Human S-Adenosylmethionine Decarboxylase Proenzyme (AMD1) Protein

Background

Adenosylmethionine Decarboxylase 1 (AMD1) is a key regulatory enzyme in polyamine biosynthesis, catalyzing the decarboxylation of S-adenosylmethionine (SAM) to form S-adenosylmethioninamine (dcSAM). This reaction provides the aminopropyl group for the synthesis of polyamines such as spermidine and spermine, which are essential for cell proliferation, differentiation, and DNA stabilization. AMD1 activity is tightly regulated at multiple levels, including transcription, translation, and post-translational modifications, to meet cellular demands for polyamine production. Dysregulation of AMD1 has been linked to various pathological conditions, including cancer, where increased polyamine synthesis supports tumor growth and survival. Inhibiting AMD1 is being explored as a potential therapeutic strategy for cancer treatment, targeting the overactive polyamine biosynthesis pathway to suppress cell proliferation. AMD1 also plays a role in cellular responses to oxidative stress and metabolic regulation, making it an important enzyme in maintaining cellular homeostasis.