and have a tendency to aggregate, indicating that formation of a second disulphide in the molecule is accompanied by denaturation of the structure. Reduction of oxidized thymus thioredoxin can be achieved by dithiothreitol or by NADPH and thioredoxin reductase representing a possible autocatalytic control mechanism. Another major difference between the mammalian and the E. coli thioredoxin syst...

The thioredoxin (Trx) system consists of thioredoxin reductase (TrxR), Trx, and nicotinamide adenine dinucleotide phosphate (NADPH). TrxR is an NADPH-dependent oxidoreductase. Trx is a ubiquitous small protein with a redox-active disulfide bridge that plays important regulatory roles in some vital metabolic reactions. In this study, a cDNA sequence (SpTrx1) showing high identity to the first Tr...

Escherichia coli B contains a cytidine diphosphate reductase system which utilizes reduced triphosphopyridine nucleotide to effect the reduction of cytidine diphosphate to deoxycytidine diphosphate (1, 2). Two components, thioredoxin and thioredoxin reductase, have been identified as oxidation-reduction carriers between TPNH and cytidine diphosphate. Thioredoxin is a low molecular weight protei...

Activity of the cysteine adducts of the cysteine proteinases papain and thaumatopain can be recovered by treatment with thioredoxin, thioredoxin reductase and NADPH. Recovery of proteinase activity did not occur if any of the components of the thioredoxin system were omitted, or if thioredoxin or thioredoxin reductase were heat-inactivated. Such an enzyme-mediated process may be of significance...

The thioredoxin system plays an important role in maintaining a reducing environment in the cell. Recently, several thioredoxin binding partners have been identified and proposed to mediate aspects of redox signaling, but the significance of these interactions is unclear in part due to incomplete understanding of the mechanism for thioredoxin binding. Thioredoxin-interacting protein (Txnip) is ...

The cytosolic thioredoxin redox system composed of thioredoxin-1 and the NADPH-dependent thioredoxin reductase-1 reductase is an important regulator of cell growth and survival. Thioredoxin-1 is overexpressed in many human tumors where it is associated with increased cell proliferation, decreased apoptosis, and decreased patient survival. We hypothesized that thioredoxin reductase-1 provides a ...

In addition to the standard NADPH thioredoxin reductases (NTRs), plants hold a plastidic NTR (NTRC), with a thioredoxin module fused at the C-terminus. NTRC is an efficient reductant of 2-Cys peroxiredoxins (2-Cys Prxs). The interaction of NTRC and chloroplastic thioredoxin x with 2-Cys Prxs has been confirmed in vivo, by bimolecular fluorescence complementation (BiFC) assays, and in vitro, by ...

Taenia solium thioredoxin-1 gene (TsTrx-1) has a length of 771 bp with three exons and two introns. The core promoter gene presents two putative stress transcription factor binding sites, one putative TATA box, and a transcription start site (TSS). TsTrx-1 mRNA is expressed higher in larvae than in adult. This gene encodes a protein of 107 amino acids that presents the Trx active site (CGPC), t...

Nicotinamide cofactor-dependent oxidoreductases have become a valuable tool for the synthesis of high value chiral compounds. The feasibility biocatalytic processes involving these enzymes stands and falls with efficiency regeneration cofactors. In this study, we describe novel NADPH method based on natural thioredoxin electron delivery system. Thioredoxin 1 (Trx1) reductase (TR) from Thermus t...

Thioredoxin is a small, multifunctional protein with a redox-active disulfide/dithiol in the active site. Thioredoxin plays several important biologic roles both in intracellular and extracellular compartments with its redox-regulating and reactive oxygen intermediates scavenging activities. We assayed the seizure response and the excitotoxic hippocampal injury in thioredoxin transgenic and wil...