Characterization of a recombinant Neisseria meningitidis alpha-2,3-sialyltransferase and its acceptor specificity.

@article{Gilbert1997CharacterizationOA,
  title={Characterization of a recombinant Neisseria meningitidis alpha-2,3-sialyltransferase and its acceptor specificity.},
  author={Michel Gilbert and Anne Marie Cunningham and David C. Watson and Alejandro Martin and James C. Richards and Warren W. Wakarchuk},
  journal={European journal of biochemistry},
  year={1997},
  volume={249 1},
  pages={187-94}
}
The structure and specificity of the recombinant alpha-2,3-sialyltransferase from Neisseria meninigitidis are reported. This enzyme showed an unusual acceptor specificity in that it could use alpha-terminal and beta-terminal Gal residues as acceptors. In addition (beta1-->4)-linked and (beta1-->3)-linked terminal Gal served as acceptors. These properties distinguish the bacterial enzyme from the more widely investigated mammalian equivalents. The protein was expressed as a membrane-associated… CONTINUE READING

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