| IED ID | IndEnz0018000699 |
| Enzyme Type ID | peroxidase000699 |
| Protein Name |
Lactoperoxidase LPO WBLP EC 1.11.1.7 |
| Gene Name | LPO |
| Organism | Bubalus bubalis (Domestic water buffalo) |
| 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 Bubalus Bubalus bubalis (Domestic water buffalo) |
| Enzyme Sequence | MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQLSEYFKHAKGQTRTAIRNGQVWEESFKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLTRGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKFSFSRLICDNTHITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN |
| Enzyme Length | 712 |
| Uniprot Accession Number | A5JUY8 |
| Absorption | |
| Active Site | ACT_SITE 226; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298" |
| Activity Regulation | |
| Binding Site | BINDING 225; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6"; BINDING 375; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6" |
| 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:12071645, ECO:0000269|PubMed:19339248}; |
| 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:0000269|PubMed:12071645}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:12071645}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:12071645}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (21); Binding site (2); Chain (1); Disulfide bond (7); Glycosylation (9); Helix (29); Metal binding (6); Modified residue (2); Propeptide (1); Sequence conflict (9); Signal peptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Nitration;Oxidoreductase;Peroxidase;Phosphoprotein;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12071645, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068}. |
| Modified Residue | MOD_RES 315; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.6"; 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 (7) |
| Cross Reference PDB | 2GJM; 2O86; 2Z5Z; 3ERH; 3FAQ; 3FNL; 4Y55; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,698 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (at 60 degrees Celsius) {ECO:0000269|PubMed:12071645}; KM=0.77 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (at 25 degrees Celsius) {ECO:0000269|PubMed:12071645}; |
| Metal Binding | METAL 227; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6"; METAL 301; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6"; METAL 303; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6"; METAL 305; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6"; METAL 307; /note="Calcium"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6"; METAL 468; /note="Iron (heme b axial ligand)" |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |