S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate.
S-adenosylmethionine decarboxylase (AdoMetDC) is a vital controller in the polyamine production process by generating the n-propylamine component required for spermidine and spermine synthesis from putrescein. Unlike other amino acid decarboxylases, AdoMetDC utilizes a covalently linked pyruvate molecule as a cofactor rather than the more conventional pyridoxal 5'-phosphate.