AMD1, also known as adenosylmethionine decarboxylase proenzyme, 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.
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