Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser.

@article{Madison1993ConvertingTP,
  title={Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser.},
  author={Edwin L. Madison and Annette Kobe and M J Gething and Joseph F. Sambrook and Elizabeth J. Goldsmith},
  journal={Science},
  year={1993},
  volume={262 5132},
  pages={419-21}
}
Unlike most serine proteases of the chymotrypsin family, tissue-type plasminogen activator (tPA) is secreted from cells as an active, single-chain enzyme with a catalytic efficiency only slightly lower than that of the proteolytically cleaved form. A zymogenic mutant of tPA has been engineered that displays a reduction in catalytic efficiency by a factor of 141 in the single-chain form while retaining full activity in the cleaved form. The residues introduced in the mutant, serine 292 and… CONTINUE READING

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