information for IndEnz0018000701
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