Functional Significance of Conserved Glycine 127 in a Human Dual-Specificity Protein Tyrosine Phosphatase

@article{Zeng2003FunctionalSO,
  title={Functional Significance of Conserved Glycine 127 in a Human Dual-Specificity Protein Tyrosine Phosphatase},
  author={W.-Y. Zeng and Y. Wang and Y.-C. Zhang and W. Yang and Y.-Y. Shi},
  journal={Biochemistry (Moscow)},
  year={2003},
  volume={68},
  pages={634-638}
}
Using site-directed mutagenesis and steady-state kinetic measurements, the functional role of the conserved glycine 127 in a human vaccinia H1-related phosphatase (VHR) was investigated. The mutations of Gly127 to Ala and Pro resulted in a significant decrease in k cat/K m, and increase in K i for arsenate, indicating that flexibility at the Gly127 site has a large effect on substrate binding and catalytic activity. No substantial decrease in k cat/K m and increase in K i values were observed… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.

References

Publications referenced by this paper.

VHR Wild type G127A G127P G127 deletion Kinetic parameters and arsenate inhibition constants for wild type and mutant

  • ZENG
  • VHR Ki,
  • 1991
1 Excerpt

Similar Papers

Loading similar papers…