Lactoperoxidase

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<StructureSection load='3eri' size='350' side='right' caption='Human α-defensin 1 (PDB entry 2pm4)' scene=>

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. LPO is used as an antimicrobial agent in milk and its products, in cosmetics, toothpaste and ophthalmic solutions.

3D structures of lactoperoxidase

Updated on 10-April-2016

  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

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman