| Literature DB >> 15130470 |
María Fernanda Amaya1, Andrew G Watts, Iben Damager, Annemarie Wehenkel, Tong Nguyen, Alejandro Buschiazzo, Gastón Paris, A Carlos Frasch, Stephen G Withers, Pedro M Alzari.
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.Entities:
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Year: 2004 PMID： 15130470 DOI： 10.1016/j.str.2004.02.036
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006