Agmatinase (also known as agmatine ureohydrolase) results from the decarboxylation of L-arginine by arginine decarboxylase to form a metabolic intermediate in the biosynthesis of putresine and higher polyamines (spermidine and spermine). Agmatinase has been shown to play a role in several important biochemical processes in humans, ranging from effects on the central nervous system to cell proliferation in cancer and viral replication. Agmatinase catalyzes the hydrolysis of agmatine to putresine and urea and is a major target for drug therapy. Human Agmatinase retains about 30% identity to bacterial agmatinases and less than 20% identity to mammalian arginases. Residues required for binding of Mn2+ at the active site in bacterial Agmatinase and other members of the arginase superfamily are fully conserved in human Agmatinase.