EVALUATION OF THE MARINE BACTERIAL <2,3-SIALYLTRANSFERASE ACTIVITY TOWARD INOSITOLS

摘要

Sialyltransferases transfer N-acetylneuraminic acid (NeuAc) from the common donor substrate of these enzymes, cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-NeuAc), to acceptor substrates. To date, we have demonstrated that marine bacterial sialyltransferases show broad acceptor substrate specificities. For instance, the α2,3-sialyltransferase from Photobacterium sp. JT-ISH-224 can transfer NeuAc residue to both the 3'-OH and the 2-OH groups of lactose simultaneously, and gave 2,3'-disialyllactose as the reaction product [1]. Furthermore, the sialyltransferase reaction toward the mannose as the substrate gave the sialylrnannoside in which the α-NeuAc residue is coupled to the anomeric position of mannose via β-glycosidic bond [2].