Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism.

@article{Itoh2006CrystalSO,
  title={Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism.},
  author={Takafumi Itoh and Wataru Hashimoto and Bunzo Mikami and Kousaku Murata},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 40},
  pages={29807-16}
}
Unsaturated glucuronyl hydrolase (UGL), which is a member of glycoside hydrolase family GH-88, is a bacterial enzyme that degrades mammalian glycosaminoglycans and bacterial biofilms. The enzyme, which acts on unsaturated oligosaccharides with an alpha-glycoside bond produced by microbial polysaccharide lyases responsible for bacterial invasion of host cells, was believed to release 4-deoxy-l-threo-5-hexosulose-uronate (unsaturated glucuronic acid, or DeltaGlcA) and saccharide with a new… CONTINUE READING

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References

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Showing 1-3 of 3 references

PLATON, a multipurpose crystallographic tool, Utrecht University, The Netherlands

A. L. Speck
2001

Solvent isotope effects for equilibria and reactions in solute-solvent interactions, Coetzee JG, Richie CD (eds) pp 407-412

P. M. Laughton, R. E. Robertson
1969

Sptem er 1, 2017 hp://w w w .jb.org/ D ow nladed from Structure of UGL complexed with substrate

A. K. Convington, M. Paabo, R. A. Robinson, R. G. Bates
Anal. Chem. 40, • 1968

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