1.8.1.9: thioredoxin-disulfide reductase
This is an abbreviated version!
For detailed information about thioredoxin-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.9
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1.8.1.9
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selenium
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selenoproteins
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selenocysteine
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gsh
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peroxiredoxins
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dismutase
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catalase
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auranofin
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glutaredoxins
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trx1
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selenoenzyme
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hydroperoxide
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peroxidases
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fad
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ribonucleotide
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redox-active
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cisplatin
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dithiols
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goldi
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se-deficient
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dtnb
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iodothyronine
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flavoenzyme
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ebselen
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redox-sensitive
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selenium-containing
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selenols
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deiodinases
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thiol-dependent
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organoselenium
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thioredoxin-like
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selenium-deficient
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se-dependent
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n-heterocyclic
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thioredoxin-dependent
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diselenide
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redox-regulated
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selenium-dependent
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thiol-disulfide
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thiol-based
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thioredoxin-1
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ask1
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carbene
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1-chloro-2,4-dinitrobenzene
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sulforaphane
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secis
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txnip
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trypanothione
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medicine
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analysis
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na2seo3
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agriculture
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thioredoxin-interacting
- 1.8.1.9
- selenium
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selenoproteins
- selenocysteine
- gsh
- peroxiredoxins
- dismutase
- catalase
- auranofin
- glutaredoxins
- trx1
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selenoenzyme
- hydroperoxide
- peroxidases
- fad
- ribonucleotide
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redox-active
- cisplatin
- dithiols
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goldi
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se-deficient
- dtnb
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iodothyronine
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flavoenzyme
- ebselen
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redox-sensitive
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selenium-containing
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selenols
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deiodinases
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thiol-dependent
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organoselenium
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thioredoxin-like
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selenium-deficient
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se-dependent
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n-heterocyclic
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thioredoxin-dependent
- diselenide
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redox-regulated
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selenium-dependent
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thiol-disulfide
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thiol-based
- thioredoxin-1
- ask1
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carbene
- 1-chloro-2,4-dinitrobenzene
- sulforaphane
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secis
