Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions.

@article{Davoodi1995AbnormallyHP,
  title={Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions.},
  author={Jamshid Davoodi and Warren W. Wakarchuk and Robert L. Campbell and Paul R Carey and Witold K Surewicz},
  journal={European journal of biochemistry},
  year={1995},
  volume={232 3},
  pages={839-43}
}
The active site of Bacillus circulans xylanase (1,4-beta-D-xylanohydrolase, EC 3.2.1.8) contains two glutamic acid residues, Glu78 and Glu172, which are crucial for the catalytic activity of the enzyme. Fourier-transform infrared spectroscopy was used to determine the ionization state of these residues as a function of pH. For the wild-type enzyme, titration of one of the carboxylate groups occurs at pH 6.8. This titration is absent in the Glu78-->Gln and Glu172-->Gln variants of the enzyme… CONTINUE READING

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