AMD1 polyclonal antibody detects endogenous levels of AMD1 protein.
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 ? and ?. Active AdoMetDC forms a heterotetramer of two ? chains and two ? chains. Both AdoMetDC proenzyme processing and mature AdoMetDC catalytic activity are stimulated by putrescine, while catalytic activity is inhibited by iodoacetic acid.
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