Generation of a subunit III-like protein by autolysis of human and porcine proproteinase e in a binary complex with procarboxypeptidase A.

Abstract

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.

• Authors: F X Avilés, R Pascual, M Salva, J Bonicel, A Puigserver
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 163 Issue 3 Pg. 1191-6 (Sep 29 1989) ISSN: 0006-291X [Print] United States
• PMID: 2675835 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Enzyme Precursors
• Macromolecular Substances
• Carboxypeptidases
• Endopeptidases
• pro-proteinase E
• Carboxypeptidases A

Topics

• Amino Acid Sequence
• Animals
• Carboxypeptidases (isolation & purification, metabolism)
• Carboxypeptidases A
• Endopeptidases (isolation & purification, metabolism)
• Enzyme Precursors (isolation & purification, metabolism)
• Humans
• Kinetics
• Macromolecular Substances
• Molecular Sequence Data
• Molecular Weight
• Pancreas (enzymology)
• Sequence Homology, Nucleic Acid
• Swine