Enzymatic synthesis of unique sialyloligosaccharides using marine bacterial α-(2→3)- and α-(2→6)-sialyltransferases

• Published in: Carbohydrate research 2010-07, Vol.345 (10), p.1417-1421
• Main Authors: Mine, Toshiki, Miyazaki, Tatsuo, Kajiwara, Hitomi, Naito, Kenta, Ajisaka, Katsumi, Yamamoto, Takeshi
• Format: Article
• Language: English
• Subjects: Carbohydrate Sequence; Marine bacteria; Molecular Sequence Data; Oligosaccharides - chemical synthesis; Oligosaccharides - chemistry; Photobacterium; Photobacterium - enzymology; Sialyltransferase; Sialyltransferases - metabolism; Substrate specificity
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/j.carres.2010.03.036

Enzymatic reaction product derived from α-Man p-(1→6)-Man p as an acceptor substrate by marine bacterial sialyltransferase. We investigated the acceptor substrate specificities of marine bacterial α-(2→3)-sialyltransferase cloned from Photobacterium sp. JT-ISH-224 and α-(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 α-(2→3)-sialyltransferase transferred N-acetylneuraminic acid (Neu5Ac) from cytidine 5′-monophospho- N-acetylneuraminic acid (CMP-Neu5Ac) to the β-anomeric hydroxyl groups of mannose (Man) and α-Man p-(1→6)-Man p, and α-(2→6)-sialyltransferase transferred N-acetylneuraminic acid to the 6-OH groups of the non-reducing end galactose residues in β-Gal p-(1→3)-Glc pNAc and β-Gal p-(1→6)-Glc pNAc.