Coliphage derived sialidase preferentially recognizes nonreducing end of polysialic acid.
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.
Department of Biotechnology, Graduate School of Engineering, Nagoya University, Nagoya 464-8603, Japan.
Yohei
Y
Kataoka
Katsuhide
K
Miyake
Shinji
S
Iijima
D003090:Coliphages / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D009439:Neuraminidase / Q000235:genetics / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*; D013379:Substrate Specificity
D012794:Sialic Acids; C021319:polysialic acid; D009439:Neuraminidase