Conformations of nicotinamide coenzymes bound to dehydrogenases determined by transferred nuclear Overhauser effects.
Conformations of nicotinamide coenzymes bound to dehydrogenases determined by transferred nuclear Overhauser effects.
复制标题
与脱氢酶结合的烟酰胺辅酶的构象由转移核奥弗豪瑟效应确定。
DOI：
10.1021/bi00281a004
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发表时间：
1983
期刊：
影响因子：
2.9
通讯作者：
Levy,GC
中科院分区：
文献类型：
--
作者：
Levy,HR;Ejchart,A;Levy,GC
1982年）。对利用NAD的脱氢酶的X射线晶体学研究已经表明，在醇脱氢酶、苹果酸脱氢酶和乳酸脱氢酶中，所有这些都是A立体特异性的，结合的NAD+的烟酰胺-核糖键的构象是反式的，而在甘油-醛-3-磷酸脱氢酶（唯一检查的B立体特异性酶）中，这种构象是顺式的（Rossmann等人，
1982). X-ray crystallographic studies on NAD-utilizing de-hydrogenases have shown that in alcohol dehydrogenase, malate dehydrogenase, and lactate dehydrogenase, all of which are A stereospecific, the conformation of the nicotinamide-ribose bond of bound NAD+ is anti, whereas in glycer-aldehyde-3-phosphate dehydrogenase, the only B-stereospecific enzyme examined, this conformation is syn (Rossmann et al.,