Banasik M, Ueda K
Department of Clinical Science and Laboratory Medicine, Kyoto University Faculty of Medicine, Japan.
Mol Cell Biochem. 1994 Sep;138(1-2):185-97. doi: 10.1007/BF00928461.
ADP-ribosylation reaction, that is the transfer of the ADP-ribose moiety of NAD+ to acceptor protein, is catalyzed by two classes of ADP-ribosyltransferases, i.e., poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferases. These two types differ not only in the number of transferring ADP-ribose units but also in the acceptor amino acid(s) and protein. Their inhibitors, particularly those of poly(ADP-ribose) synthetase, have been successfully employed in studies on biological functions of the enzymes and other related fields of research. Recently, we found many potent and specific inhibitors of poly(ADP-ribose) synthetase, and broadened their chemical as well as biochemical variety. More recently, we found several potent inhibitors of arginine-specific mono(ADP-ribosyl)transferases and activators of poly(ADP-ribose) synthetase.
ADP-核糖基化反应，即NAD⁺的ADP-核糖部分转移至受体蛋白，由两类ADP-核糖基转移酶催化，即聚（ADP-核糖）合成酶和单（ADP-核糖）转移酶。这两种类型不仅在转移的ADP-核糖单元数量上不同，而且在受体氨基酸和蛋白质方面也存在差异。它们的抑制剂，尤其是聚（ADP-核糖）合成酶的抑制剂，已成功应用于酶的生物学功能研究及其他相关研究领域。最近，我们发现了许多聚（ADP-核糖）合成酶的强效和特异性抑制剂，并拓宽了它们的化学及生化种类。最近，我们还发现了几种精氨酸特异性单（ADP-核糖）转移酶的强效抑制剂和聚（ADP-核糖）合成酶的激活剂。
