通过转移核Overhauser效应确定的与脱氢酶结合的烟酰胺辅酶的构象。

Conformations of nicotinamide coenzymes bound to dehydrogenases determined by transferred nuclear Overhauser effects.

作者信息

Levy H R, Ejchart A, Levy G C

出版信息

Biochemistry. 1983 Jun 7;22(12):2792-6. doi: 10.1021/bi00281a004.

Abstract

Transferred nuclear Overhauser enhancement was used to examine the conformation of NAD+ and NADP+ bound to glucose-6-phosphate dehydrogenase and glutamate dehydrogenase and of NAD+ bound to lactate dehydrogenase. The results demonstrate that the conformation of the nicotinamide-ribose bond is anti for dehydrogenases with A stereospecificity and syn for dehydrogenases with B stereospecificity. In those dehydrogenases that bind both NAD+ and NADP+, significant differences occur in the conformations of the bound nicotinamide coenzymes.

摘要

转移核Overhauser效应被用于检测与葡萄糖-6-磷酸脱氢酶和谷氨酸脱氢酶结合的NAD⁺和NADP⁺以及与乳酸脱氢酶结合的NAD⁺的构象。结果表明，对于具有A立体特异性的脱氢酶，烟酰胺-核糖键的构象为反式，而对于具有B立体特异性的脱氢酶，该键的构象为顺式。在那些同时结合NAD⁺和NADP⁺的脱氢酶中，结合的烟酰胺辅酶的构象存在显著差异。