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Glycobiology
Year: 2010  |  Volume: 20  |  Issue: 2  |  Page No.: 158 - 165

An {alpha}2,6-sialyltransferase cloned from Photobacterium leiognathi strain JT-SHIZ-119 shows both sialyltransferase and neuraminidase activity

T Mine, S Katayama, H Kajiwara, M Tsunashima, H Tsukamoto, Y Takakura and T. Yamamoto    

Abstract:

We cloned, expressed, and characterized a novel β-galactoside 2,6-sialyltransferase from Photobacterium leiognathi strain JT-SHIZ-119. The protein showed 56–96% identity to the marine bacterial 2,6-sialyltransferases classified into glycosyltransferase family 80. The sialyltransferase activity of the N-terminal truncated form of the recombinant enzyme was 1477 U/L of Escherichia coli culture. The truncated recombinant enzyme was purified as a single band by sodium dodecyl sulfate polyacrylamide gel electrophoresis through 3 column chromatography steps. The enzyme had distinct activity compared with known marine bacterial 2,6-sialyltransferases. Although 2,6-sialyltransferases cloned from marine bacteria, such as Photobacterium damselae strain JT0160, P. leiognathi strain JT-SHIZ-145, and Photobacterium sp. strain JT-ISH-224, show only 2,6-sialyltransferase activity, the recombinant enzyme cloned from P. leiognathi strain JT-SHIZ-119 showed both 2,6-sialyltransferase and 2,6-linkage-specific neuraminidase activity. Our results provide important information toward a comprehensive understanding of the bacterial sialyltransferases belonging to the group 80 glycosyltransferase family in the CAZy database.

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