81162-84-7Relevant academic research and scientific papers
Synthesis and Biochemical Properties of Chemically Stable Product Analogues of the Reaction Catalyzed by S-Adenosyl-L-methionine Decarboxylase
Kolb, Michael,Danzin, Charles,Barth, Jacqueline,Claverie, Nicole
, p. 550 - 556 (2007/10/02)
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.
