Autolysis of proproteinase E in bovine procarboxypeptidase A ternary complex gives rise to subunit III.

Abstract

Extracts of bovine pancreatic tissue are shown by HPLC to contain two distinct ternary complexes of procarboxypeptidase A (subunit I), chymotrypsinogen C (subunit II) and either proproteinase E or subunit III. It is shown that proproteinase E in the complex generates subunit III by removal of 13 N-terminal residues when the former is allowed to autolyze in solution or when catalytic amounts of isolated active proteinase E are added to it. Autolysis of proproteinase E was accompanied by the loss of potential activity towards specific synthetic substrates and occurred at a higher rate in pancreatic juice than in pancreatic tissue extracts, even when both were processed in the presence of serine protease inhibitors. We conclude that subunit III (also called truncated protease E) is an autolytic product of proproteinase E and not an ab initio component of the native ternary complex.

• Authors: R Pascual, J Vendrell, F X Avilés, J Bonicel, C Wicker, A Puigserver
• Journal: FEBS letters (FEBS Lett) Vol. 277 Issue 1-2 Pg. 37-41 (Dec 17 1990) ISSN: 0014-5793 [Print] England
• PMID: 2269366 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Enzyme Precursors
• Multienzyme Complexes
• Carboxypeptidases
• Endopeptidases
• pro-proteinase E
• Carboxypeptidases A

Topics

• Amino Acid Sequence
• Animals
• Carboxypeptidases (metabolism)
• Carboxypeptidases A
• Cattle
• Endopeptidases (metabolism)
• Enzyme Activation
• Enzyme Precursors (metabolism)
• Molecular Sequence Data
• Molecular Weight
• Multienzyme Complexes (metabolism)
• Pancreas (enzymology)
• Pancreatic Juice (enzymology)