Hydrolase and sialyltransferase activities of Trypanosoma cruzi trans-sialidase towards NeuAc-α-2,3-Gal-β-O-PNP

Harrison, Jennifer A., Kartha, K. P. Ravindranathan, Turnbull, W. Bruce, Scheuerl, Shona L., Naismith, James H., Schenkman, Sergio and Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275 (2001) Hydrolase and sialyltransferase activities of Trypanosoma cruzi trans-sialidase towards NeuAc-α-2,3-Gal-β-O-PNP. Bioorganic and Medicinal Chemistry Letters, 11 (2). pp. 141-144. ISSN 0960-894X

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Abstract

NeuAc-α-2,3-Gal-β-O-PNP has been synthesised and its ability to act as a substrate for the hydrolase and transferase activities of Trypanosoma cruzi trans-sialidase have been investigated. The turn-over of this compound shows marked differences from the behaviour of NeuAc-MU. In addition, distinct differences in the action of T. cruzi trans-sialidase and Clostridium perfringens neuraminidase on NeuAc-α-2,3-Gal-β-O-PNP were apparent.

Item Type:	Article
Additional Information:	Funding Information: This work was supported by the BBSRC, the Wellcome Trust (Grant refs: 042472 and 040331), GlaxoWellcome, and the Association for International Cancer Research.
Uncontrolled Keywords:	biochemistry,molecular medicine,molecular biology,pharmaceutical science,drug discovery,clinical biochemistry,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School:	Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	10 Sep 2024 12:30
Last Modified:	25 Sep 2024 18:08
URI:	https://ueaeprints.uea.ac.uk/id/eprint/96660
DOI:	10.1016/S0960-894X(00)00611-9

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