| IED ID | IndEnz0018000698 |
| Enzyme Type ID | peroxidase000698 |
| Protein Name |
Lactoperoxidase LPO EC 1.11.1.7 |
| Gene Name | LPO |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN |
| Enzyme Length | 712 |
| Uniprot Accession Number | P80025 |
| 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:0000269|PubMed:19339248"; BINDING 375; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000269|PubMed:19339248" |
| 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). May protect the udder from infection and promote growth in newborn calves. Inhibits growth of the following bacterial species: E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis, and S.dysenteriae. {ECO:0000250|UniProtKB:A5JUY8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (30); Binding site (2); Chain (1); Disulfide bond (6); Glycosylation (5); Helix (29); Metal binding (6); Modified residue (2); Mutagenesis (4); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (8) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Calcium;Cleavage on pair of basic residues;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:2050150}. |
| Modified Residue | MOD_RES 315; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248"; MOD_RES 482; /note="3'-nitrotyrosine"; /evidence="ECO:0000250|UniProtKB:P11678" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (48) |
| Cross Reference PDB | 2IPS; 2NQX; 2PT3; 2PUM; 2QPK; 2QQT; 2QRB; 3BXI; 3ERI; 3GC1; 3GCJ; 3GCK; 3GCL; 3I6N; 3KRQ; 3NYH; 3PY4; 3R4X; 3R5O; 3S4F; 3TGY; 3UBA; 3V6Q; 4GM7; 4GN6; 4KSZ; 4NJB; 4PNX; 5B72; 5GH0; 5GLS; 5WV3; 5ZGS; 6A4Y; 6KMK; 6KY7; 6L2J; 6L5G; 6L9T; 6LCO; 6M7E; 7C75; 7D52; 7DLQ; 7DMR; 7DN6; 7DN7; 7VIN; |
| Mapped Pubmed ID | 19465478; 19907057; 20461536; 27986533; 28653416; 29174286; 33427997; 33882424; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,642 |
| Kinetics | |
| Metal Binding | METAL 227; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248"; METAL 301; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248"; METAL 303; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248"; METAL 305; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248"; METAL 307; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248"; METAL 468; /note="Iron (heme b axial ligand)" |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda | 1.11.1.7; |