We investigated the acceptor substrate specificities of marine bacterial alpha-(2-->3)-sialyltransferase cloned from Photobacterium sp. JT-ISH-224 and alpha-(2-->6)-sialyltransferase cloned from Photobacterium damselae JT0160 using several saccharides as acceptor substrates. After purifying the enzymatic reaction products, we confirmed their structure by NMR spectroscopy. The alpha-(2-->3)-sialyltransferase transferred N-acetylneuraminic acid (Neu5Ac) from cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac) to the beta-anomeric hydroxyl groups of mannose (Man) and alpha-Manp-(1-->6)-Manp, and alpha-(2-->6)-sialyltransferase transferred N-acetylneuraminic acid to the 6-OH groups of the non-reducing end galactose residues in beta-Galp-(1-->3)-GlcpNAc and beta-Galp-(1-->6)-GlcpNAc.
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