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Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme

Toppo, Stefano, Flohé, Leopold, Ursini, Fulvio, Vanin, Stefano and Maiorino, Matilde (2009) Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme. Biochimica et Biophysica Acta (BBA) - General Subjects, 1790 (11). pp. 1486-1500. ISSN 03044165

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Abstract

Kinetics and molecular mechanisms of GPx-type enzymes are reviewed with emphasis on structural features relevant to efficiency and specificity. In Sec-GPxs the reaction takes place at a single redox centre with selenocysteine as redox-active residue (peroxidatic Sec, UP). In contrast, most of the non-vertebrate GPx have the UP replaced by a cysteine (peroxidatic Cys, CP) and work with a second redox centre that contains a resolving cysteine (CR). While the former type of enzymes is more or less specific for GSH, the latter are reduced by “redoxins”. The common denominator of the GPx family is the first redox centre comprising the (seleno)cysteine, tryptophan, asparagine and glutamine. In this architectural context the rate of hydroperoxide reduction by UP or CP, respectively, is enhanced by several orders of magnitude compared to that of free selenolate or thiolate. Mammalian GPx-1 dominates H2O2 metabolism, whereas the domain of GPx-4 is the reduction of lipid hydroperoxides with important consequences such as counteracting 12/15-lipoxygenase-induced apoptosis and regulation of inflammatory responses. Beyond, the degenerate GSH specificity of GPx-4 allows selenylation and oxidation to disulfides of protein thiols. Heterodimer formation of yeast GPx with a transcription factor is discussed as paradigm of a redox sensing that might also be valid in vertebrates.

Item Type: Article
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history > QH301 Biology
Schools: School of Applied Sciences
School of Applied Sciences > Forensic Biology Research Group
Depositing User: Sara Taylor
Date Deposited: 06 Oct 2011 14:08
Last Modified: 05 Jul 2013 15:45
URI: http://eprints.hud.ac.uk/id/eprint/11622

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