Characterization of Ruminococcus albus cellodextrin phosphorylase and identification of a key phenylalanine residue for acceptor specificity and affinity to the phosphate group.

@article{Sawano2013CharacterizationOR,
  title={Characterization of Ruminococcus albus cellodextrin phosphorylase and identification of a key phenylalanine residue for acceptor specificity and affinity to the phosphate group.},
  author={Tatsuya Sawano and Wataru Saburi and Ken Hamura and Hirokazu Matsui and Haruhide Mori},
  journal={The FEBS journal},
  year={2013},
  volume={280 18},
  pages={4463-73}
}
Ruminococcus albus has the ability to intracellularly degrade cello-oligosaccharides primarily via phosphorolysis. In this study, the enzymatic characteristics of R. albus cellodextrin phosphorylase (RaCDP), which is a member of glycoside hydrolase family 94, was investigated. RaCDP catalyzes the phosphorolysis of cellotriose through an ordered 'bi bi… CONTINUE READING