Int J Biochem Mol Biol 2013;4(3):108-128

Review Article
Lactoperoxidase: structural insights into the function, ligand binding and inhibition

Sujata Sharma, Amit Kumar Singh, Sanket Kaushik, Mau Sinha, Rashmi Prabha Singh, Pradeep Sharma, Harshverdhan Sirohi, Punit Kaur, Tej
P Singh

Department of Biophysics, All India Institute of Medical Sciences, New Delhi - 110029, India

Received July 22, 2013; Accepted August 21, 2013; Epub September 13, 2013; Published September 15, 2013

Abstract: Lactoperoxidase (LPO) is a member of a large group of mammalian heme peroxidases that include myeloperoxidase (MPO),
eosino-phil 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. (IJBMB1307006).

Keywords: Lactoperoxidase, lactoperoxidase system, mammalian heme peroxidases, antimicrobial, structure

Address correspondence to: Tej P Singh, Department of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi - 110029,
India. Tel: +91-11-2658-8931; Fax: +91-11-2658-8663; E-mail: tpsingh.aiims@gmail.com
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