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txnip
- trypanothione
- medicine
- analysis
- na2seo3
- agriculture
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thioredoxin-interacting
Reaction
Synonyms
all0737, ApTR, At2g41680, AtNTRA, AtNTRB, bacillithiol disulfide reductase, bacillithiol-disulfide reductase, BBOV_I002190, Bdr, BSSB reductase, CeTR2, DmTR, DmTrxR, DmTrxR-1, EC 1.6.4.5, EhTRXR, ferredoxin:thioredoxin reductase, FTR, general stress protein 35, GSP35, HCOI_01258400, hemolysate thioredoxin reductase, hemolysate TR, hTrxR, HvNTR1, HvNTR2, L-TR, L-TrxR, More, MtNTRC, mTR3, multifunctional thioredoxin-glutathione reductase, NAD(P)H:paraquat oxidoreductase, NADP-dependent thioredoxin reductase, NADP-linked thioredoxin reductase, NADP-thioredoxin reductase, NADP-thioredoxin reductase C, NADPH thioredoxin reductase, NADPH thioredoxin reductase C, NADPH-dependent thioredoxin reductase, NADPH-dependent thioredoxin reductase 2, NADPH-dependent thioredoxin reductase C, NADPH-dependent thioredoxin reductase I, NADPH-dependent thioredoxin reductase-1, NADPH-dependent TRX reductase, NADPH-thioredoxin reductase, NADPH-thioredoxin reductase C, NADPH-Trx reductase, NADPH2:oxidized thioredoxin oxidoreductase, NAPDH-dependent BSSB reductase, NTR, Ntr1, NTR2, Ntr3, NTRA, NTRAB, NtrB, NTRC, PH0178, PH1426, PhRP, PhTrxR, protein-disulfide oxidoreductase, reductase, thioredoxin, SEP1, taTrxR, TGR, thioredoxin glutathione reductase, thioredoxin h reductase, thioredoxin reductase, thioredoxin reductase (NADPH), thioredoxin reductase 1, thioredoxin reductase 2, thioredoxin reductase-1, thioredoxin reductase1, TON_1603, TR, TR1, TR2, TR3, TRase, TrR, Trr1, Trr1p, TRR2, Trx1, Trx3, TrxB, TrxB1, TrxB2, TrxR, TrxR-1(cyto), TrxR-1(mito), TrxR1, TrxR2, TrxR3, TrxRB3, TRXRD, TrxRh1, TrxRh2, TrxT, Txnrd1, TXNRD1-v3, Txnrd2, TXNRD3, TxrR-1, YpdA
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General Information on EC 1.8.1.9 - thioredoxin-disulfide reductase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
NTRC can be considered as a TRX that bears its own NTR, which might explain the high catalytic efficiency of the enzyme. The catalytically active form of NTRC is a homodimer arranged in a head-to-tail conformation, which interacts with 2-Cys PRXs through the TRX domain with high affinity for NADPH
drug target
anti-cancer target. Selenocysteine is important for the biological functions of mammalian TrxR and distinguishes it from prokaryotic thioredoxin reductases. Therefore it is a promising drug target
drug target
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drug-resistant Staphylococcus aureus, especially methicillin-resistant (MRSA) and vancomycin-resistant Staphylococcus aureus (VRSA), pose a great threat to human health globally. The Trx system in GSH-deficient pathogens is a viable antibacterial drug target
drug target
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ebselen as an inhibitor of thiol-dependent enzymes in pathogens
drug target
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drug-resistant Staphylococcus aureus, especially methicillin-resistant (MRSA) and vancomycin-resistant Staphylococcus aureus (VRSA), pose a great threat to human health globally. The Trx system in GSH-deficient pathogens is a viable antibacterial drug target
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evolution
based on sequence analysis, YpdA belongs to the pyridine nucleotide-disulfide oxidoreductase family of proteins that use flavin adenine dinucleotide (FAD) to transport reducing equivalents from NAD(P)H to cysteine residues
evolution
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based on sequence analysis, YpdA belongs to the pyridine nucleotide-disulfide oxidoreductase family of proteins that use flavin adenine dinucleotide (FAD) to transport reducing equivalents from NAD(P)H to cysteine residues
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evolution
Staphylococcus aureus PS 47
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based on sequence analysis, YpdA belongs to the pyridine nucleotide-disulfide oxidoreductase family of proteins that use flavin adenine dinucleotide (FAD) to transport reducing equivalents from NAD(P)H to cysteine residues
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malfunction
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ablation of cytosolic thioredoxin reductase (Txnrd1) or mitochondrial thioredoxin reductase (Txnrd2) yields embryonic lethal phenotypes
malfunction
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cells deficient in isoformTR1 are particularly sensitive to diamide, while isoform TR3-knockdown cells are more sensitive to hydrogen peroxide
malfunction
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in the absence of NTRC, imbalanced metabolic activities presumably modulate the chloroplast retrograde signals, leading to altered expression of nuclear genes and, ultimately, to the formation of the pleiotrophic phenotypes in ntrc mutant plants
malfunction
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inhibition of mitochondrial thioredoxin reductase leads to oxidation of downstream enzymes such as thioredoxin and peroxiredoxin
malfunction
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reporter gene transactivation by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. Decreased reporter gene activity in thioredoxin reductase null cells is due to reduced p53 specific activity rather than reduced p53 protein levels
malfunction
