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) plays a crucial regulatory part in the polyamine biosynthetic pathway by producing the n-propylamine residue necessary for the synthesis of spermidine and spermine from putrescein. Unlike many amino acid decarboxylases, AdoMetDC employs a covalently attached pyruvate residue as a cofactor instead of the more typical pyridoxal 5'-phosphate.