Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus.

@article{Yoshida2010RoleOA,
  title={Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus.},
  author={Erina Yoshida and Masafumi Hidaka and Shinya Fushinobu and Takashi Koyanagi and Hiromichi Minami and Hisanori Tamaki and Motomitsu Kitaoka and Takane Katayama and Hidehiko Kumagai},
  journal={The Biochemical journal},
  year={2010},
  volume={431 1},
  pages={39-49}
}
β-Glucosidase from Kluyveromyces marxianus (KmBglI) belongs to the GH3 (glycoside hydrolase family 3). The enzyme is particularly unusual in that a PA14 domain (pf07691), for which a carbohydrate-binding role has been claimed, is inserted into the catalytic core sequence. In the present study, we determined the enzymatic properties and crystal structure of KmBglI in complex with glucose at a 2.55 A (1 A=0.1 nm) resolution. A striking characteristic of KmBglI was that the enzyme activity is… CONTINUE READING
25 Citations
44 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 25 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 44 references

Prevotella ruminicola 23

  • E. Yoshida, M. Hidaka, +5 authors H. Kumagai
  • J. Bacteriol
  • 2009

Volvariella volvacea, the edible straw mushroom

  • D. Dodd, S. A. Kocherginskaya, +4 authors I.K.O. Cann
  • Enzyme Microb. Technol
  • 2009

of a barley β - D - glucan exohydrolase , a family 3 glycosyl hydrolase

  • M. D. Balcewich, K. A. Stubbs, +4 authors B. L. Mark
  • 2009

Similar Papers

Loading similar papers…