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

Luca De Gioia, Elena M. Ghibaudi, Enzo Laurenti, Mario Salmona, Rosa Pia Ferrari

Research output: Contribution to journalArticle

36 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)476-485
Number of pages10
JournalJournal of Biological Inorganic Chemistry
Volume1
Issue number5
Publication statusPublished - Oct 1996

Fingerprint

Eosinophil Peroxidase
Lactoperoxidase
Scaffolds
X-Rays
X rays
Peroxidase
Apoproteins
Heme
Esters
Theoretical Models
Oxidation
Enzymes

Keywords

  • Eosinophil peroxidase Myeloperoxidase
  • Lactoperoxidase
  • Molecular modelling
  • Protein structure

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeioperoxidase X-ray structure. / De Gioia, Luca; Ghibaudi, Elena M.; Laurenti, Enzo; Salmona, Mario; Ferrari, Rosa Pia.

In: Journal of Biological Inorganic Chemistry, Vol. 1, No. 5, 10.1996, p. 476-485.

Research output: Contribution to journalArticle

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