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LPO lactoperoxidase [ Bos taurus (domestic cattle) ]

Gene ID: 280844, updated on 8-Apr-2026
Official Symbol
LPOprovided by VGNC
Official Full Name
lactoperoxidaseprovided by VGNC
Primary source
VGNC:VGNC:30970
See related
BGD:BT12484; EnsemblRapid:ENSBTAG00070007304
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
all
Try the new Gene page
Try the new Transcripts and proteins table
See LPO in Genome Data Viewer
Location:
chromosome: 19
Exon count:
15
Annotation release Status Assembly Chr Location
RS_2024_12 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 Sequence:
NC_037346.1 Chromosome 19 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

  • Project title: Dominette sequence data
  • BioProject: PRJNA294306
  • Analysis date: Tue Dec 17 08:57:05 2024

Related articles in PubMed

  1. Lactoperoxidase folding and catalysis relies on the stabilization of the alpha-helix rich core domain: a thermal unfolding study. Boscolo B, et al. Biochim Biophys Acta, 2007 Sep. PMID 17698426
  2. Susceptibility of Escherichia coli to bactericidal action of lactoperoxidase, peroxide, and iodide or thiocyanate. Thomas EL, et al. Antimicrob Agents Chemother, 1978 Feb. PMID 348097, Free PMC Article
  3. Oxidation of Escherichia coli sulfhydryl components by the peroxidase-hydrogen peroxide-iodide antimicrobial system. Thomas EL, et al. Antimicrob Agents Chemother, 1978 Jun. PMID 354515, Free PMC Article
  4. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Aune TM, et al. Eur J Biochem, 1977 Oct 17. PMID 562752
  5. Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. Cals MM, et al. Eur J Biochem, 1991 Jun 15. PMID 2050150

See all (24) 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)

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 defense response to bacterium IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in response to oxidative stress IEA
Inferred from Electronic Annotation
more info
 PubMed 
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

NEW Try the new Transcript table

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
    A0AAF6YY46
    Related
    ENSBTAP00070009624.1, ENSBTAT00070016620.1
    Conserved Domains (1) summary
    cd09824
    Location:283 → 694
    myeloperoxidase_like; Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

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, A0AAF6YY46
    Related
    ENSBTAP00070009610.1, ENSBTAT00070016606.1

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

    UniProtKB/Swiss-Prot
    P80025
    UniProtKB/TrEMBL
    A0AAF6YY46
    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
    A0AAF6YY46

  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
    A0AAF6YY46
    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, A0AAF6YY46
    Related
    ENSBTAP00070009588.1, ENSBTAT00070016585.1
    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
    A0AAF6YY46
    Related
    ENSBTAP00070009598.1, ENSBTAT00070016594.1
    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
    A0AAF6YY46
    Related
    ENSBTAP00070009539.1, ENSBTAT00070016535.1
    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
    ENSBTAP00070009641.1, ENSBTAT00070016640.1
    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
    A0AAF6YY46
    Related
    ENSBTAP00070009563.1, ENSBTAT00070016559.1
    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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