Three Streptococcus pneumoniae Sialidases: Three Different Products

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Title Three Streptococcus pneumoniae Sialidases: Three Different Products
Author Xu, Guogang; Kiefel, Milton; Wilson, Jenny; Andrew, Peter W.; Oggioni, Marco R.; Taylor, Garry L.
Journal Name Journal of the American Chemical Society
Editor Peter J. Stang
Year Published 2011
Place of publication United States
Publisher American Chemical Society
Abstract Streptococcus penumoniae is a major human pathogen responsible for respiratory tract infections, septicemia, and meningitis and continues to produce numerous cases of disease with relatively high mortalities. S. pneumoniae encodes up to three sialidases, NanA, NanB, and NanC, that have been implicated in pathogenesis and are potential drug targets. NanA has been shown to be a promiscuous sialidase, hydrolyzing the removal of Neu5Ac from a variety of glycoconjugates with retention of configuration at the anomeric center, as we confirm by NMR. NanB is an intramolecular trans-sialidase producing 2,7-anhydro-Neu5Ac selectively from R2,3-sialosides. Here, we show that the first product of NanC is 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en) that can be slowly hydrated by the enzyme to Neu5Ac. We propose that the three pneumococcal sialidases share a common catalytic mechanism up to the final product formation step, and speculate on the roles of the enzymes in the lifecycle of the bacterium.
Peer Reviewed Yes
Published Yes
Alternative URI
Copyright Statement This document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Journal of the American Chemical Society, copyright 2011American Chemical Society after peer review. To access the final edited and published work see
Volume 133
Issue Number 6
Page from 1718
Page to 1721
ISSN 0002-7863
Date Accessioned 2011-06-22
Date Available 2015-09-04T04:34:19Z
Language en_US
Research Centre Institute for Glycomics
Faculty Faculty of Science, Environment, Engineering and Technology
Subject Proteins and Peptides
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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