Regulation of thioredoxin peroxidase activity by C-terminal truncation

K. H. Koo, S. Lee, S. Y. Jeong, E. T. Kim, H. J. Kim, K. Kim, K. Song, H. Z. Chae

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Thioredoxin peroxidase is a member of peroxiredoxin (Prx) family, which uses a thioredoxin (Trx) as an immediate electron donor for the reduction of peroxide. We have identified C-terminal truncated TPx from Schizosaccharomyces pombe and also have found the truncated form is significantly tenacious against the inactivation of H2O2 than the intact form. Peroxidase assay of a series of recombinant C-terminal truncation mutants (Δ192, Δ191, Δ188, Δ184, Δ176, and Δ165) revealed that TPx could be inactivated (Δ192), reactivated (Δ191-Δ176) and reinactivated (Δ165) by serial truncation from C-terminus. We did not find any significant kinetic difference among reactivated forms; however, distinctive loss of affinity to H2O2 (Km = 5 μM) than that of the intact form (< <5 μM, undeterminable) was monitored. Characterization of a series of Lys191 point mutants manifested that the loss of affinity caused by a deprivation of positive charge born in Lys191 and the loss of affinity resulted in the resistibility to H2O2. Disk inhibition assay with S. pombe cells overexpressing wild-type, Δ192 and Δ191 mutants evidenced that the truncated forms functioning in vitro as well as in vivo.

Original languageEnglish
Pages (from-to)312-318
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 2002 Jan 15

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

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    Koo, K. H., Lee, S., Jeong, S. Y., Kim, E. T., Kim, H. J., Kim, K., Song, K., & Chae, H. Z. (2002). Regulation of thioredoxin peroxidase activity by C-terminal truncation. Archives of Biochemistry and Biophysics, 397(2), 312-318.