A recombinant α-(2→3)-sialyltransferase with an extremely broad acceptor substrate specificity fromPhotobacteriumsp. JT-ISH-224 can transferN-acetylneuraminic acid to inositols

Toshiki Mine, Tatsuo Miyazaki, Hitomi Kajiwara, Naoya Tateda, Katsumi Ajisaka, Takeshi Yamamoto

Index: Carbohydr. Res. 345(17) , 2485-90, (2010)

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Abstract

We confirmed that a recombinant α-(2→3)-sialyltransferase cloned from Photobacterium sp. JT-ISH-224 recognizes inositols having a structure corresponding to the C-3 and C-4 of a galactopyranoside moiety, such as epi-, 1d-chiro, myo-, and muco-inositol, as acceptor substrates, and that the enzyme can transfer N-acetylneuraminic acid (Neu5Ac) from cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac) to them. After purifying the reaction products, the structures were confirmed by use of NMR spectroscopy and mass spectrometry. From these results, it was clearly shown that the α-(2→3)-sialyltransferase from Photobacterium sp. JT-ISH-224 recognizes acceptor substrates through the cis-diol structure corresponding to the 3- and 4-position of the galactopyranoside moiety.Copyright © 2010 Elsevier Ltd. All rights reserved.