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stable knockdown of TxnRd1 in both HeLa and FaDu cells nearly abolishes curcumin-mediated radiosensitization. TxnRd1 knockdown cells show decreased radiation-induced reactive oxygen species and sustained extracellular signal-regulated kinase 1/2 activation
malfunction
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Txnrd1 knock-out cells cannot be rescued from glutathione depletion-induced cell death either by antioxidants, xCT overexpression, or co-culturing with xCT-overexpressing cells that condition the medium with Cys
malfunction
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combined deficiencies of three thioredoxin m isoforms and NADPH-dependent thioredoxin reductase C (NTRC) leads to a cumulative decrease in leaf pigmentation, tetrapyrrole biosynthesis intermediate contents, 5-aminolevulinic acid synthesis rate, and Mg-protoporphyrin IX methyltransferase activity
malfunction
in plants with altered content of the NADPH-dependent chloroplast thioredoxin system, the strict correlation between lumenal pH and non-photochemical quenching is partially lost
malfunction
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the disruption of the gene ntrC triggers a global change in the cellular physiology of A.7120 involving fluctuations in the proteome, metabolome and activities of antioxidant enzymes. However, the lack of NTRC does not drastically alter viability
malfunction
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TRR1 deletion causes sensitivity to the inhibitors of the TORC1 pathway, such as rapamycin. This correlates with low Tor2p kinase levels and indicates a direct role of Trr1p in its stability. The autophagy caused by nitrogen starvation is reduced in the trr1DELTA mutant
malfunction
truncated polypeptides containing either the NTR or the TRX domain of NTRC showed that this novel enzyme could display both activities. Overexpression of 2-Cys PRXs, which has no significant effect in wild-type plants, resultes in further growth impairment in the ntrc mutant background (lacking individual TRXs), showing that the severity of the ntrc phenotype depends on 2-Cys PRXs levels. Very severe growth inhibition phenotypes of mutants combining the deficiencies of NTRC and TRXs f or x are also rescued by decreasing the contents of 2-Cys PRXs
malfunction
Trxrd2-/- cells are more susceptible to glutathione depletion. Loss of Trxrd2 results in enhanced peroxynitrite steady-state levels in both vascular endothelial cells and vessels
malfunction
YpdA overexpression confers greater resistance to stress. The YpdA G10A mutant protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium. Decreased fitness of the ypdA mutant results in reduced survival in neutrophils (PMNs). The ypdA mutant survives less well than the parent and the complemented mutant. The survival of SH1000 (BSH null strain), akin to the ypdA mutant, is also less than the parent and complemented mutant in this assay
malfunction
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YpdA overexpression confers greater resistance to stress. The YpdA G10A mutant protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium. Decreased fitness of the ypdA mutant results in reduced survival in neutrophils (PMNs). The ypdA mutant survives less well than the parent and the complemented mutant. The survival of SH1000 (BSH null strain), akin to the ypdA mutant, is also less than the parent and complemented mutant in this assay
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malfunction
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in the absence of NTRC, imbalanced metabolic activities presumably modulate the chloroplast retrograde signals, leading to altered expression of nuclear genes and, ultimately, to the formation of the pleiotrophic phenotypes in ntrc mutant plants
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malfunction
Staphylococcus aureus PS 47
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YpdA overexpression confers greater resistance to stress. The YpdA G10A mutant protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium. Decreased fitness of the ypdA mutant results in reduced survival in neutrophils (PMNs). The ypdA mutant survives less well than the parent and the complemented mutant. The survival of SH1000 (BSH null strain), akin to the ypdA mutant, is also less than the parent and complemented mutant in this assay
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malfunction
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reporter gene transactivation by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. Decreased reporter gene activity in thioredoxin reductase null cells is due to reduced p53 specific activity rather than reduced p53 protein levels
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metabolism
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the TrxR/thioredoxin pathway is of central importance in limiting cellular reactive oxygen species
metabolism
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
metabolism
Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. Bdr additionally functions as a bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. The BSH redox network comprised of three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. BrxC (YtxJ) is a monothiol bacilliredoxin and Bdr is bacilliredoxin reductase. DNA-binding transcription factor OhrR is inactivated by S-bacillithiolation. BrxB can regenerate active OhrR, with generation of BrxB-SSB. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. Following their inactivation, S-bacillithiolated OhrR (OhrR-SSB) and MetE (MetE-SSB) can be reduced by two bacilliredoxin (Brx) proteins, BrxA and BrxB. The enzyme is part of the BSH redox network comprising three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. Both BrxA and BrxB are dithiol class enzymes and are detected in vivo in their S-bacillithiolated forms after oxidative stress
