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The bovine pro-carboxypeptidase A-S6 ternary complex: a rare case of a secreted protein complex.

Authors
  • Chapus, C
  • Puigserver, A
  • Kerfélec, B
Type
Published Article
Journal
Biochimie
Publisher
Elsevier
Publication Date
Sep 01, 1988
Volume
70
Issue
9
Pages
1143–1151
Identifiers
PMID: 3147706
Source
Medline
License
Unknown

Abstract

Up to now, a non-covalent ternary complex in which the pro-carboxypeptidase A (subunit I) is associated to two functionally different proteins (subunits II and III) has only been found in the pancreas of ruminant species. In the other species studied so far, the pro-carboxypeptidase A is secreted either as a monomer or as a binary association with a functionally different protein. Subunit I is the immediate precursor of carboxypeptidase A. Subunit II is a chymotrypsinogen of the C-type, involved, like subunit I, in the degradation of proteins and peptides. Although closely related to the pancreatic serine endopeptidases, subunit III appears to be devoid of any specific enzymatic activity. Information about the spatial organization of the subunits in the ternary complex has been deduced from the sequential dissociation of the complex. In contrast to the mechanism of activation of subunits I and II, which is independent of their aggregation state, the catalytic properties of the resulting enzymes are sensitive to their aggregation state. Moreover, the structural basis of inactivity of subunit III as well as the physiological role of the ternary complex are also discussed in this review.

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