Product binding varies dramatically between processive and nonprocessive cellulase enzymes.

@article{Bu2012ProductBV,
  title={Product binding varies dramatically between processive and nonprocessive cellulase enzymes.},
  author={Lintao Bu and Mark R. Nimlos and Michael R. Shirts and Jerry St{\aa}hlberg and Michael E. Himmel and Michael F. Crowley and Gregg T Beckham},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 29},
  pages={24807-13}
}
Cellulases hydrolyze β-1,4 glycosidic linkages in cellulose, which are among the most prevalent and stable bonds in Nature. Cellulases comprise many glycoside hydrolase families and exist as processive or nonprocessive enzymes. Product inhibition negatively impacts cellulase action, but experimental measurements of product-binding constants vary significantly, and there is little consensus on the importance of this phenomenon. To provide molecular level insights into cellulase product… CONTINUE READING
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