Differential temperature dependence of tobacco etch virus and rhinovirus 3C proteases

Sreejith Raran-Kurussi, József Tözsér, Scott Cherry, Joseph E. Tropea, David S. Waugh

Research output: Contribution to journalArticle

14 Citations (Scopus)


Because of their stringent sequence specificity, the 3C-like proteases from tobacco etch virus (TEV) and human rhinovirus are often used for the removal of affinity tags. The latter enzyme is rumored to have greater catalytic activity at 4 °C, the temperature at which fusion protein substrates are usually digested. Here we report that experiments with fusion protein and peptide substrates confirm this conjecture. Whereas the catalytic efficiency of rhinovirus 3C protease is approximately the same at its optimum temperature (30 °C) and at 4 °C, TEV protease is 10-fold less active at the latter temperature due primarily to a reduction in kcat.

Original languageEnglish
Pages (from-to)142-144
Number of pages3
JournalAnalytical Biochemistry
Issue number2
Publication statusPublished - May 15 2013


  • 3C protease
  • Affinity tag removal
  • Fusion protein protease
  • Prescission protease
  • Protease
  • Tobacco etch virus (TEV) protease

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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