Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei cellobiohydrolase I.

@article{Reinikainen1992InvestigationOT,
  title={Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei cellobiohydrolase I.},
  author={Tapani Reinikainen and Laura Ruohonen and Tarja K. Nevanen and Leif Laaksonen and Per Kraulis and T. A. Jones and Jonathan C Knowles and Tuula T. Teeri},
  journal={Proteins},
  year={1992},
  volume={14 4},
  pages={475-82}
}
The function of the cellulose-binding domain (CBD) of the cellobiohydrolase I of Trichoderma reesei was studied by site-directed mutagenesis of two amino acid residues identified by analyzing the 3D structure of this domain. The mutant enzymes were produced in yeast and tested for binding and activity on crystalline cellulose. Mutagenesis of the tyrosine residue (Y492) located at the tip of the wedge-shaped domain to alanine or aspartate reduced the binding and activity on crystalline cellulose… CONTINUE READING

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