Stereochemical course of glucan hydrolysis by barley (1-->3)- and (1-->3, 1-->4)-beta-glucanases.

@article{Chen1995StereochemicalCO,
  title={Stereochemical course of glucan hydrolysis by barley (1-->3)- and (1-->3, 1-->4)-beta-glucanases.},
  author={L. Chen and M. Sadek and B. Stone and R. Brownlee and G. Fincher and P. H{\o}j},
  journal={Biochimica et biophysica acta},
  year={1995},
  volume={1253 1},
  pages={
          112-6
        }
}
The stereochemical course of hydrolysis of Laminaria digitata laminarin and barley (1-->3, 1-->4)-beta-glucan by barley (1-->3)-beta-glucanase (E.C. 3.2.1.39) isoenzyme GII and (1-->3, 1-->4)-beta-glucanase (EC 3.2.1.73) isoenzyme EII, respectively, has been determined by 1H-NMR. Both enzymes catalyse hydrolysis with retention of anomeric configuration (e-->e) and may therefore operate via a double displacement mechanism. We predict that all other members of Family 17 of beta-glycosyl… Expand
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  • Biology, Medicine
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