Recombinant Human Adenosylmethionine Decarboxylase 1, His-tagged

AMD1 is synthesized initially as an inactive proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.

• Supplier: Creative Biomart
• Product #: AMD1-2483H