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EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.5.1.22Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.22analysis of X-ray crystal structure of the wild-type human SMS in complex with spermidine and 5-methylthioadenosine, PDB ID 3C6K, and folding free energy calculations, dimer structure analysis of wild-type and mutant enzymes, overview 723531
Show all pathways known for 2.5.1.22Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.22in complex with 5'-methylthioadenosine and spermidine and with 5'-methylthioadenosine and spermine. Enzyme is a dimer of two identical subunits. Each monomer has three domains, a C-terminal domain, which contains the active site and is similar in structure to spermidine synthase, a central domain made up of four beta-strands, and an N-terminal domain with remarkable structural similarity to S-adenosylmethionine decarboxylase 687717
Show all pathways known for 2.5.1.22Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.22Purified SpmSyn is crystallized as ternary complex in the presence of spermidine and 5'-methylthioadenosine or spermidine and 5'-methylthioadenosine using the hanging drop vapor diffusion method. The SpmSyn-5'-methylthioadenosine-spermidine complex is crystallized in 12% polyethylene glycol and 0.1 M MES (pH 6.5). The SpmSyn-5'-methylthioadenosine-spermine complex is crystallized in 18% polyethylene glycol, 0.1 M NaCl, and 0.1 M BisTris (pH 6.5). Crystals are soaked in the corresponding mother liquor supplemented with 20% glycerol as cryoprotectant before freezing in liquid nitrogen. 692270
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