Evidence for tryptophan in proximity to histidine and cysteine as essential to the active site of an alkaline protease.

@article{Tanksale2000EvidenceFT,
  title={Evidence for tryptophan in proximity to histidine and cysteine as essential to the active site of an alkaline protease.},
  author={A M Tanksale and J V Vernekar and Mohini S. Ghatge and Vasanti V. Deshpande},
  journal={Biochemical and biophysical research communications},
  year={2000},
  volume={270 3},
  pages={910-7}
}
The presence, microenvironment, and proximity of an essential Trp with the essential His and Cys residues in the active site of an alkaline protease have been demonstrated for the first time using chemical modification, chemo-affinity labeling, and fluorescence spectroscopy. Kinetic analysis of the N-bromosuccinimide- (NBS) or p-hydroxymercuribenzoate- (PHMB) modified enzyme from Conidiobolus sp. revealed that a single Trp and Cys are essential for activity in addition to the Asp, His, and Ser… CONTINUE READING

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