Co-catalytic metallopeptidases as pharmaceutical targets.
Curr Opin Chem Biol
; 7(2): 197-206, 2003 Apr.
Article
en En
| MEDLINE
| ID: mdl-12714052
ABSTRACT
Understanding the reaction mechanism of co-catalytic metallopeptidases provides a starting point for the design and synthesis of new molecules that can be screened as potential pharmaceuticals. Many of the enzymes that contain co-catalytic metallo-active sites play important roles in cellular processes such as tissue repair, protein maturation, hormone level regulation, cell-cycle control and protein degradation. Therefore, these enzymes play central roles in several disease states including cancer, HIV, stroke, diabetes, bacterial infections, neurological processes, schizophrenia, seizure disorders, and amyotrophic lateral sclerosis. The mechanism of AAP, an aminopeptidase from Aeromonas proteolytica, is one of the best-characterized examples of a metallopeptidase containing a co-catalytic metallo-active site, although this enzyme is not a specific pharmaceutical target at this time. As a large majority of co-catalytic metallopeptidases contain active sites that are nearly identical to the one observed in AAP, the major steps of their catalytic mechanisms are likely to be very similar. With this in mind, it is possible to propose a general catalytic mechanism for the hydrolysis of amino acid substrates.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Metaloendopeptidasas
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Curr Opin Chem Biol
Asunto de la revista:
BIOQUIMICA
Año:
2003
Tipo del documento:
Article
País de afiliación:
Estados Unidos