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    LPO lactoperoxidase [ Bos taurus (cattle) ]

    Gene ID: 280844, updated on 6-Jun-2024

    Summary

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    Official Symbol
    LPOprovided by VGNC
    Official Full Name
    lactoperoxidaseprovided by VGNC
    Primary source
    VGNC:VGNC:30970
    See related
    BGD:BT12484; Ensembl:ENSBTAG00000012780
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Bos taurus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
    Orthologs
    human mouse all
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    Genomic context

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    See LPO in Genome Data Viewer
    Location:
    chromosome: 19
    Exon count:
    15
    Annotation release Status Assembly Chr Location
    RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 19 NC_037346.1 (9216246..9246107)

    Chromosome 19 - NC_037346.1Genomic Context describing neighboring genes Neighboring gene MKS transition zone complex subunit 1 Neighboring gene uncharacterized LOC112442599 Neighboring gene U6 spliceosomal RNA Neighboring gene U6 spliceosomal RNA Neighboring gene myeloperoxidase Neighboring gene TSPO associated protein 1 Neighboring gene uncharacterized LOC132342999

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_037346.1 Chromosome 19 Reference ARS-UCD2.0 Primary Assembly

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The inhibition effects of some natural products on lactoperoxidase purified from bovine milk. Köksal Z, et al. J Biochem Mol Toxicol, 2017 Sep. PMID 28594102
    2. Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH. Singh AK, et al. Protein J, 2012 Oct. PMID 22886082
    3. Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases. Souza CE, et al. PLoS One, 2011. PMID 22132121, Free PMC Article
    4. First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases. Singh AK, et al. J Biol Inorg Chem, 2010 Sep. PMID 20461536
    5. 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. Singh AK, et al. J Biol Chem, 2010 Jan 8. PMID 19907057, Free PMC Article

    See all (22) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Bovine LPO enzyme was effectively inhibited by phenolic molecules. Ki values of these natural products were found as 0.20 +/- 0.09, 0.22 +/- 0.17, 0.49 +/- 0.11, 0.49 +/- 0.27, and 1.20 +/- 0.25 muM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition.
      Title: The inhibition effects of some natural products on lactoperoxidase purified from bovine milk.
    2. establish urate as a likely physiological substrate for LPO that will influence host defense and give rise to reactive electrophilic metabolites
      Title: Uric acid and thiocyanate as competing substrates of lactoperoxidase.
    3. Studied the 3-dimensional structure of CO-LPO at 2.0A resolution and infrared (IR) spectra of the iron-bound CO stretch from pH 3 to 8.8 at 1 cm(-1) resolution.
      Title: Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH.
    4. LPO serve as a catalytic sink for HOCl (hypochlorous acid), while HOCl serves to modulate LPO catalytic activity, bioavailability, and function.
      Title: Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases.
    5. Results describe the crystal structure of the complex of lactoperoxidase and 3-amino-1,2,4-triazole (amitrole), which revealed the presence of two ligand molecules, one in the substrate binding site and the second in the hydrophobic channel.
      Title: First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases.
    6. LPO can be used for INH activation. It also indicates that the conversion of INH into isonicotinoyl radical by LPO may be the cause of INH toxicity.
      Title: 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.
    7. The structures of three complexes of LPO with aromatic substrate, acetylsalicylic acid, and two aromatic inhibitors salicylhydroxamic acid and benzylhydroxamic acid indicate the distinctiveness in their modes of binding as a substrate and as an inhibitor.
      Title: 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.
    8. The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution.
      Title: Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution.
    9. lactoperoxidase containing thiocyanate (SCN(-)) and hypothiocyanate (OSCN(-)) ions were purified and crystallized; the structure was determined at 2.3-A resolution and refined to R(cryst) and R(free) factors of 0.184 and 0.221, respectively
      Title: Inhibition of lactoperoxidase by its own catalytic product: crystal structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3-A resolution.
    10. Comparative spectroscopic analysis of the ferrous forms of LPO, wild-type MPO and the variants demonstrate that a single, stable ferrous form of MPO is present only in those proteins which retain an intact sulfonium linkage.
      Title: The role of the sulfonium linkage in the stabilization of the ferrous form of myeloperoxidase: a comparison with lactoperoxidase.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Pathways from PubChem

