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Regulation of thioredoxin peroxidase activity by C-terminal truncation.
Arch Biochem Biophys. 2002 Jan 15; 397(2):312-8.AB

Abstract

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 (Delta192, Delta191, Delta188, Delta184, Delta176, and Delta165) revealed that TPx could be inactivated (Delta192), reactivated (Delta191-Delta176) and reinactivated (Delta165) by serial truncation from C-terminus. We did not find any significant kinetic difference among reactivated forms; however, distinctive loss of affinity to H2O2 (K(m) = 5 microM) than that of the intact form (<<5 microM, undeterminable) was monitored. Characterization of a series of Lys(191) point mutants manifested that the loss of affinity caused by a deprivation of positive charge born in Lys(191) and the loss of affinity resulted in the resistibility to H2O2. Disk inhibition assay with S. pombe cells overexpressing wild-type, Delta192 and Delta191 mutants evidenced that the truncated forms functioning in vitro as well as in vivo.

Authors+Show Affiliations

Department of Biological Sciences, Chonnam National University, Gwangju, 500-757, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11795888

Citation

Koo, Kyung Hee, et al. "Regulation of Thioredoxin Peroxidase Activity By C-terminal Truncation." Archives of Biochemistry and Biophysics, vol. 397, no. 2, 2002, pp. 312-8.
Koo KH, Lee S, Jeong SY, et al. Regulation of thioredoxin peroxidase activity by C-terminal truncation. Arch Biochem Biophys. 2002;397(2):312-8.
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), 312-8.
Koo KH, et al. Regulation of Thioredoxin Peroxidase Activity By C-terminal Truncation. Arch Biochem Biophys. 2002 Jan 15;397(2):312-8. PubMed PMID: 11795888.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of thioredoxin peroxidase activity by C-terminal truncation. AU - Koo,Kyung Hee, AU - Lee,Songmi, AU - Jeong,Soo Young, AU - Kim,Eui Tae, AU - Kim,Hyung Jung, AU - Kim,Kanghwa, AU - Song,Kiwon, AU - Chae,Ho Zoon, PY - 2002/2/6/pubmed PY - 2002/2/28/medline PY - 2002/2/6/entrez SP - 312 EP - 8 JF - Archives of biochemistry and biophysics JO - Arch Biochem Biophys VL - 397 IS - 2 N2 - 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 (Delta192, Delta191, Delta188, Delta184, Delta176, and Delta165) revealed that TPx could be inactivated (Delta192), reactivated (Delta191-Delta176) and reinactivated (Delta165) by serial truncation from C-terminus. We did not find any significant kinetic difference among reactivated forms; however, distinctive loss of affinity to H2O2 (K(m) = 5 microM) than that of the intact form (<<5 microM, undeterminable) was monitored. Characterization of a series of Lys(191) point mutants manifested that the loss of affinity caused by a deprivation of positive charge born in Lys(191) and the loss of affinity resulted in the resistibility to H2O2. Disk inhibition assay with S. pombe cells overexpressing wild-type, Delta192 and Delta191 mutants evidenced that the truncated forms functioning in vitro as well as in vivo. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/11795888/Regulation_of_thioredoxin_peroxidase_activity_by_C_terminal_truncation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003986101927006 DB - PRIME DP - Unbound Medicine ER -