IED Industry Enzyme Database

Detail Information for IndEnz0018000700
IED ID IndEnz0018000700
Enzyme Type ID peroxidase000700
Protein Name Lactoperoxidase
EC 1.11.1.7
Gene Name LPO
Organism Capra hircus (Goat)
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 Caprinae Capra Capra hircus (Goat)
Enzyme Sequence MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLLAKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKLLDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHVTKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN
Enzyme Length 712
Uniprot Accession Number A0A452E9Y6
Absorption
Active Site ACT_SITE 226; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298
Activity Regulation ACTIVITY REGULATION: Inhibited by small molecule methimazole (MMZ). {ECO:0000269|PubMed:27398304}.
Binding Site BINDING 225; /note="Heme b; covalent"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"; BINDING 375; /note="Heme b; covalent"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"
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:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304};
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) (PubMed:10894086). May protect the udder from infection and promote growth in newborns. Inhibits growth of several fungi including A.niger, Trichoderma species, C.cassicola, P.meadii and C.salmonicolor (PubMed:10894086). Does not have anti-fungal activity towards C.albicans and Pythium species (PubMed:10894086). Inhibits growth of several Gram-positive bacteria including some Staphylococcus species and Gram-negative bacteria including E.coli, P.aeruginosa and some Salmonella species (PubMed:10894086). {ECO:0000269|PubMed:10894086}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (28); Binding site (2); Chain (1); Disulfide bond (7); Glycosylation (9); Helix (29); Metal binding (6); Modified residue (2); Propeptide (1); Sequence conflict (7); Signal peptide (1); Site (1); Turn (6)
Keywords 3D-structure;Antibiotic;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:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}.
Modified Residue MOD_RES 315; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18191143; MOD_RES 482; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:P11678
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D X-ray crystallography (19)
Cross Reference PDB 2E9E; 2EFB; 2EHA; 2OJV; 2R5L; 3N8F; 3NAK; 3NIU; 3QF1; 3R55; 3RKE; 3SXV; 4MSF; 4OEK; 4QJQ; 5FF1; 5HPW; 6LF7; 7WCS;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 80,366
Kinetics
Metal Binding METAL 227; /note="Calcium"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"; METAL 301; /note="Calcium"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"; METAL 303; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"; METAL 305; /note="Calcium"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"; METAL 307; /note="Calcium"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"; METAL 468; /note="Iron (heme b axial ligand); via tele nitrogen"; /evidence="ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"
Rhea ID RHEA:56136
Cross Reference Brenda