Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition.

@article{Nagem2004CrystalSO,
  title={Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition.},
  author={Ronaldo Alves Pinto Nagem and Adriana L. Rojas and Alexander M. Golubev and Olga S Korneeva and Elena V. Eneyskaya and Anna A Kulminskaya and Kirill N. Neustroev and Igor Polikarpov},
  journal={Journal of molecular biology},
  year={2004},
  volume={344 2},
  pages={471-80}
}
Exo-inulinases hydrolyze terminal, non-reducing 2,1-linked and 2,6-linked beta-d-fructofuranose residues in inulin, levan and sucrose releasing beta-d-fructose. We present the X-ray structure at 1.55A resolution of exo-inulinase from Aspergillus awamori, a member of glycoside hydrolase family 32, solved by single isomorphous replacement with the anomalous scattering method using the heavy-atom sites derived from a quick cryo-soaking technique. The tertiary structure of this enzyme folds into… CONTINUE READING

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