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Glycobiology
Year: 2010  |  Volume: 20  |  Issue: 2  |  Page No.: 260 - 268

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

J Cheng, S Huang, H Yu, Y Li, K Lau and X. Chen    

Abstract:

Trans-sialidases catalyze the transfer of a sialic acid from one sialoside to an acceptor to form a new sialoside. 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. 2,8-Trans-sialidase activity was also described for a multifunctional Campylobacter jejuni sialyltransferase CstII. We report here the discovery of the 2,6-trans-sialidase activity of a previously reported recombinant truncated bacterial 2,6-sialyltransferase from Photobacterium damsela (15Pd2,6ST). This is the first time that the 2,6-trans-sialidase activity has ever been identified. Kinetic studies indicate that 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 Neu5AcpNP and LacβMU, 2,6-linked sialoside Neu5Ac2,6LacβMU has been obtained in one-step in high yield using the trans-sialidase activity of 15Pd2,6ST. In addition to the 2,6-trans-sialidase activity, 15Pd2,6ST also has 2,6-sialidase activity. The multifunctionality is thus a common feature of many bacterial sialyltransferases.

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