Sharma Sujata, Singh Amit Kumar, Kaushik Sanket, Sinha Mau, Singh Rashmi Prabha, Sharma Pradeep, Sirohi Harshverdhan, Kaur Punit, Singh Tej P
Department of Biophysics, All India Institute of Medical Sciences New Delhi - 110029, India.
Int J Biochem Mol Biol. 2013 Sep 13;4(3):108-28.
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.
乳过氧化物酶（LPO）是一大类哺乳动物血红素过氧化物酶中的一员，这类酶包括髓过氧化物酶（MPO）、嗜酸性粒细胞过氧化物酶（EPO）和甲状腺过氧化物酶（TPO）。LPO存在于包括乳汁在内的外分泌液中。它负责使多种微生物失活，因此是机体防御机制的重要组成部分。在过氧化氢的帮助下，它催化卤化物、拟卤化物和有机芳香分子的氧化。历史上，LPO于1943年被分离出来，距今近七十年，但直到最近才阐明其三维晶体结构。本综述提供了这种蛋白质从发现到理解其结构、功能和应用的各种细节。为了突出LPO在结构和功能上的物种依赖性差异，对来自不同物种的LPO的序列、结构和功能进行了详细比较。对配体结合的结构基础以及底物和抑制剂结合模式的差异进行了广泛分析。
