| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152647 | Journal of Inorganic Biochemistry | 2017 | 4 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
