Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase.
Structure
; 12(5): 775-84, 2004 May.
Article
em En
| MEDLINE
| ID: mdl-15130470
ABSTRACT
Sialidases are a superfamily of sialic-acid-releasing enzymes that are of significant interest due to their implication as virulence factors in the pathogenesis of a number of diseases. However, extensive studies of viral and microbial sialidases have failed to provide a comprehensive picture of their mechanistic properties, in part because the structures of competent enzyme-substrate complexes and reaction intermediates have never been described. Here we report these structures for the Trypanosoma cruzi trans-sialidase (TcTS), showing that catalysis by sialidases occurs via a similar mechanism to that of other retaining glycosidases, but with some intriguing differences that may have evolved in response to the substrate structure.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trypanosoma cruzi
/
Glicoproteínas
/
Neuraminidase
Limite:
Animals
Idioma:
En
Revista:
Structure
Ano de publicação:
2004
Tipo de documento:
Article