Synthesis and biochemical properties of chemically stable product analogues of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase.
Synthesis and biochemical properties of chemically stable product analogues of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase.
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S-腺苷-L-甲硫氨酸脱羧酶催化反应的化学稳定产物类似物的合成和生化性质。
DOI：
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发表时间：
1982
影响因子：
7.3
通讯作者：
N. Claverie
中科院分区：
文献类型：
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作者：
M. Kolb;C. Danzin;J. Barth;N. Claverie
本文合成了由s -腺苷- l-蛋氨酸脱羧酶（SAM-DC）催化的脱羧s -腺苷- l-蛋氨酸（dc-SAM）的结构类似物，并对其侧链部分进行了修饰，并研究了它们对SAM-DC的抑制能力。主要研究了以氮原子代替硫原子的化合物。来自这些抑制研究的数据已经导致了SAM-DC结合所需的结构特征的描述。结果表明，SAM-DC不需要一个末端的伯氨基、一个末端的羧基和磺胺官能团。还发现，以氮取代硫为唯一修饰的dc-SAM类似物仍然能够与酶形成亚甲基。在SAM和dc-SAM中发现，这些化合物也引起SAM- dc的时间依赖性失活。
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.