Aminoalcohols as probes of the two-subsite active site of beta-D-xylosidase from Selenomonas ruminantium.

@article{Jordan2009AminoalcoholsAP,
  title={Aminoalcohols as probes of the two-subsite active site of beta-D-xylosidase from Selenomonas ruminantium.},
  author={Douglas Brian Jordan and Jeffrey A Mertens and Jay D. Braker},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1794 1},
  pages={144-58}
}
Catalysis and inhibitor binding by the GH43 beta-xylosidase are governed by the protonation states of catalytic base (D14, pK(a) 5.0) and catalytic acid (E186, pK(a) 7.2) which reside in subsite -1 of the two-subsite active site. Cationic aminoalcohols are shown to bind exclusively to subsite -1 of the catalytically-inactive, dianionic enzyme (D14(-)E186(-)). Enzyme (E) and aminoalcohols (A) form E-A with the affinity progression: triethanolamine>diethanolamine>ethanolamine. E186A mutation… CONTINUE READING