metabolism
regulation of enzyme activity based on thiol-disulfide exchange is a regulatory mechanism in which the protein disulfide reductase activity of thioredoxins (TRXs) plays a central role. Plant chloroplasts are equipped with a complex set of up to 20 TRXs and TRX-like proteins, the activity of which is supported by reducing power provided by photosynthetically reduced ferredoxin (FDX) with the participation of a FDX-dependent TRX reductase (FTR). Therefore, the FDX-FTR-TRXs pathway allows the regulation of redox-sensitive chloroplast enzymes in response to light. In addition, chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. The NTRC gene encodes a polypeptide containing both NTR and TRX domains. NTRC is unique to oxygenic photosynthetic organisms. Both redox systems, NTRC and FDX-FTR-TRXs, participate in fine-tuning chloroplast performance in response to changes in light intensity. Participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase, in the control of the reducing activity of chloroplast TRXs as well as in the rapid oxidation of stromal enzymes upon darkness. Analysis of relationship of 2-Cys PRXs with NTRC and the FDX-FTR-TRXs redox systems for fine-tuning chloroplast performance in response to changes in light intensity and darkness, overview. The activity of thiol-dependent peroxidases (TPXs) relies on the disulfide reductase activity of NTRC, TRXs, and glutaredoxins (GRXs)
metabolism
the TrxR/Pdo redox cascade can use H2 as the electron donor when the frhAGB-encoded hydrogenase mediates electron transfer. When FrhAGB is replaced with FrhAG, it also catalyzes the reduction of Pdo with slightly weaker activity. The specific activity of the FrhAG hydrogenase is 40% lower than that of the FrhAGB hydrogenase
metabolism
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Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. Bdr additionally functions as a bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. The BSH redox network comprised of three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. BrxC (YtxJ) is a monothiol bacilliredoxin and Bdr is bacilliredoxin reductase. DNA-binding transcription factor OhrR is inactivated by S-bacillithiolation. BrxB can regenerate active OhrR, with generation of BrxB-SSB. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. Following their inactivation, S-bacillithiolated OhrR (OhrR-SSB) and MetE (MetE-SSB) can be reduced by two bacilliredoxin (Brx) proteins, BrxA and BrxB. The enzyme is part of the BSH redox network comprising three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. Both BrxA and BrxB are dithiol class enzymes and are detected in vivo in their S-bacillithiolated forms after oxidative stress
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metabolism
Pyrococcus furiosus OT-3
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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
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physiological function
Thermosynechococcus vestitus
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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
physiological function
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NTRC is the most important pathway for chloroplast 2-Cys peroxiredoxins reduction, probably the only one during the night
physiological function
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transcriptional activation of aniA and norB under microaerobic conditions is dependent on thioredoxin reductase, TrxB plays an important role in promoting the survival of gonococci during cervical infection
physiological function
Txnrd1 gene is essential for normal development during embryogenesis
physiological function
Txnrd2 gene is essential for normal development during embryogenesis
physiological function
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glutathione deficiency can be rescued by forced expression of xCT (the substrate-specific subunit of the cystine/glutamate antiporter), which additionally requires the presence of functional isoform Txnrd1, but not isoform Txnrd2
physiological function
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isoform Txnrd1 but not Txnrd2 is required for cerebellar development
physiological function
NTRC is maintained at a constant level during hardening and functions as an antioxidant with 2-Cys peroxiredoxin in the acquisition of freezing tolerance of Chlorella
physiological function
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NTRC regulates several key processes, including chlorophyll biosynthesis and the shikimate pathway, in chloroplasts. NTRC has a critical role in the regulation of photoperiod-dependent metabolic and developmental processes in Arabidopsis
physiological function
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the thioredoxin reductase-1 splice variant TXNRD1_v3 is an atypical inducer of cytoplasmic filaments and cell membrane filopodia. The glutaredoxin domain of TXNRD1_v3 is an atypical regulator of the cell cytoskeleton that potently induces formation of highly ordered cytoplasmic filaments and cell membrane filopodia
physiological function
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the thioredoxin system has a large number of functions in DNA synthesis, defense against oxidative stress and apoptosis or redox signaling with reference to many diseases
