Lactoperoxidase: Difference between revisions

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<StructureSection load='3eri' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
<StructureSection load='3eri' size='350' side='right' caption='Glycosylated bovine lactoferrin containing heme complex with thiocyanate, I- (purple) and Ca+2 (green) ions  (PDB entry [[3eri]])' scene=''>
== Function ==
== 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<ref>PMID:10837362</ref>.
'''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<ref>PMID:10837362</ref>.

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