Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties

Biochim Biophys Acta. 2000 Mar 7;1477(1-2):284-98. doi: 10.1016/s0167-4838(99)00280-0.


Among the different aspects of recent progress in the field of metallocarboxypeptidases has been the elucidation of the three dimensional structures of the pro-segments (in monomeric or oligomeric species) and their role in the expression, folding and inhibition/activation of the pancreatic and pancreatic-like forms. Also of great significance has been the cloning and characterization of several new regulatory carboxypeptidases, enzymes that are related with important functions in protein and peptide processing and that show significant structural differences among them and also with the digestive ones. Many regulatory carboxypeptidases lack a pro-region, unlike the digestive forms or others in between from the evolutionary point of view. Finally, important advances have been made on the finding and characterization of new protein inhibitors of metallocarboxypeptidases, some of them with interesting potential applications in the biotechnological/biomedical fields. These advances are analyzed here and compared with the earlier observations in this field, which was first explored by Hans Neurath and collaborators.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens
  • Binding Sites
  • Carboxypeptidases / antagonists & inhibitors*
  • Carboxypeptidases / chemistry
  • Carboxypeptidases A
  • Catalysis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / metabolism
  • Enzyme Precursors / chemistry
  • Glycoproteins / chemistry
  • Lysine Carboxypeptidase / antagonists & inhibitors
  • Models, Molecular
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Protease Inhibitors
  • Protein Conformation
  • Zinc / chemistry*


  • Antigens
  • Enzyme Inhibitors
  • Enzyme Precursors
  • Glycoproteins
  • Lxn protein, rat
  • Plant Proteins
  • Protease Inhibitors
  • Carboxypeptidases
  • Carboxypeptidases A
  • Lysine Carboxypeptidase
  • Zinc