Mutational and structural studies of the active-site residues in truncated Fibrobacter succinogenes1,3-1,4-beta-D-glucanase.

@article{Tsai2008MutationalAS,
  title={Mutational and structural studies of the active-site residues in truncated Fibrobacter succinogenes1,3-1,4-beta-D-glucanase.},
  author={L. Tsai and Hsiao-Chuan Huang and C. Hsiao and Yuan-Neng Chiang and L. Shyur and Yu-Shiun Lin and Shu-hua Lee},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2008},
  volume={64 Pt 12},
  pages={
          1259-66
        }
}
1,3-1,4-beta-D-Glucanases (EC 3.2.1.73) specifically hydrolyze beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in lichenan or beta-D-glucans. It has been suggested that truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase (TFsbeta-glucanase) can accommodate five glucose rings in its active site upon enzyme-substrate interaction. In this study, 12 mutant enzymes were created by mutating the conserved residues Gln70, Asn72, Gln81 and Glu85 proposed to bind to… Expand
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