detection of chemical stimulus involved in sensory perception of bitter taste
response to oxidative stress
hydrogen peroxide catabolic process
thiocyanate metabolic process
cell redox homeostasis
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
4025
76113
Ensembl
ENSG00000167419
ENSMUSG00000009356
UniProt
P22079
n/a
RefSeq (mRNA)
NM_001160102 NM_006151
NM_080420
RefSeq (protein)
NP_001153574 NP_006142
n/a
Location (UCSC)
Chr 17: 58.22 – 58.27 Mb
Chr 11: 87.7 – 87.72 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Lactoperoxidase is a peroxidase enzyme secreted from mammary, salivary and other mucosal glands including the lungs, bronchii and nose[5] that functions as a natural and the first line of defense against bacteria and viruses.[6] Lactoperoxidase is a member of the heme peroxidase family of enzymes. In humans, lactoperoxidase is encoded by the LPO gene.[7][8]
Lactoperoxidase catalyzes the oxidation of several inorganic and organic substrates by hydrogen peroxide.[9] These substrates include bromide and iodide and therefore lactoperoxidase can be categorised as a haloperoxidase. An other important substrate is thiocyanate. The oxidized products produced through the action of this enzyme have potent and non-specific bactericidal and antiviral activities, including destruction of the influenza virus. Lactoperoxidase together with its inorganic ion substrates, hydrogen peroxide, and oxidized products is known as the lactoperoxidase system.[10] Hence LPO is considered a very important defense against invasive bacteria and viral agents such as influenza and the SARS-CoV-2 virus when sufficient iodine is provided.[11][12][13]
The lactoperoxidase system plays an important role in the innate immune system by killing bacteria in milk and mucosal (linings of mostly endodermal origin, covered in epithelium, which are involved in absorption and secretion) secretions hence augmentation of the lactoperoxidase system may have therapeutic applications. Furthermore, addition or augmentation of the lactoperoxidase system has potential applications in controlling bacteria in food and consumer health care products. The lactoperoxidase system does not attack DNA and is not mutagenic.[14] However, under certain conditions, the lactoperoxidase system may contribute to oxidative stress.[15] Furthermore, lactoperoxidase may contribute to the initiation of breast cancer, through its ability to oxidize estrogenic hormones producing free radical intermediates.[16]
^ abcGRCh38: Ensembl release 89: ENSG00000167419 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000009356 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Tenovuo JO (1985). "The peroxidase system in human secretions". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN 978-0-8247-7298-7.
^Pruitt KM, Reiter B (1985). "Biochemistry of peroxidase systems: antimicrobial effects". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN 978-0-8247-7298-7.
^Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ (September 1990). "Molecular cloning of cDNAs encoding bovine and human lactoperoxidase". DNA and Cell Biology. 9 (7): 499–509. doi:10.1089/dna.1990.9.499. PMID 2222811.
^Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F (September 1996). "Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA". Gene. 173 (2): 261–4. doi:10.1016/0378-1119(96)00078-9. PMID 8964511.
^Kohler H, Jenzer H (1989). "Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals". Free Radical Biology & Medicine. 6 (3): 323–39. doi:10.1016/0891-5849(89)90059-2. PMID 2545551.
^Cite error: The named reference isbn0-8247-7298-9 was invoked but never defined (see the help page).
^Rayman MP (November 2020). "Iodine and Selenium as Antiviral Agents: Potential Relevance to SARS-CoV-2 and Covid-19". Archives of Oral and Maxillofacial Surgery. 3 (1): 69. doi:10.36959/379/357. ISSN 2689-8772.
^Derscheid RJ, van Geelen A, Berkebile AR, Gallup JM, Hostetter SJ, Banfi B, et al. (February 2014). "Increased concentration of iodide in airway secretions is associated with reduced respiratory syncytial virus disease severity". American Journal of Respiratory Cell and Molecular Biology. 50 (2): 389–97. doi:10.1165/rcmb.2012-0529OC. PMC 3930944. PMID 24053146.
^Smith ML, Sharma S, Singh TP (September 2021). "Iodide supplementation of the anti-viral duox-lactoperoxidase activity may prevent some SARS-CoV-2 infections". European Journal of Clinical Nutrition. 76 (4): 629–630. doi:10.1038/s41430-021-00995-2. PMC 8408568. PMID 34471253.
