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

被引：41

作者：

Fernández, MR ^{[1
]}

Biosca, JA ^{[1
]}

Parés, X ^{[1
]}

机构：

[1] Univ Autonoma Barcelona, Fac Sci, Dept Biochem & Mol Biol, E-08193 Barcelona, Spain

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2003年 / 60卷 / 05期

关键词：

formaldehyde dehydrogenase; alcohol dehydrogenase; nitrosoglutathione; ADH3; nuclear enzyme; nitrosative stress;

D O I：

10.1007/s00018-003-3025-x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1013 / 1018

页数：6

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