LPO

Summary

Gene Symbol: LPO
Description: lactoperoxidase
Alias: lactoperoxidase, lactoperoxydase
Species: cow
Products:     LPO

Top Publications

  1. Aune T, Thomas E. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Eur J Biochem. 1977;80:209-14 pubmed
  2. Dull T, Uyeda C, Strosberg A, Nedwin G, Seilhamer J. Molecular cloning of cDNAs encoding bovine and human lactoperoxidase. DNA Cell Biol. 1990;9:499-509 pubmed
    Peptide sequences obtained from cyanogen bromide fragments of bovine lactoperoxidase (bLPO) were used to design oligonucleotide probes for library screening...
  3. Singh A, Singh N, Tiwari A, Sinha M, Kushwaha G, Kaur P, et al. First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases. J Biol Inorg Chem. 2010;15:1099-107 pubmed publisher
    ..To provide answers to these questions, the crystal structure of the complex of lactoperoxidase and 3-amino-1,2,4-triazole (amitrole) has been determined, which revealed the presence of two ligand ..
  4. Seidel A, Parker H, Turner R, Dickerhof N, Khalilova I, Wilbanks S, et al. Uric acid and thiocyanate as competing substrates of lactoperoxidase. J Biol Chem. 2014;289:21937-49 pubmed publisher
    ..Whether it reacts sufficiently rapidly with lactoperoxidase (LPO) to act as a physiological substrate remains unknown...
  5. Colas C, Kuo J, Ortiz de Montellano P. Asp-225 and glu-375 in autocatalytic attachment of the prosthetic heme group of lactoperoxidase. J Biol Chem. 2002;277:7191-200 pubmed
    The heme in lactoperoxidase is attached to the protein by ester bonds between the heme 1- and 5-methyl groups and Glu-375 and Asp-275, respectively...
  6. Koksal Z, Kalin R, Gerni S, Gulcin I, Ozdemir H. The inhibition effects of some natural products on lactoperoxidase purified from bovine milk. J Biochem Mol Toxicol. 2017;31: pubmed publisher
    ..isoliquiritigenin, and 1,1,2,2-tetrakis(p-hydroxyphenyl)ethane (Tetrakis), were investigated against bovine lactoperoxidase (LPO) enzyme...
  7. Brogioni S, Stampler J, Furtmüller P, Feis A, Obinger C, Smulevich G. The role of the sulfonium linkage in the stabilization of the ferrous form of myeloperoxidase: a comparison with lactoperoxidase. Biochim Biophys Acta. 2008;1784:843-9 pubmed publisher
    ..Upon reduction from Fe(III) to Fe(II), lactoperoxidase (LPO) but not myeloperoxidase (MPO) is shown to adopt three distinct active site conformations which depend ..
  8. Watanabe S, Murata S, Kumura H, Nakamura S, Bollen A, Moguilevsky N, et al. Bovine lactoperoxidase and its recombinant: comparison of structure and some biochemical properties. Biochem Biophys Res Commun. 2000;274:756-61 pubmed
    Biochemical properties of bovine lactoperoxidase isolated from milk and recombinant bovine lactoperoxidase expressed by Chinese hamster ovary cells were compared...
  9. Rae T, Goff H. The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l-peptides. J Biol Chem. 1998;273:27968-77 pubmed
    The heme prosthetic group from the bovine milk enzyme lactoperoxidase (LPO), termed heme l, is isolated through an approach that combines proteolytic hydrolysis and reverse-phase high performance liquid chromatographic separation of the ..

