Tryptic treatment of human and porcine proproteinase E, procarboxypeptidase A binary complexes gave rise to active proteinase E after removal of an 11-residue N-terminal activation peptide. By contrast, upon treatment of either complex with active proteinase E, not only was the activation peptide released but also the hydrophobic dipeptide Val12-Val13 of the corresponding enzyme. No serine protease activity on specific synthetic peptide substrates could be detected. The structural homology of inactive proteinase E with subunit III of ruminant procarboxypeptidase A was strengthened by the existence of a functional homology since truncated proteinase E still possessed a weakly functional active site. Thus, subunit III-like proteins are generated by proteinase E-catalyzed limited proteolysis of proproteinase E. © 1989.
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 29 Sep 1989|
Avilés, F. X., Pascual, R., Salva, M., Bonicel, J., & Puigserver, A. (1989). Generation of a subunit III-like protein by autolysis of human and porcine proproteinase E in a binary complex with procarboxypeptidase A. Biochemical and Biophysical Research Communications, 163(3), 1191-1196. https://doi.org/10.1016/0006-291X(89)91104-2