Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.

@article{Severi2008SialicAM,
  title={Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.},
  author={Emmanuele Severi and Axel M{\"u}ller and Jennifer R. Potts and Andrew P. Leech and David Williamson and Keith S Wilson and Gavin H. Thomas},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 8},
  pages={4841-9}
}
The acquisition of host-derived sialic acid is an important virulence factor for some bacterial pathogens, but in vivo this sugar acid is sequestered in sialoconjugates as the alpha-anomer. In solution, however, sialic acid is present mainly as the beta-anomer, formed by a slow spontaneous mutarotation. We studied the Escherichia coli protein YjhT as a member of a family of uncharacterized proteins present in many sialic acid-utilizing pathogens. This protein is able to accelerate the… CONTINUE READING

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YjhT Is a Sialic Acid Mutarotase 4848 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • T. R. Schneider, G. M. Sheldrick
  • Crystallogr. Sect. D Biol. Crystallogr
  • 2008
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Nucleic Acids Res. 35,W375–W383 YjhT Is a Sialic Acid Mutarotase

  • I. W. Davis, A. Leaver-Fay, +9 authors D. C. Richardson
  • FEBRUARY 22,
  • 2007
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