AMD1 polyclonal antibody

AdoMetDC (adenosylmethionine decarboxylase 1), also known as S-adenosylmethionine decarboxylase proenzyme (SAMDC) or AMD1, is a 334 amino acid protein which is an important intermediate enzyme in polyamine biosynthesis pathways. Using a pyruvoyl group as a cofactor, AdoMetDC catalyzes the conversion of S-adenosyl-L-methionine to (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt and carbon dioxide. AdoMetDC is synthesized as an inactive proenzyme that undergoes self-maturation to form two non-identical subunits designated α and β. Active AdoMetDC forms a heterotetramer of two α chains and two β chains. Both AdoMetDC proenzyme processing and mature AdoMetDC catalytic activity are stimulated by putrescine, while catalytic activity is inhibited by iodoacetic acid.