Kinetic and Mechanistic Analysis of Trypanosoma cruzi Trans-Sialidase Reveals a Classical Ping-Pong Mechanism with Acid/Base Catalysis-Reference-Cited by-同舟云学术

Kinetic and Mechanistic Analysis of Trypanosoma cruzi Trans-Sialidase Reveals a Classical Ping-Pong Mechanism with Acid/Base Catalysis

Published:2008-02-20 Issue:11 Volume:47 Page:3507-3512
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Damager Iben¹,Buchini Sabrina¹,Amaya Maria F.¹,Buschiazzo Alejandro¹,Alzari Pedro¹,Frasch Alberto C.¹,Watts Andrew¹,Withers Stephen G.¹

Affiliation:

1. Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, British Columbia, V6T1Z1 Canada, Unite de Biochimie Structurale, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris, France, and Instituto de Investigaciones Biotechnologicas, Universidad National de San Martin, CC 30, 1650 San Martin, Argentina

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi7024832

Reference20 articles.

1. Structural basis of sialyltransferase activity in trypanosomal sialidases

2. STRUCTURAL AND FUNCTIONAL PROPERTIES OF TRYPANOSOMA TRANS-SIALIDASE

3. Enzymatic characterization of beta-D-galactoside alpha 2,3-trans-sialidase from Trypanosoma cruzi

4. Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase

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