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Updated: Aug 9, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
Published on: November 25, 2017
Coliphage derived sialidase preferentially recognizes nonreducing end of polysialic acid
Yohei Kataoka1, Katsuhide Miyake, Shinji Iijima
1Department of Biotechnology, Graduate School of Engineering, Nagoya University, Nagoya 464-8603, Japan.
Abstract:
Bacteriophages infecting Escherichia coli K1 strains generally have endotype polysialic acid-degrading enzymes. We studied the digestion mechanism of a sialidase associated with the coliphage 63D using polysialic acid radiolabeled at its nonreducing end or reducing end. It was found that this enzyme preferentially recognizes the nonreducing end of polysialic acid, suggesting that the 63D associated sialidase does not randomly digest its substrate but acts like an exotype glycosidase.
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