^White WE, Pruitt KM, Mansson-Rahemtulla B (February 1983). "Peroxidase-thiocyanate-peroxide antibacterial system does not damage DNA". Antimicrobial Agents and Chemotherapy. 23 (2): 267–72. doi:10.1128/aac.23.2.267. PMC 186035. PMID 6340603.
^Cite error: The named reference pmid7955118 was invoked but never defined (see the help page).
^Cite error: The named reference pmid10994878 was invoked but never defined (see the help page).
viruses. Lactoperoxidase is a member of the heme peroxidase family of enzymes. In humans, lactoperoxidase is encoded by the LPO gene. Lactoperoxidase catalyzes...
of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase. The addition of peroxide with the glutamyl-375 and aspartyl-225 of lactoperoxidase forms...
Margarita (2014). "Combined treatments of high-pressure with the lactoperoxidase system or lactoferrin on the inactivation of Listeria monocytogenes...
to be an important part in the biosynthesis of hypothiocyanite by a lactoperoxidase. Thus the complete absence of thiocyanate or reduced thiocyanate in...
human respiratory tract in a redox reaction catalyzed by the enzyme lactoperoxidase. It has been researched extensively for its capabilities as an alternative...
omniscience London Philharmonic Orchestra Louisiana Philharmonic Orchestra Lactoperoxidase, an antibacterial protein present in milk and saliva This disambiguation...
the lingual papillae. Enzymes and non-enzymatic proteins, such as lactoperoxidase, lysozyme, and lactoferrin, have been used in mouthwashes (e.g., Biotene)...
it also contained enzymes including glucose oxidase, lactoferrin, lactoperoxidase and lysozyme. The PBF (plaque biofilm) product line contained additional...
components of the innate immune system, such as lactoferrin, lysozyme, lactoperoxidase, complement, and proline-rich polypeptides (PRP). A number of cytokines...
oxidizes bromide. The mammalian haloperoxidases myeloperoxidase (MPO), lactoperoxidase (LPO) and eosinophil peroxidase (EPO) are also capable of oxidizing...
biochemical solutions. Sodium azide is an instantaneous inhibitor of lactoperoxidase, which can be useful to stop lactroperoxidase catalyzed 125I protein...
and saliva contain a wide range of antimicrobial compound including lactoperoxidase system, producing hypothiocyanite and lactoferrin, with hypothiocyanite...
clean and contains enough antimicrobial compounds such as lactoferrin, lactoperoxidase, and secretory immunoglobulin A which can help clear pathogens from...
"Mutations affecting the calcium-binding site of myeloperoxidase and lactoperoxidase". Biochemical and Biophysical Research Communications. 281 (4): 1024–9...
Wijkstrom-Frei C, Randell SH, Fernandez VE, Salathe M (January 2007). "The lactoperoxidase system links anion transport to host defense in cystic fibrosis". FEBS...
protein antibiotic. The structural studies on the lactoperoxidase system, that is, lactoperoxidase along with its inorganic ion substrates, hydrogen peroxide...
submucosal glands of the respiratory tract secrete myeloperoxidase and lactoperoxidase (LPO) that catalyzes the oxidation of thiocyanate and detoxify hydrogen...
the epithelial surface; and enzymatic components such as lysozyme, lactoperoxidase and antileukoprotease. Disruption to any of these local and systemic...
biologically active. The composition is approximately 54% lactoferrin and 41% lactoperoxidase, with other active proteins, such as Cyastin C and high mobility group-like...
immunoglobin (IgA), lysozyme, lactoferrin, histidine-rich polypeptide and lactoperoxidase to suppress C. tropicalis’ overgrowth, C. tropicalis is reported to...
been shown to be subject to high antibacterial activity from Bovine lactoperoxidase. Janda, J. Michael; Sharon L. Abbott (2006). The Enterobacteria (2nd ed...
similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in...
colostrum and cat milk, could also bear this coverage: lactoferrin, lactoperoxidase, lysozyme, rich proline polypeptide — PRP and alpha-lactalbumine. Lactoferrin...
PMID 18511861. — Review Conner GE, Salathe M, Forteza R (December 2002). "Lactoperoxidase and hydrogen peroxide metabolism in the airway". American Journal of...
Global Information
