Lactoperoxidase

From Proteopedia

spinqualitylabelsall models Glycosylated bovine lactoferrin containing heme complex with thiocyanate, I- (purple) and Ca+2 (green) ions (PDB entry 3eri) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Lactoperoxidase (LPO) catalyzes the oxidation of thiocyanate, bromide and iodide using hydrogen peroxide. LPO is the second most abundant enzyme in milk. Heme is the cofactor of LPO. LPO contains a strongly-chelated calcium ion[1]. Relevance The short-lived oxidized intermediates of the LPO reaction serve as potent bactericidal agents[2]. LPO is used as an antimicrobial agent in milk and its products, in cosmetics, toothpaste and ophthalmic solutions. Structural highlights The [3]. Water molecules shown as red spheres. .

3D structures of lactoperoxidase

Updated on 26-March-2024

References

1. ↑ Gerson C, Sabater J, Scuri M, Torbati A, Coffey R, Abraham JW, Lauredo I, Forteza R, Wanner A, Salathe M, Abraham WM, Conner GE. The lactoperoxidase system functions in bacterial clearance of airways. Am J Respir Cell Mol Biol. 2000 Jun;22(6):665-71. PMID:10837362
2. ↑ Gerson C, Sabater J, Scuri M, Torbati A, Coffey R, Abraham JW, Lauredo I, Forteza R, Wanner A, Salathe M, Abraham WM, Conner GE. The lactoperoxidase system functions in bacterial clearance of airways. Am J Respir Cell Mol Biol. 2000 Jun;22(6):665-71. PMID:10837362
3. ↑ Sheikh IA, Singh AK, Singh N, Sinha M, Singh SB, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP. Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution. J Biol Chem. 2009 May 29;284(22):14849-56. Epub 2009 Apr 1. PMID:19339248 doi:10.1074/jbc.M807644200