More Information

Publications20

  1. Cals M, Mailliart P, Brignon G, Anglade P, Dumas B. Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. Eur J Biochem. 1991;198:733-9 pubmed
    Much is known about bovine lactoperoxidase but no data are available on its primary structure. In this work its main active fraction was isolated from cow's milk and sequenced using a conventional strategy...
  2. Suriano G, Watanabe S, Ghibaudi E, Bollen A, Ferrari R, Moguilevsky N. Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages between heme group and apo-Protein in bovine lactoperoxidase. Bioorg Med Chem Lett. 2001;11:2827-31 pubmed
    ..A.; Otto, C.; Dekker, H. L.; Wever, R. J. Biol. Chem. 1999, 274, 26794), we examined for bovine lactoperoxidase the effect of mutation of Asp225 and Glu375, the residues thought to be responsible for the covalent binding ..
  3. Sheikh I, Singh A, Singh N, Sinha M, Singh S, Bhushan A, et al. Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution. J Biol Chem. 2009;284:14849-56 pubmed publisher
    The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution. It revealed that the SCN(-) ion is bound to LPO in the distal heme cavity...
  4. DePillis G, Ozaki S, Kuo J, Maltby D, Ortiz de Montellano P. Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group. J Biol Chem. 1997;272:8857-60 pubmed
    The covalently bound prosthetic group of lactoperoxidase (LPO) has been obtained by hydrolysis of the protein and identified as a dihydroxylated heme...
  5. Singh A, Smith M, Yamini S, Ohlsson P, Sinha M, Kaur P, et al. Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH. Protein J. 2012;31:598-608 pubmed publisher
    b>Lactoperoxidase (LPO) is a hemeprotein catalyzing the oxidation of thiocyanate and I(-) into antimicrobials and small aromatic organics after being itself oxidized by H(2)O(2)...
  6. Boscolo B, Leal S, Ghibaudi E, Gomes C. Lactoperoxidase folding and catalysis relies on the stabilization of the alpha-helix rich core domain: a thermal unfolding study. Biochim Biophys Acta. 2007;1774:1164-72 pubmed
    b>Lactoperoxidase (LPO) belongs to the mammalian peroxidase family and catalyzes the oxidation of halides, pseudo-halides and a number of aromatic substrates at the expense of hydrogen peroxide...
  7. Singh A, Singh N, Sharma S, Shin K, Takase M, Kaur P, et al. Inhibition of lactoperoxidase by its own catalytic product: crystal structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3-A resolution. Biophys J. 2009;96:646-54 pubmed publisher
    ..b>Lactoperoxidase is a heme containing an enzyme that catalyzes the inactivation of a wide range of microorganisms...
  8. Singh A, Singh N, Sinha M, Bhushan A, Kaur P, Srinivasan A, et al. Binding modes of aromatic ligands to mammalian heme peroxidases with associated functional implications: crystal structures of lactoperoxidase complexes with acetylsalicylic acid, salicylhydroxamic acid, and benzylhydroxamic acid. J Biol Chem. 2009;284:20311-8 pubmed publisher
    The binding and structural studies of bovine lactoperoxidase with three aromatic ligands, acetylsalicylic acid (ASA), salicylhydoxamic acid (SHA), and benzylhydroxamic acid (BHA) show that all the three compounds bind to lactoperoxidase ..
  9. Singh A, Kumar R, Pandey N, Singh N, Sinha M, Bhushan A, et al. Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases: binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2.7 A resolution. J Biol Chem. 2010;285:1569-76 pubmed publisher
    Isoniazid (INH) is an anti-tuberculosis prodrug that is activated by mammalian lactoperoxidase and Mycobacterium tuberculosis catalase peroxidase (MtCP)...
  10. Souza C, Maitra D, Saed G, Diamond M, Moura A, Pennathur S, et al. Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases. PLoS ONE. 2011;6:e27641 pubmed publisher
    b>Lactoperoxidase (LPO) is the major consumer of hydrogen peroxide (H(2)O(2)) in the airways through its ability to oxidize thiocyanate (SCN(-)) to produce hypothiocyanous acid, an antimicrobial agent...
  11. Thomas E, Aune T. Susceptibility of Escherichia coli to bactericidal action of lactoperoxidase, peroxide, and iodide or thiocyanate. Antimicrob Agents Chemother. 1978;13:261-5 pubmed
    The bactericidal action that results from lactoperoxidase-catalyzed oxidation of iodide or thiocyanate was studied, using Escherichia coli as the test organism...