Detail Information for IndEnz0018000698
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;