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Cellular and Molecular Life Sciences CMLS

, Volume 60, Issue 5, pp 1013–1018 | Cite as

S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

  • M. R. Fernández
  • J. A. Biosca
  • X. Parés
Research Article

Abstract:

S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM–1 min–1, respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 μM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.

Key words: Formaldehyde dehydrogenase; alcohol dehydrogenase; nitrosoglutathione; ADH3; nuclear enzyme; nitrosative stress. 

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Copyright information

© Birkhäuser Verlag, 2003

Authors and Affiliations

  • M. R. Fernández
    • 1
  • J. A. Biosca
    • 1
  • X. Parés
    • 1
  1. 1.Department of Biochemistry and Molecular Biology, Faculty of Sciences, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona (Spain), Fax: +34 93 581 1264, e-mail: xavier.pares@uab.es ES

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