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Glycobiology Advance Access published online on October 30, 2009
Glycobiology, doi:10.1093/glycob/cwp172
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Trans-sialidase activity of Photobacterium damsela {alpha}2,6-sialyltransferase and its application in the synthesis of sialosides

Jiansong Cheng, Shengshu Huang, Hai Yu, Yanhong Li, Kam Lau and Xi Chen1

Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616, USA

1 To whom correspondence should be addressed; Tel: 1-530-754-6037; Fax: 1-530-752-8995; e-mail: chen{at}chem.ucdavis.edu

Received on August 14, 2009; accepted on October 27, 2009

Trans-sialidases catalyze the transfer of a sialic acid from one sialoside to an acceptor to form a new sialoside. {alpha}2,3-Trans-sialidase activity was initially discovered in the parasitic protozoan Trypanosoma cruzi, and more recently was found in a multifunctional Pasteurella multocida sialyltransferase PmST1. {alpha}2,8-Trans-sialidase activity was also described for a multifunctional Campylobacter jejuni sialyltransferase CstII. We report here the discovery of the {alpha}2,6-trans-sialidase activity of a previously reported recombinant truncated bacterial {alpha}2,6-sialyltransferase from Photobacterium damsela ({Delta}15Pd2,6ST). This is the first time that the {alpha}2,6-trans-sialidase activity has ever been identified. Kinetic studies indicate that {Delta}15Pd2,6ST-catalyzed trans-sialidase reaction follows a ping-pong bi-bi reaction mechanism. Cytidine 5’-monophosphate, the product of sialyltransferase reactions, is not required by the trans-sialidase activity of the enzyme but enhances the trans-sialidase activity modestly as a non-essential activator. Using chemically synthesized Neu5Ac{alpha}pNP and LacβMU, {alpha}2,6-linked sialoside Neu5Ac{alpha}2,6LacβMU has been obtained in one-step in high yield using the trans-sialidase activity of {Delta}15Pd2,6ST. In addition to the {alpha}2,6-trans-sialidase activity, {Delta}15Pd2,6ST also has {alpha}2,6-sialidase activity. The multifunctionality is thus a common feature of many bacterial sialyltransferases.

Key words: Enzyme / sialidase / sialoside / sialyltransferase / trans-sialidase


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