1.8.1.9 BrxA bacilliredoxin disulfide + NADPH + H+ - 1.8.1.9 BrxB bacilliredoxin disulfide + NADPH + H+ - 1.8.1.9 BrxC bacilliredoxin disulfide + NADPH + H+ - 1.8.1.9 additional information ribonucleotide reductase, thioredoxin and thioredoxin reductase constitute a system necessary for the biosynthesis of deesoxyribonucleotides 1.8.1.9 additional information HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2 1.8.1.9 additional information EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediates the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo 1.8.1.9 additional information function of TRXR1 in the self-defense mechanism against self-generated oxidative stress 1.8.1.9 additional information homozygous (-/-) knockout of Txnrd1 is embryonically lethal. No major effect of Txnrd1 hemizygosity and/or Se on male fertility and the viability of offspring 1.8.1.9 additional information homozygous (-/-) knockout of Txnrd2 is embryonically lethal. No major effect of Txnrd2 hemizygosity and/or Se on male fertility and the viability of offspring 1.8.1.9 additional information mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity 1.8.1.9 additional information NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxin system is suggested to be important for scavenging H2O2 independent of light-driven generation of reducing equivalents 1.8.1.9 additional information plants of the ntra ntrb knockout mutant are viable and fertile, although with a wrinkled seed phenotype, slower plant growth, and pollen with reduced fitness. Neither cytosolic nor mitochondrial NADPH-dependent thioredoxin reductases are essential in plants 1.8.1.9 additional information the combination of thioredioxin and thioredoxin reductase revives the activity of glutathione reductase from both the cortex and nucleus of aged clear lenses. In cataract lenses (grade II and grade IV) there is a statistically significant recovery of glutathione reductase activity in the cortex, but not in the nucleus 1.8.1.9 additional information the enzyme can promote oxidative stress by redox cycling of paraquat: paraquat + O2 + NADPH + H+ --> paraquat radical + O2- radical + NADP+ 1.8.1.9 additional information thioredoxin reductase is essential for formate dehydrogenase H production and for labelling the formate dehydrogenase H polypeptide with 75Se-selenite 1.8.1.9 additional information thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis 1.8.1.9 additional information NADPH thioredoxin reductase C functions as an electron donor to 2-Cys peroxiredoxin and transfers the reducing power from NADPH to the peroxiredoxin, which reduces peroxides in the cyanobacterium under oxidative stress 1.8.1.9 additional information in addition, the enzyme exhibits NAD(P)H dependent oxidase activity, which generates hydrogen peroxide from molecular oxygen 1.8.1.9 additional information the enzyme cannot use thioredoxin from Spirulina as an electron acceptor 1.8.1.9 additional information the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin 1.8.1.9 additional information Bdr and BrxB function cooperatively to debacillithiolate OhrR 1.8.1.9 NADPH + H+ + ubiquinone-10 HEK cells overexpressing TrxR1 reduce ubiquinone-10 1.8.1.9 oxidized bacillithiol disulfide + NADH + H+ - 1.8.1.9 oxidized bacillithiol disulfide + NADPH + H+ - 1.8.1.9 protein-disulfide + NADPH + H+ the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione 1.8.1.9 thioredoxin + NADP+ - 1.8.1.9 thioredoxin + NADP+ detoxification of hydrogen peroxide, protection of the cell against oxidative damage 1.8.1.9 thioredoxin + NADP+ radical reduction, prevention of cells from UV-generated free radical caused damage on the skin 1.8.1.9 thioredoxin + NADP+ defense against oxidative stress 1.8.1.9 thioredoxin + NADP+ metabolic function of thioredoxin reductase-thioredoxin system: supplies reducing equivalents for a wide variety of acceptors, e.g. : ribonucleotide reductase, nonspecific protein disulfide reductase, methionine sulfoxide reductase, D-proline reductase 1.8.1.9 thioredoxin + NADP+ reduction of free radicals at the surface of the epidermis, enzyme may play a role in physiology of pancreatic beta-cells 1.8.1.9 thioredoxin + NADP+ major anti-oxidant in keratinocytes, melanocytes, melanoma cells 1.8.1.9 thioredoxin + NADP+ the enzyme forms a redox system with protein-disulfide oxidoreductase PhRP (PH0178) 1.8.1.9 thioredoxin 1 + NADP+ TrxR2 prefers its endogenous substrate thioredocin 2 over thioredoxin 1 (10fold), whereas isoform TrxR1 efficiently reduces both thioredoxin 1 and thioredoxin 2 1.8.1.9 thioredoxin 1 + NADP+ + - 1.8.1.9 thioredoxin 2 + NADP+ - 1.8.1.9 thioredoxin 2 + NADP+ TrxR2 prefers its endogenous substrate thioredocin 2 over thioredoxin 1 (10fold), whereas isoform TrxR1 efficiently reduces both thioredoxin 1 and thioredoxin 2 1.8.1.9 thioredoxin 3 + NADP+ - 1.8.1.9 thioredoxin disulfide + H2 - 1.8.1.9 thioredoxin disulfide + NADH + H+ - 1.8.1.9 thioredoxin disulfide + NADPH + H+ - 1.8.1.9 thioredoxin disulfide + NADPH + H+ DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2. This process is consistent with the corresponding redox potentials and is essential for GSSG/GSH cycling in Drosophila melanogaster, which is deficient in glutathione reductase 1.8.1.9 thioredoxin disulfide + NADPH + H+ the tandem system involving thioredoxin reductase and thioredoxin proves to be operative for reducing low molecular weight disulfides, including putative physiological substrates as cystine and oxidized trypanothione 1.8.1.9 thioredoxin disulfide + NADPH + H+ the enzyme (TrxR) can use NADPH to reduce thioredoxin disulfide which passes the reducing equivalent to its downstream substrates involved in various biomedical events, such as ribonucleotide reductase for deoxyribonucleotide and DNA synthesis, or peroxiredoxins for counteracting oxidative stress