| 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. | The inhibition effects of some natural products on lactoperoxidase purified from bovine milk.
Köksal Z, Kalın R, Gerni S, Gülçin İ, Özdemir H. | 01/6/2018 |
| establish urate as a likely physiological substrate for LPO that will influence host defense and give rise to reactive electrophilic metabolites | Uric acid and thiocyanate as competing substrates of lactoperoxidase.
Seidel A, Parker H, Turner R, Dickerhof N, Khalilova IS, Wilbanks SM, Kettle AJ, Jameson GN., Free PMC Article | 02/21/2015 |
| 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. | Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH.
Singh AK, Smith ML, Yamini S, Ohlsson PI, Sinha M, Kaur P, Sharma S, Paul JA, Singh TP, Paul KG. | 03/23/2013 |
| LPO serve as a catalytic sink for HOCl (hypochlorous acid), while HOCl serves to modulate LPO catalytic activity, bioavailability, and function. | Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases.
Souza CE, Maitra D, Saed GM, Diamond MP, Moura AA, Pennathur S, Abu-Soud HM., Free PMC Article | 04/7/2012 |
| 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. | First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases.
Singh AK, Singh N, Tiwari A, Sinha M, Kushwaha GS, Kaur P, Srinivasan A, Sharma S, Singh TP. | 01/1/2011 |
| 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. | 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, Kumar RP, Pandey N, Singh N, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP., Free PMC Article | 02/1/2010 |
| 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. | 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.
Singh AK, Singh N, Sinha M, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP., Free PMC Article | 01/21/2010 |
| The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution. | Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution.
Sheikh IA, Singh AK, Singh N, Sinha M, Singh SB, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP., Free PMC Article | 01/21/2010 |
| 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 | Inhibition of lactoperoxidase by its own catalytic product: crystal structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3-A resolution.
Singh AK, Singh N, Sharma S, Shin K, Takase M, Kaur P, Srinivasan A, Singh TP., Free PMC Article | 01/21/2010 |
| 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. | The role of the sulfonium linkage in the stabilization of the ferrous form of myeloperoxidase: a comparison with lactoperoxidase.
Brogioni S, Stampler J, Furtmüller PG, Feis A, Obinger C, Smulevich G. | 01/21/2010 |
| at higher temperature, the protein hydrophobic core, rich in alpha-helices, unfolds with concomitant disruption of the catalytic heme pocket & activity loss. the stabilizing role of the disulfide bridges and the covalently bound heme cofactor are shown. | Lactoperoxidase folding and catalysis relies on the stabilization of the alpha-helix rich core domain: a thermal unfolding study.
Boscolo B, Leal SS, Ghibaudi EM, Gomes CM. | 01/21/2010 |