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JBIC Journal of Biological Inorganic Chemistry

, Volume 1, Issue 5, pp 476–485 | Cite as

A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeloperoxidase X-ray structure

  • De Gioia
  • Elena M. Ghibaudi
  • Enzo Laurenti
  • Mario Salmona
  • R. P. Ferrari
ORIGINAL ARTICLE

Abstract

 Lactoperoxidase (LPO), eosinophil peroxidase (EPO) and myeloperoxidase (MPO) belong to the class of haloperoxidases, a group of mammalian enzymes able to catalyze the peroxidative oxidation of halides and pseudohalides, such as thiocyanate. They all play a key role in the development of antibacterial activity. The homology in their functional role is emphasized by the striking similarity of their primary structures. A theoretical model for the three-dimensional structure of LPO and EPO has been developed on the basis of the X-ray structure of MPO, a high degree of similarity having been found in their sequences. Evidence supporting the hypothesis of an ester linkage between heme and apoprotein in LPO and EPO, originally proposed by Hultquist and Morrison is discussed.

Key words Lactoperoxidase Eosinophil peroxidase Myeloperoxidase Molecular modelling Protein structure 

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Copyright information

© Society of Biological Inorganic Chemistry 1996

Authors and Affiliations

  • De Gioia
    • 1
  • Elena M. Ghibaudi
    • 2
  • Enzo Laurenti
    • 2
  • Mario Salmona
    • 3
  • R. P. Ferrari
    • 2
  1. 1.Dipartimento di Chimica Inorganica e Metallorganica, Università di Milano, Via Venezian 21, I-20133 Milan, ItalyIT
  2. 2.Dipartimento di Chimica I.F.M., Università di Torino, Via P. Giuria 7, I-10125 Turin, ItalyIT
  3. 3.Istituto di Ricerche Farmacologiche "Mario Negri", Via Eritrea 62, I-20157 Milan, ItalyIT

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