Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 60, Issue 5, Pages 1013-1018Publisher
BIRKHAUSER VERLAG AG
DOI: 10.1007/s00018-003-3025-x
Keywords
formaldehyde dehydrogenase; alcohol dehydrogenase; nitrosoglutathione; ADH3; nuclear enzyme; nitrosative stress
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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 muM) 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.
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