Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum.

@article{Taylor2006StructuralII,
  title={Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum.},
  author={E. Taylor and N. Smith and J. Turkenburg and S. D'Souza and H. Gilbert and G. Davies},
  journal={The Biochemical journal},
  year={2006},
  volume={395 1},
  pages={
          31-7
        }
}
The digestion of the plant cell wall requires the concerted action of a diverse repertoire of enzyme activities. An important component of these hydrolase consortia are arabinofuranosidases, which release L-arabinofuranose moieties from a range of plant structural polysaccharides. The anaerobic bacterium Clostridium thermocellum, a highly efficient plant cell wall degrader, possesses a single alpha-L-arabinofuranosidase (EC 3.2.1.55), CtAraf51A, located in GH51 (glycoside hydrolase family 51… Expand
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Molecular Basis of Arabinobio-hydrolase Activity in Phytopathogenic Fungi
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