Structural Insights Into the Catalytic Mechanism of Trypanosoma Cruzi Trans-Sialidase

María Fernanda Amaya (1) , Andrew G Watts (2) , Iben Damager (2) , Annemarie Wehenkel (1) , Tong Nguyen (1) , Alejandro Buschiazzo (1) , Gastón Paris (3) , A.Carlos Frasch (3) , Stephen G Withers (2) , Pedro M Alzari (1)

1 Biochimie Structurale
2 UBC - University of British Columbia
3 UNSAM - Universidad Nacional de San Martin

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.

Domains: Cristallography; Biochemistry [q-bio.BM]

María Fernanda Amaya, Andrew G Watts, Iben Damager, Annemarie Wehenkel, Tong Nguyen, et al.. Structural Insights Into the Catalytic Mechanism of Trypanosoma Cruzi Trans-Sialidase. Structure, 2004, 12 (5), pp.775 - 784. ⟨10.1016/j.str.2004.02.036⟩. ⟨pasteur-02554101⟩