physiological function
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the thioredoxin system, comprising thioredoxin, thioredoxin reductase, and NADPH, is critical for cellular stress response, protein repair, and protection against oxidative damage
physiological function
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the thioredoxin system, comprising thioredoxin, thioredoxin reductase, and NADPH, is critical for cellular stress response, protein repair, and protection against oxidative damage
physiological function
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thioredoxin reductase 1 overexpression upregulates monocyte chemoattractant protein-1 release in human endothelial cells by 34%. TrxR1 enhances reactive oxygen species generation, NF-kappaB activity and subsequent monocyte chemoattractant protein-1 expression in endothelial cells, and may promote rather than prevent vascular endothelium from forming atherosclerotic plaque
physiological function
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thioredoxin reductase-1 mediates curcumin-induced radiosensitization of squamous carcinoma cells. Overexpressing catalytically active TxnRd1 in HEK-293 cells, with low basal levels of TxnRd1, increases their sensitivity to curcumin alone and to the combination of curcumin and ionizing radiation
physiological function
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Trr2/Trx3 and Trr2/GSH systems exhibit similar capacities for supporting peroxidredoxin 1 catalysis. TRR2 is required for cadmium and hydrogen peroxide resistance promoted by overexpression of peroxiredoxin 1
physiological function
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TrxR helps maintenance of redox homeostasis in Plasmodium infection. TrxR is essential for the survival of erythrocytic stages of parasites
physiological function
TrxR1 plays a key role in protection against oxidant stress
physiological function
a double knockout mutant lacking NtrC and sulfiredoxin shows a phenotype similar to the NtrC mutant, while the sulfiredoxin mutant resembles wild-type plants. The deficiency of NtrC causes reduced overoxidation of 2-Cys peroxiredoxins, whereas the deficiency of sulfiredoxin has the opposite effect. The disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation. The overoxidation of chloroplast 2-Cys peroxiredoxins shows no circadian oscillation. The low level of 2-Cys peroxiredoxin overoxidation in the NtrC mutant is light dependent
physiological function
a knockout mutant strain displays higher level of reactive oxygen species in normal growth conditions. Oxidative stress treatments such as hydrogen peroxide, methyl-viologen or high light irradiance lead to an increase in the expression of genes related to reactive oxygen species detoxification, including NtrC and peroxiredoxin genes, with a concomitant increase in the amount of NtrC and 2-Cys peroxiredoxin. The mutant shows a pronounced overoxidation of 2-Cys peroxiredoxin and a time-delay recovery of its reduced form upon oxidative stress treatments
physiological function
Arabidopsis thaliana NtrC knockout mutants show lower magnesium protoporphyrin IX and magnesium protoporphyrin IX monomethylester steady-state levels, the substrate and the product of protoporphyrin IX methyltransferase CHLM preceding MgPMME cyclase, while protoporphyrin IX strongly accumulates in mutant leaves after 5-aminolevulinic acid feeding. The mutant has a reduced capacity to synthesize 5-aminolevulinic acid and reduced CHLM activity compared with the wild-type. The contents of glutamyl-transfer RNA reductase1 and CHLM are reduced. NtrC physically interacts with glutamyl-transfer RNA reductase1 and CHLM. NtrC mutant plants contain partly oxidized CHLM, the wild-type has only reduced CHLM
physiological function
Arabidopsis thaliana plants lacking NtrC tolerate high light intensities, display drastically elevated non-photochemical quenching component qE, have larger trans-thylakoid pH differences and have 10fold higher zeaxanthin levels under low and medium light intensities. A double-knockout mutant, lacking additionally photosystem II component PsbS, is devoid of qE. This double mutant grows faster than the NtrC mutant and has a higher chlorophyll content. The photosystem II activity is partially restored, and linear electron transport rates under low and medium light intensities are twice as high as compared with plants lacking NtrC alone
physiological function
growth rate of isoform Ntr1 mutants is significantly lower than that of control cells
physiological function
growth rate of isoform Ntr2 mutants is significantly lower than that of control cells
physiological function
HepG2 cells utilize cytosolic thioredoxin reductase TrxR1 and thioredoxin to defend against the high glucose/palmitate-mediated increase in reactive oxygen species. Enhanced TrxR1/thioredoxin palmitoylation occurs in parallel with a decrease in their activities
physiological function
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loss of glutathione reductase, thioredoxin reductase and thioredoxin peroxidase-encoding genes results in strains severely attenuated in their ability to grow in rice cells and that fail to produce spreading necrotic lesions on the leaf surface. The thioredoxin proteins contribute to cell-wall integrity. Glutathione and thioredoxin gene expression, under axenic growth conditions, is dependent on both the presence of glucose and the sugar/NADPH sensor Tps1
physiological function
