Journal article

Publication year: 2006

Pages: 3595-3600

Journal: FEBS Letters

Volume number: 580

Issue number: 15

ISSN: 0014-5793

DOI Link: https://doi.org/10.1016/j.febslet.2006.05.038

Publisher: Wiley

Abstract: 
The substrate spectrum of human thioredoxin reductase (hTrxR) is attributed to its C-terminal extension of 16 amino acids carrying a selenocysteine residue. The concept of an evolutionary link between thioredoxin reductase and glutathione reductase (GR) is presently discussed and supported by the fact that almost all residues at catalytic and substrate recognition sites are identical. Here, we addressed the question if a deletion of the C-terminal part of TrxR leads to recognition of glutathione disullide (GSSG), the substrate of GR. We introduced mutations at the putative substrate binding site to enhance GSSG binding and turnover. However, none of these enzyme species accepted GSSG as substrate better than the full length cysteine mutant of TrxR, excluding a role of the C-terminal extension in preventing GSSG binding. Furthermore, we show that GSSG binding at the N-terminal active site of TrxR is electrostatically disfavoured. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Harvard Citation style: Urig, S., Lieske, J., Fritz-Wolf, K., Irmler, A. and Becker, K. (2006) Truncated mutants of human thioredoxin reductase 1 do not exhibit glutathione reductase activity, FEBS Letters, 580(15), pp. 3595-3600. https://doi.org/10.1016/j.febslet.2006.05.038

APA Citation style: Urig, S., Lieske, J., Fritz-Wolf, K., Irmler, A., & Becker, K. (2006). Truncated mutants of human thioredoxin reductase 1 do not exhibit glutathione reductase activity. FEBS Letters. 580(15), 3595-3600. https://doi.org/10.1016/j.febslet.2006.05.038