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    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables heme binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    enables thiocyanate peroxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in response to oxidative stress IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in extracellular space IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    lactoperoxidase
    Names
    lactoperoxydase
    NP_776358.1
    XP_010813999.2
    XP_010814001.1
    XP_010814003.1
    XP_015313999.1
    XP_024835317.1
    XP_024835319.1
    XP_024835324.1
    XP_059733680.1
    XP_059733681.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_173933.2 → NP_776358.1  lactoperoxidase precursor

      See identical proteins and their annotated locations for NP_776358.1

      Status: PROVISIONAL

      Source sequence(s)
      M58150
      UniProtKB/Swiss-Prot
      P80025
      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Related
      ENSBTAP00000092409.1, ENSBTAT00000116703.1
      Conserved Domains (1) summary
      cd09824
      Location:283 → 694
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

    RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference ARS-UCD2.0 Primary Assembly

    Genomic

    1. NC_037346.1 Reference ARS-UCD2.0 Primary Assembly

      Range
      9216246..9246107
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_059877697.1 → XP_059733680.1  lactoperoxidase isoform X4

      UniProtKB/TrEMBL
      A0AAA9TJ67, A0AAA9TV47, G3MXZ0
      Related
      ENSBTAP00000098374.1, ENSBTAT00000128808.1

    2. XM_024979556.2 → XP_024835324.1  lactoperoxidase isoform X5

      UniProtKB/Swiss-Prot
      P80025
      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Related
      ENSBTAP00000101269.1, ENSBTAT00000119114.1
      Conserved Domains (1) summary
      cd09824
      Location:283 → 694
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

    3. XM_059877698.1 → XP_059733681.1  lactoperoxidase isoform X5

      UniProtKB/Swiss-Prot
      P80025
      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0

    4. XM_010815699.4 → XP_010814001.1  lactoperoxidase isoform X5

      See identical proteins and their annotated locations for XP_010814001.1

      UniProtKB/Swiss-Prot
      P80025
      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Conserved Domains (1) summary
      cd09824
      Location:283 → 694
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

    5. XM_010815697.4 → XP_010813999.2  lactoperoxidase isoform X3

      UniProtKB/TrEMBL
      A0AAA9T6G9, A0AAA9TV47, G3MXZ0
      Related
      ENSBTAP00000091377.1, ENSBTAT00000102963.1
      Conserved Domains (2) summary
      cd09824
      Location:296 → 707
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases
      pfam03098
      Location:151 → 687
      An_peroxidase; Animal haem peroxidase

    6. XM_024979551.2 → XP_024835319.1  lactoperoxidase isoform X2

      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Conserved Domains (1) summary
      cd09824
      Location:315 → 726
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

    7. XM_015458513.3 → XP_015313999.1  lactoperoxidase isoform X5

      UniProtKB/Swiss-Prot
      P80025
      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Conserved Domains (1) summary
      cd09824
      Location:283 → 694
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

    8. XM_024979549.2 → XP_024835317.1  lactoperoxidase isoform X1

      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Related
      ENSBTAP00000054415.3, ENSBTAT00000066160.3
      Conserved Domains (1) summary
      cd09824
      Location:333 → 744
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

    9. XM_010815701.4 → XP_010814003.1  lactoperoxidase isoform X5

      See identical proteins and their annotated locations for XP_010814003.1

      UniProtKB/Swiss-Prot
      P80025
      UniProtKB/TrEMBL
      A0AAA9TV47, G3MXZ0
      Conserved Domains (1) summary
      cd09824
      Location:283 → 694
      myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P80025.1 GenPept UniProtKB/Swiss-Prot:P80025

    Gene LinkOut

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