Thioredoxin (TRX) catalyzes the reduction of disulfide bonds in proteins via the NADPH-dependent thioredoxin reductase system. Reducing the disulfide bonds of allergenic proteins in food by TRX lowers the allergenicity. We established in this study a method to prepare TRX-enriched extracts from the edible yeast, Saccharomyces cerevisiae, on a large and practical scale, with the objective of dev...

Mammalian thioredoxin reductases contain a TGA-encoded C-terminal penultimate selenocysteine (Sec) residue, and show little homology to bacterial, yeast, and plant thioredoxin reductases. Here we show that the nematode, Caenorhabditis elegans, contains two homologs related to the mammalian thioredoxin reductase family. The gene for one of these homologs contains a cysteine codon in place of TGA...

The flavin prosthetic group (FAD) of thioredoxin reductase has been replaced by 1-deazaFAD (carbon substituted for nitrogen at position 1). Reduction of 1-deazaFAD-thioredoxin reductase by four electrons proceeds in two stages having midpoint potentials that are separated by 0.063 V. Two-electron reduced 1-deazaFAD-thioredoxin reductase (EH2) has spectral characteristics that are different from...

The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into...

The thioredoxin and glutathione systems play a central role in thiol-disulfide redox homeostasis in many organisms by providing electrons to essential enzymes, and defence against oxidative stress. These systems have recently been characterized in platyhelminth parasites, and the emerging biochemical scenario is the existence of linked processes with the enzyme thioredoxin glutathione reductase...

Heteroaromatic quinols 4-(benzothiazol-2-yl)-4-hydroxycyclohexa-2,5-dienone (1) and 4-(1-benzenesulfonyl-1H-indol-2-yl)-4-hydroxycyclohexa-2,5-dienone (2) exhibit potent and selective antitumor activity against colon, renal, and breast carcinoma cell lines in vitro (GI50 < 500 nmol/L). In vivo growth inhibition of renal, colon, and breast xenografts has been observed. Profound G2-M cell cycle b...

Keywords Malignancy Thioredoxin reductase Thioredoxin system Thioredoxin system comprised of thiorexin and NADPH dependent thiorexin reductase, is responsible for redox regulation of cells by controlling the apoptosis, proliferation and other vital processes of cells. The efficacy of thioredoxin system has been represented in a wide range of physiological and biological reactions in bacteria, y...

Thioredoxin reductase and thioredoxin constitute the cellular thioredoxin system, which provides reducing equivalents to numerous intracellular target disulfides. Mammalian thioredoxin reductase contains the rare amino acid selenocysteine. Known as the "21st" amino acid, selenocysteine is inserted into proteins by recoding UGA stop codons. Some model eukaryotic organisms lack the ability to ins...

Partial purification of a thioredoxin system from Novikoff ascites hepatoma cells has been previously reported (MOORE, E. C. (1967) Biochem. Biophys. Res. Commun. 29, 264-268). Thioredoxin from the same mammalian source has now been purified to electrophoretic homogeneity by ammonium sulfate fractionation, heat treatment, DEAE-cellulose chromatography, and Sephadex chromatography. 1-Dimethylami...