Lactoperoxidase
From Proteopedia
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| - | <StructureSection load='3eri' size='350' side='right' caption=' | + | <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>. | ||
Revision as of 09:13, 10 April 2016
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3D structures of lactoperoxidase
Updated on 10-April-2016
References
- ↑ 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
- ↑ 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
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