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Regulation of Glutathione Peroxidases

  • Chapter
Oxidative Stress and Signal Transduction

Abstract

The glutathione peroxidases (GPx) belong to a superfamily of phylogenetically related proteins of diverse functions.1 The members of the superfamily containing a selenocysteine residue in their catalytic centers are highly efficient peroxidases reacting with a variety of hydroperoxides at rate constants of greater than 106 M-1 s-1.1 A cysteine residue in homologous position is catalytically less effective by about three orders of magnitude.2,3 Such GPx-like proteins, although still potential redox catalysts, can not be rated as peroxidases, if this term is to designate enzymes that must remove peroxides rapidly from a biological environment.

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Authors
  1. Leopold Flohé
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  2. Edgar Wingender
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  3. Regina Brigelius-Flohé
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  1. University of Southern California, USA

    Henry Jay Forman  & Enrique Cadenas  & 

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Flohé, L., Wingender, E., Brigelius-Flohé, R. (1997). Regulation of Glutathione Peroxidases. In: Forman, H.J., Cadenas, E. (eds) Oxidative Stress and Signal Transduction. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5981-8_17

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  • DOI: https://doi.org/10.1007/978-1-4615-5981-8_17

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