Agmatine deiminase from maize shoots: purification and properties.

Agmatine deiminase was purified to a specific activity of 537 nkat/mg protein using an improved procedure. The recovery was 47% and the enzyme was homogeneous and remarkably stable. The molecular mass of the enzyme as determined by gel filtration was 75 kDa, and SDS-PAGE suggests that the enzyme is a heterodimer composed of subunits of 43.5 and 44 kDa. The Km for agmatine was 12 microM and arcaine was shown to be a potent competitive inhibitor of the enzyme, with a Ki of 3.3 microM. The enzyme does not have either putrescine synthase activity or the activities of its components ornithine and putrescine transcarbamylase. These results distinctly demonstrate that agmatine deiminase is different from putrescine synthase.