Peroxidases of trypanosomatids

• Type: Another Publication in an International Scientific Journal
• Date: 2008

Authors

castro, h (Author) Other; tomas, am (Author) ICBAS

Journal

Title: ANTIOXIDANTS & REDOX SIGNALING

Vol. 10

Pages: 1593-1606

ISSN: 1523-0864

Publisher: Mary Ann Liebert

Indexing

ISI Web of Knowledge - 42 Citations

Scopus - 40 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-003-WBE

DOI: 10.1089/ars.2008.2050

Abstract (EN): This article provides an overview about the recent advances in the dissection of the peroxide metabolism of Trypanosomatidae. This family of protozoan organisms comprises the medically relevant parasites Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp. Over the past 10 years, three major families of peroxidases have been identified in these organisms: (a) 2-cysteine peroxiredoxins, (b) nonselenium glutathione peroxidases, and (c) ascorbate peroxidases. In trypanosomatids, these enzymes display the unique feature of using reducing equivalents derived from trypanothione, a dithiol found exclusively in these protozoa. The electron transfer between trypanothione and the peroxidases is mediated by a redox shuttle, which can either be tryparedoxin, ascorbate, or even glutathione. The preference for the intermediate molecule differs among each peroxidase and so does the specificity for the peroxide substrate. These observations, added to the fact that these peroxidases are distributed throughout different subcellular compartments, point to the existence of an elaborate peroxide metabolism in trypanosomatids. With the completion of the trypanosomatids genome, other molecules displaying peroxidase activity might be added to this list in the future.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 14