thioredoxins (trxs) are small ubiquitous oxidoreductase proteins with two redox-active cys residues in a conserved active site (wcg/ppc) that regulate numerous target proteins via thiol/disulfide exchanges in the cells of prokaryotes and eukaryotes. the isoforms ostrx23 with a typical active site (wcgpc) and ostrx20 with an atypical active site (wctpc) are two  trx h- type isoforms in rice that ...

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...

Thioredoxins (Trxs) are small ubiquitous oxidoreductase proteins with two redox-active Cys residues in a conserved active site (WCG/PPC) that regulate numerous target proteins via thiol/disulfide exchanges in the cells of prokaryotes and eukaryotes. The isoforms OsTrx23 with a typical active site (WCGPC) and OsTrx20 with an atypical active site (WCTPC) are two  Trx h- type isoforms in rice that ...

Selenium compounds like selenite (SeO3(2-) may form a covalent adduct with glutathione (GSH) in the form of selenodiglutathione (GS-Se-SG), which is assumed to be important in the metabolism of selenium. We have isolated GS-Se-SG and studied its reactions with NADPH and thioredoxin reductase from calf thymus or with thioredoxin reductase and thioredoxin from Escherichia coli. Incubation of 0.1 ...

Plants possess two well described thioredoxin systems: a cytoplasmic system including several thioredoxins and an NADPH-dependent thioredoxin reductase and a specific chloroplastic system characterized by a ferredoxin-dependent thioredoxin reductase. On the basis of biochemical activities, plants also are supposed to have a mitochondrial thioredoxin system as described in yeast and mammals, but...

Mitochondrial thioredoxin-glutathione reductase was purified from larval Taenia crassiceps (cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions. At 25 degrees C specific activities were 437 +/- 27 mU mg(-1) and 840 +/- 49 mU mg(-1) with thioredoxin and GSSG, respectively. Apparent K(m)...

Thioredoxin reductase (EC l&4.5), which catalyzes the reduction of the disulfide bridge in thioredoxin by NADPH, was purified from calf liver and thymus. Preparation methods, involving chromatography on DEAE-cellulose, TEAEcellulose, and Sephadex G-200 or G-100 were used to purify the calf liver enzyme llOO-fold and the thymus enzyme 2800fold. The enzyme was shown to catalyze an NADPH-dependent...

Recycling of ascorbic acid from its oxidized forms is required to maintain intracellular stores of the vitamin in most cells. Since the ubiquitous selenoenzyme thioredoxin reductase can recycle dehydroascorbic acid to ascorbate, we investigated the possibility that the enzyme can also reduce the one-electron-oxidized ascorbyl free radical to ascorbate. Purified rat liver thioredoxin reductase c...

Understanding how pathogenic fungi adapt to host plant cells is of major concern to securing global food production. The hemibiotrophic rice blast fungus Magnaporthe oryzae, cause of the most serious disease of cultivated rice, colonizes leaf cells asymptomatically as a biotroph for 4-5 days in susceptible rice cultivars before entering its destructive necrotrophic phase. During the biotrophic ...

The thioredoxin system is vital in maintaining the cellular redox state and implicated various cancers other diseases. It comprises of reductase, NADPH. Various methods have been developed for detection quantification reductase enzyme. Most these suffer shortfall poor specificity, hence there need to develop more robust specific techniques. Recently, has an increased interest fluorescent probes...