S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation
S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation
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DOI：
10.1007/s00018-003-3025-x
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发表时间：
2003-05-01
影响因子：
8
通讯作者：
Parés, X
中科院分区：
文献类型：
--
作者：
Fernández, MR;Biosca, JA;Parés, X
S-亚硝基谷胱甘肽（GSNO）的形成代表了一种储存和运输一氧化氮的机制。对人类肝脏和酿酒酵母提取物的分析揭示了仅存在一种能够显著减少GSNO的酶，其被鉴定为谷胱甘肽依赖性甲醛脱氢酶（GSHDH）。GSNO是已知的人和酵母酶的最佳底物（kcat/Km分别= 444，400和350，000 mM（-1）min（-1））。虽然NADH是优选的辅因子，但可以预测体内与NADPH（Km = 460 μ M）的某些活性。亚细胞定位表明，在活的酵母细胞中的胞浆和核分布的EPODH。这与以前在大鼠中的结果一致，并且表明在真核细胞的胞质和核隔室中GSNO水平的调节中的作用。
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.