Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
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منابع مشابه
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...
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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...
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Thiol:disulfide oxidoreductases have a CXXC motif within their active sites. To initiate the reduction of a substrate disulfide bond, the thiolate form of the N-terminal cysteine residue (CXXC) of this motif performs a nucleophilic attack. Escherichia coli thioredoxin [Trx (CGPC)] is the best characterized thiol:disulfide oxidoreductase. Previous determinations of the active-site pKa values of ...
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AhpF of Salmonella typhimurium, the flavoprotein reductase required for catalytic turnover of AhpC with hydroperoxide substrates in the alkyl hydroperoxide reductase system, is a 57 kDa protein with homology to thioredoxin reductase (TrR) from Escherichia coli. Like TrR, AhpF employs tightly bound FAD and redox-active disulfide center(s) in catalyzing electron transfer from reduced pyridine nuc...
متن کاملNADPH-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...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2003
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20030093