Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides.

@article{Malmberg1994ArginineDO,
  title={Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides.},
  author={Russell L. Malmberg and M L Cellino},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 4},
  pages={
          2703-6
        }
}
Oat arginine decarboxylase is synthesized as a 66-kDa proenzyme, but the soluble enzyme is found in oats as a complex of 42- and 24-kDa polypeptide fragments, both derived from the 66-kDa precursor. We report here that this proteolytic cleavage is the result of a processing enzyme, distinct from arginine decarboxylase itself, that leads to activation of the arginine decarboxylase. The proteolysis is resistant to a standard set of protease inhibitors, but is inhibited by high concentrations of… CONTINUE READING

Figures, Tables, and Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 24 CITATIONS

References

Publications referenced by this paper.

Plant Physwl

  • N. Young, A Galston
  • Plant Physwl
  • 1984

Similar Papers

Loading similar papers…