Kolb M, Danzin C, Barth J, Claverie N
J Med Chem. 1982 May;25(5):550-6. doi: 10.1021/jm00347a014.
Structural analogues of decarboxylated S-adenosyl-L-methionine (dc-SAM), product of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase (SAM-DC), with modifications in the side-chain portion of the molecule have been synthesized, and their ability to inhibit SAM-DC has been investigated. Mainly, compounds with a nitrogen atom in place of the sulfur were investigated. The data from these inhibition studies have resulted in a delineation of the structural features required for binding on SAM-DC. It was concluded that a terminal primary amino group, a terminal carboxyl group, and the sulfonium functionality are not required for binding on SAM-DC. It was also found that analogues of dc-SAM in which replacement of the sulfur by nitrogen was the only modification were still able to form an azomethine with the enzyme. As found for SAM and dc-SAM, these compounds also caused a time-dependent inactivation of SAM-DC.
已合成了由S-腺苷-L-甲硫氨酸脱羧酶（SAM-DC）催化反应的产物——脱羧S-腺苷-L-甲硫氨酸（dc-SAM）的结构类似物，这些类似物在分子的侧链部分有所修饰，并对它们抑制SAM-DC的能力进行了研究。主要研究了用氮原子取代硫的化合物。这些抑制研究的数据已得出了SAM-DC结合所需的结构特征。得出的结论是，末端伯氨基、末端羧基和锍官能团并非SAM-DC结合所必需。还发现，其中用氮取代硫是唯一修饰的dc-SAM类似物仍能与该酶形成甲亚胺。正如对SAM和dc-SAM所发现的那样，这些化合物也导致了SAM-DC的时间依赖性失活。
