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Primary Information | |
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| BoMiProt ID | Bomi131 |
| Protein Name | Lactoperoxidase |
| Organism | Bos taurus |
| Uniprot ID | P80025 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_776358.1 |
| Aminoacid Length | 712 |
| Molecular Weight | 80642 |
| FASTA Sequence | Download |
| Gene Name | LPO |
| Gene ID | 280844 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | saliva, airway mucus, tears |
| Protein Function | Promotes host defence against microbes in milk saliva and airways; controlled catalysis of oxidation of certain molecules; |
| Biochemical Properties | calcium and iron containing peroxidase; hydrogen peroxide and thiocyanate ions were essential for the bactericidal activity of this enzyme; enxymatic activity increases with decreasing pH; human protein is moderately cationic with a pI of ~7.5, whereas the bovine protein is more cationic with a pI of ~9.6; hydrophobicity, cationicity, and helical propensity determie the antimicrobial properties; differences in glycosylation and a partial deamidation can cause noticeable chromatographic and electrophoretic heterogeneity; stability and structural inegrity are maintained by calcium ions; binding of prosthetic heme group to protein occurs through a self processing mechanism with the help of H2O2 and once the cross-linking is complete, the enzyme attains a fully efficient catalytic form |
| Significance in milk | Biocidal activity, efficient antibiotics and antiviral agents against a wide spectrum of bacteria, fungi, and viruses; activated lactoperoxidase by peroxide can preserve raw milk during transportation, reduces refrigeration and pasteurization requirement; |
| PTMs | glycoprotein; four to five N-glycosylation sites and are characterizedby a carbohydrate content of about 10 %; |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P80025|PERL_BOVIN Lactoperoxidase OS=Bos taurus OX=9913 GN=LPO PE=1 SV=1
MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFL DSRTRLKTTLSSEAPTTQQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRR DTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRS PALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIV GYLDEEGVLDQN*212RSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYC IQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAV TSFLDASLVYGSEPS*315LASRLRN*322LSSPLGLMAVNQEAWDHGLAYLPFNNKK PSPCEFIN*358TTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKL NPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYN*449N SVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNT WRIIKDGGIDPLVRGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDL AAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDL YKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENP GVFTEKQRDSLQKVSFSRLICDNTHITKVPLHAFQANNYPHDFVDCSTVD KLDLSPWASREN |
| CATH | Matched CATH superfamily 1.10.640.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| PDB ID | 2ips, 2nqx, 2pt3, 2pum, 2qpk, 2qqt, 2qrb, 3bxi, 3eri, 3gc1, 3gcj, 3gck, 3gcl, 3i6n, 3krq, 3nyh, 3ogw, 3py4, 3q9k, 3ql6, 3r4x, 3r5o, 3s4f, 3tgy, 3uba, 3v6q, 4gm7, 4gn6, 4ksz, 4njb, 4nt3, 4pnx, 5b72, 5gh0, 5gls, 5wv3, 5zgs, 5zww, 6a4y, |
| Bibliography | 1. Salathe, M., Holderby, M., Forteza, R., Abraham, W. M., Wanner, A., and Conner, G. E. (1997) Isolation and Characterization of a Peroxidase from the Airway. Am. J. Respir. Cell Mol. Biol. 17, 97–105. 2. Wijkstrom-Frei, C., El-Chemaly, S., Ali-Rachedi, R., Gerson, C., Cobas, M. A., Forteza, R., Salathe, M., and Conner, G. E. (2003) Lactoperoxidase and Human Airway Host Defense. Am. J. Respir. Cell Mol. Biol. 29, 206–212. 3. Singh, P. K., Iqbal, N., Sirohi, H. V., Bairagya, H. R., Kaur, P., Sharma, S., and Singh, T. P. (2018) Structural basis of activation of mammalian heme peroxidases. Prog. Biophys. Mol. Biol. 133, 49–55. 4. Reiter, B., Marshall, V. M., BjörckL, and Rosén, C. G. (1976) Nonspecific bactericidal activity of the lactoperoxidases-thiocyanate-hydrogen peroxide system of milk against Escherichia coli and some gram-negative pathogens. Infect. Immun. 13, 800–807. 5. Reiter, B., Marshall, V. M., and Philips, S. M. (1980) The antibiotic activity of the lactoperoxidase-thiocyanate-hydrogen peroxide system in the calf abomasum. Res. Vet. Sci. 28, 116–122. 6. Klebanoff, S. J. and Luebke, R. G. (1965) The Antilactobacillus System of Saliva. Role of Salivary Peroxidase. Exp. Biol. Med. 118, 483–486. 7. Kussendrager, K. D. and van Hooijdonk, A. C. (2000) Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 84 Suppl 1, S19-25. 8. Kamau, D. N., Doores, S., and Pruitt, K. M. (1990) Enhanced thermal destruction of Listeria monocytogenes and Staphylococcus aureus by the lactoperoxidase system. Appl. Environ. Microbiol. 56, 2711–2716. 9. Arqués, J. L., Rodríguez, E., Nuñez, M., and Medina, M. (2008) Antimicrobial Activity of Nisin, Reuterin, and the Lactoperoxidase System on Listeria monocytogenes and Staphylococcus aureus in Cuajada, a Semisolid Dairy Product Manufactured in Spain. J. Dairy Sci. 91, 70–75. 10. Furtmüller, P. G., Jantschko, W., Regelsberger, G., Jakopitsch, C., Arnhold, J., and Obinger, C. (2002) Reaction of lactoperoxidase compound I with halides and thiocyanate. Biochemistry 41, 11895–11900. 11. Redwan, E. M., EL-Fakharany, E. M., Uversky, V. N., and Linjawi, M. H. (2014) Screening the anti infectivity potentials of native N- and C-lobes derived from the camel lactoferrin against hepatitis C virus. BMC Complement. Altern. Med. 14, 219. 12. Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., and Obinger, C. (2006) Active site structure and catalytic mechanisms of human peroxidases. Arch. Biochem. Biophys. 445, 199–213 |