Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides.
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DOI：
10.1042/bst0170313
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发表时间：
1989-04
影响因子：
3.9
通讯作者：
H. Levy
中科院分区：
文献类型：
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作者：
H. Levy
在这次研讨会的背景下，有趣的是，葡萄糖6-磷酸脱氢酶（G6 PD）和NADP+都是首次在红细胞中发现的（1，2）。在随后的二十年中，G6 PD从各种动物、植物和微生物中分离出来（3）。这些酶都利用NADP+作为葡萄糖6-磷酸氧化的辅酶。随着其他NADP相关酶的发现，以及氧化型和还原型烟酰胺辅酶的代谢作用被认识到，很明显，尽管NAD和NADP在结构上非常相似，但它们在代谢中的功能完全不同。具体地，NADH的氧化通常与分解代谢、ATP生成过程（如线粒体电子传递）相关，而NADPH氧化伴随着线粒体的电子传递。
In the context of this symposium, it is of interest that both glucose 6-phosphate dehydrogenase (G6PD) and NADP+ were first discovered in erythrocytes (1, 2). During the subsequent two decades, G6PD was isolated from a variety of animals, plants and microorganisms (3). These enzymes all utilized NADP+ as the coenzyme for the oxidation of glucose 6-phosphate. As other NADP-linked enzymes were discovered and as the metabolic roles of the oxidized and reduced nicotinamide coenzymes were recognized, it became clear that despite their great structural similarity, NAD and NADP functioned quite differently in metabolism. In particular, the oxidation of NADH is generally associated with catabolic, ATP-generating processes, such as mitochondrial electron transport, whereas NADPH oxidation accompanies