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Biochim Biophys Acta. 2000 Mar 7;1477(1-2):284-98.

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

Author information

1
Departament de Bioquímica i Biologia Molecular, Facultat de Ciències, and Institut de Biologia Fonamental. Universitat Autònoma de Barcelona, E-08193, Bellaterra, Spain.

Abstract

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.

PMID:
10708864
DOI:
10.1016/s0167-4838(99)00280-0
[Indexed for MEDLINE]

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