Nemchinskaia V L, Braun A D
Tsitologiia. 1978 Mar;20(3):251-63.
The nature of a before unknown biological activity of NAD as a substrate in protein modification reaction is considered. Upon enzymatic digestion of NAD its adenosinediphosphate ribose (ADPR) part is transferred to acceptor proteins. ADPR in its mono- or polymeric form is covalently linked to proteins at the expense of NAD's high energy bound. Negatively charged ADPR, in association with a protein, is able to alter the charge, conformation and biological activity of the latter. The reaction is important in structural rearrangements of chromatin, in the synthesis and repair of DNA, in cell growth and differentiation and in the mechanisms of actions of actions of bacterial toxins.
人们对烟酰胺腺嘌呤二核苷酸(NAD)作为蛋白质修饰反应底物的一种此前未知的生物活性的性质进行了研究。在NAD被酶解时,其二磷酸腺苷核糖(ADPR)部分会转移到受体蛋白上。单聚或多聚形式的ADPR以NAD的高能键为代价与蛋白质共价连接。带负电荷的ADPR与蛋白质结合后,能够改变蛋白质的电荷、构象和生物活性。该反应在染色质的结构重排、DNA的合成与修复、细胞生长与分化以及细菌毒素的作用机制中都很重要。