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- W83847820 abstract "Lactoperoxidase (LPO) is a member of a large group of mammalian heme peroxidases that include myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). The LPO is found in exocrine secretions including milk. It is responsible for the inactivation of a wide range of micro-organisms and hence, is an important component of defense mechanism in the body. With the help of hydrogen peroxide, it catalyzes the oxidation of halides, pseudohalides and organic aromatic molecules. Historically, LPO was isolated in 1943, nearly seventy years ago but its three-dimensional crystal structure has been elucidated only recently. This review provides various details of this protein from its discovery to understanding its structure, function and applications. In order to highlight species dependent variations in the structure and function of LPO, a detailed comparison of sequence, structure and function of LPO from various species have been made. The structural basis of ligand binding and distinctions in the modes of binding of substrates and inhibitors have been analyzed extensively." @default.
- W83847820 created "2016-06-24" @default.
- W83847820 creator A5003774336 @default.
- W83847820 creator A5004136768 @default.
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- W83847820 creator A5061345100 @default.
- W83847820 creator A5066372965 @default.
- W83847820 creator A5071077771 @default.
- W83847820 creator A5083794797 @default.
- W83847820 date "2013-09-13" @default.
- W83847820 modified "2023-09-23" @default.
- W83847820 title "Lactoperoxidase: structural insights into the function,ligand binding and inhibition." @default.
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