Mammalian agmatinases constitute unusual members in the family of Mn2 +-dependent ureahydrolases

Agmatinases (AGM) hydrolyze of agmatine to putrescine and urea, and belong to Mn2 +-dependent ureahydrolases. In human-AGM the six amino acid ligands that coordinate Mn2 + ions are conserved, four mutations are observed in the murine enzyme. We demonstrate that similar to its human counterpart murine-AGM has in vivo agmatinase activity.