AdoMetDC Antikörper (H-9): sc-390073

Polyamines are compounds that have two or more primary amino groups and are important to cellular processes, such as cellular growth, proliferation and tumor promotion. 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.