Lactoperoxidase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_2ips| PDB=2ips | SIZE=400| SCENE= |right|CAPTION=Heme containing glycosylated bovine lactoperoxidase complex with carbonate, thiocyanate, calcium (green) and iodide (purple) ions [[2ips]] }} | ||
| - | < | + | <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<ref>PMID:10837362</ref>. | |
| - | + | ||
| - | + | == Relevance == | |
| - | '''Lactoperoxidase''' (LPO) catalyzes the oxidation of thiocyanate, bromide and iodide using hydrogen peroxide. The short-lived oxidized intermediates of the reaction serve as potent bactericidal agents. LPO is used as an antimicrobial agent in milk and its products, in cosmetics, toothpaste and ophthalmic solutions | + | 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== | ==3D structures of lactoperoxidase== | ||
| Line 75: | Line 74: | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 08:59, 10 April 2016
| |||||||||||
Proteopedia Page Contributors and Editors (what is this?)
Joel L. Sussman, Michal Harel, Alexander Berchansky, Jaime Prilusky
