Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.

@article{Deshpande1990ChemicalMO,
  title={Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.},
  author={Vasanti V. Deshpande and J Hinge and M B Rao},
  journal={Biochimica et biophysica acta},
  year={1990},
  volume={1041 2},
  pages={172-7}
}
N-Bromosuccinimide (NBS) completely inactivated xylanases from Chainia and alkalophilic and thermophilic (AT) Bacillus with a concomittant decrease in absorption at 280 nm and with second-order rate constants of 10,500 and 5000 M-1.min-1, respectively at pH 6.0 and 25 degrees C. The kinetic analysis of inactivation indicated that one and three tryptophan residues were essential for the xylanase activity from Chainia and Bacillus, respectively. The xylanases were also inhibited by 2-hydroxy-5… CONTINUE READING