نتایج جستجو برای: dependent thioredoxin reductase

تعداد نتایج: 728251  

Journal: :Carcinogenesis 1999
H E Ganther

Numerous studies in animal models and more recent studies in humans have demonstrated cancer chemopreventive effects with Se. There is extensive evidence that monomethylated forms of Se are critical metabolites for chemopreventive effects of Se. Induction of apoptosis in transformed cells is an important chemopreventive mechanism. Apoptosis can be triggered by micromolar levels of monomethylate...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1969
O Berglund O Karlström P Reichard

The ribonucleotide reductase system of Escherichia coli B participates in the biosynthesis of DNA by reducing ribonucleoside diphosphates to the corresponding deoxyribonucleotides. The enzyme is regulated in a complicated way by allosteric modifiers. We now find that infection of E. coli with the bacteriophage T4 results in the appearance of a new ribonucleotide reductase system which shows a s...

2001
Arne Holmgren

This reaction in vitro requires the combined function of three pure Escherichia coli proteins, namely the Bl and B2 subunits of ribonucleotide reductase and glutaredoxin. The stoichiometry was demonstrated by determinations of the products r3H]dCDP and GSSG. The standard assay couples oxidation of NADPH to the reduction of GSSG by glutathione reductase. The apparent K,,, value of glutaredoxin w...

2017
Susanna Boronat Alba Domènech Mercè Carmona Sarela García-Santamarina M Carmen Bañó José Ayté Elena Hidalgo

The thioredoxin and glutaredoxin pathways are responsible of recycling several enzymes which undergo intramolecular disulfide bond formation as part of their catalytic cycles such as the peroxide scavengers peroxiredoxins or the enzyme ribonucleotide reductase (RNR). RNR, the rate-limiting enzyme of deoxyribonucleotide synthesis, is an essential enzyme relying on these electron flow cascades fo...

Journal: :The Journal of biological chemistry 2002
Fanis Missirlis Julia K Ulschmid Mitsuko Hirosawa-Takamori Sebastian Grönke Ulrich Schäfer Katja Becker John P Phillips Herbert Jäckle

Defense against oxidative stress in mammals includes the regeneration of the major thiol reductants glutathione and thioredoxin by glutathione reductase and thioredoxin reductase (TrxR), respectively. In contrast, Drosophila, and possibly insects in general, lacks glutathione reductase and must rely solely on the TrxR system. The mammalian TrxRs described so far are selenoproteins that utilize ...

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