Thioredoxin Reductase

Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat.

Thioredoxins h are ubiquitous proteins reduced by NADPH- thioredoxin reductase (NTR). They are able to reduce disulphides in target proteins. In monocots, thioredoxins h accumulate at high level in seeds and show a predominant localization in the nucleus of seed cells. These results suggest that the NTR-thioredoxin h system probably plays an important role in seed physiology. To date, the study...

Mammalian Selenoprotein Thioredoxin-glutathione Reductase

Thioredoxin Reductase and its Inhibitors

Thioredoxin plays a crucial role in a wide number of physiological processes, which span from reduction of nucleotides to deoxyriboucleotides to the detoxification from xenobiotics, oxidants and radicals. The redox function of Thioredoxin is critically dependent on the enzyme Thioredoxin NADPH Reductase (TrxR). In view of its indirect involvement in the above mentioned physio/pathological proce...

NADPH-Dependent Thioredoxin Reductase and a New Thioredoxin from Wheat

An albumin fraction extracted from wheat flour contains thioredoxin reductase (Mr = 65,000) and a heat-stable thioredoxin (Mr = 15,000) which are separated on DEAE cellulose and further purified by gel filtration. W heat thioredoxin stimulates E. coli ribonucleotide reductase but not chloroplast fructose-bis-phosphatase. The enzyme is NADPH-dependent (Km = 3.2 X 10 -6 m) . In presence of the th...

Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase.

Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/o...