Detail Information for IndEnz0018000699
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