Neisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Binding

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Title Neisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Binding
Author Bohm, Raphael; Freiberger, Friedrich; Stummeyer, Katharina; Gerardy-Schahn, Rita; von Itzstein, Mark; Haselhorst, Thomas Erwin
Journal Name ChemBioChem
Year Published 2010
Place of publication Germany
Publisher Wiley-VCH Verlag
Abstract On the loose: We report an STD NMR spectroscopic study of the polysialyltransferase from Neisseria meningitidis serogroup B (NmB-polyST). The spectra reveal that the cytosine and ribose moiety receive more saturation than the sialic acid residue of CMP-Neu5Ac. This loose binding enables a fast and efficient sialyl transfer to the acceptor substrate. Our analysis offers a view of the structural determinants necessary for binding to NmB-polyST that provide the basis for the development of novel NmB-polyST inhibitors.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1002/cbic.200900659
Volume 11
Issue Number 2
Page from 170
Page to 174
ISSN 1439-4227
Date Accessioned 2010-11-26
Date Available 2011-03-07T08:54:03Z
Language en_AU
Research Centre Institute for Glycomics
Faculty Faculty of Science, Environment, Engineering and Technology
Subject Medical Biochemistry and Metabolomics
URI http://hdl.handle.net/10072/36880
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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