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.
Keywords: Key words: Formaldehyde dehydrogenase; alcohol dehydrogenase; nitrosoglutathione; ADH3; nuclear enzyme; nitrosative stress.
Footnotes
Received 20 January 2003; received after revision 7 March 2003; accepted 21 March 2003
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ID="*"Corresponding author.