Synthesis and biochemical properties of chemically stable product analogues of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase.

摘要: Structural analogues of decarboxylated S-adenosyl-L-methionine (dc-SAM), product the reaction catalyzed by decarboxylase (SAM-DC), with modifications in side-chain portion molecule have been synthesized, and their ability to inhibit SAM-DC has investigated. Mainly, compounds a nitrogen atom place sulfur were The data from these inhibition studies resulted delineation structural features required for binding on SAM-DC. It was concluded that terminal primary amino group, carboxyl sulfonium functionality are not also found dc-SAM which replacement only modification still able form an azomethine enzyme. As SAM dc-SAM, caused time-dependent inactivation