mutants lacking both NtrC and thioredoxin Trxs f, which participate in metabolic redox regulation, or, to a lower extent Trx x, which has antioxidant function, show severe growth-retarded phenotypes, decreased photosynthesis performance, and almost abolished light-dependent reduction of fructose-1,6-bisphosphatase. The combined deficiency of both redox systems provokes aberrant chloroplast ultrastructure. Both the NtrC-Trx f1f2 and NtrC-trx x mutants show high mortality at the seedling stage, which is overcome by the addition of an exogenous carbon source
physiological function
overexpression of isoform NTRC in Arabidopsis thaliana leads to a freezing and cold stress tolerance, whereas a knockout mutant shows a stress-sensitive phenotype. The recombinant NTRC proteins exhibits a cryoprotective activity for malate dehydrogenase and lactic dehydrogenase. Recombinant NTRC efficiently protect RNA and DNA from RNase A and metal catalyzed oxidation damage, respectively. The C-terminal thioredoxin domain is required for the nucleic acid-protein complex formation
physiological function
overexpression wild-type NtrC promotes plant growth by increasing leaf size and biomass yield of the rosettes. Complementation of the mutant with the full-length NtrC gene containing an active reductase but an inactive Trx domain, or vice versa, recovers wild-type chloroplast phenotype and, partly, rosette biomass production
physiological function
plants lacking functional NtrC show localized cell death accompanied by elevated accumulation of hydrogen peroxide in response to Pseudomonas syringae pathogens. The NtrC mutant shows enhanced bacterial growth and disease susceptibility of pathogens and elevated jasmonic acid-mediated signaling pathways in response to Pseudomonas syringae pathogens
physiological function
the enhanced NtrC transcript expression upon methyl viologen treamtment confers oxidative stress tolerance. Overexpressing plants show extreme drought tolerance with lower water loss compared to wild-type and NtrC mutant strains. Drought-responsive genes such as RD29A and DREB2A are enhanced in overexpressing strains by drought, compared to wild-type and NtrC mutant strains
physiological function
the NtrC-dependent redox regulation of CHLI-1 ATPase contributes to the chlorophyll-deficient phenotype of NtrC mutants
physiological function
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the thioredoxin system plays a major role in releasing the L chain of tetanus neurotoxin and botulinum neurotoxins after their translocation across the membrane of the endocytic vesicle
physiological function
Trx1 shows reversible association with tissue factor in human serum and plasma samples. The association is dependent on Trx1 residue Cys73 that bridges tissue factor residue Cys209 via a disulfide bond. Trx1 Cys73 is absolutely required for Trx1 to interfere with factor FVIIa binding to purified and cell-surface tissue factor, consequently suppressing tissue factor-dependent procoagulant activity and proteinase-activated receptor-2 activation. Trx1/TrxR plays an important role in sensing the alterations of NADPH/NADP+ states and transducing this redox-sensitive signal into changes in tissue factor activity. With NADPH, Trx1/TrxR facilitates the reduction of tissue factor, causing a decrease in tissue factor activity, with NADP+, Trx1/TrxR promotes the oxidation of tissue factor, leading to an increase in its activity
physiological function
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under cadmium stress conditions, NTR activity and thioredoxin h3 and thioredoxin h4 expression are stimulated, while the overall activity of thioredoxin decreases. When incubated with Cd ions in vitro, the disulfide reductase activity of thioredoxin h3 and f isoforms is drastically inhibited. The NADPH status is also affected, since cadmium treatment provokes an increase in oxidized state of coenzyme as compared to control redox ratio
physiological function
Bdr (YpdA) functions as an NADPH-dependent bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue
physiological function
chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. Redox regulation is an additional layer of control of the signaling function of the chloroplast. Redox regulation based on dithiol-disulfide interchange constitutes an essential regulatory mechanism that allows the rapid adaptation of chloroplast metabolism to light
physiological function
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cytosolic thioredoxin reductase 1 is required for correct folding of proteins entering the endoplasmic reticulum, in the reconstituted translation/translocation system as well as in intact cells grown in culture
physiological function
enzyme YpdA participates in stress response upon exposure to specific physiologically relevant stresses. Role of YpdA in regulating BSH and BSSB levels, the enzyme is responsible for the recycling of oxidized bacillithiol disulfide (BSSB) to the reduced form (BSH). Enzyme YpdA plays in protecting Staphylococcus aureus cells from the oxidative killing by human neutrophils (PMNs)
physiological function
redox regulation in heterotrophic organisms relies on NADPH, thioredoxins, and an NADPH-dependent TRX reductase (NTR). NTRC-dependent regulation of 2-Cys peroxiredoxin (PRX) is critical for optimal function of the photosynthetic apparatus
physiological function
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role of the enzyme (NTRC) in the regulation of the NADPH pool. Biological significance of NTRC in oxidative stress management. NTRC is not involved in the membrane organization process
physiological function
the enzyme (NTRC) plays a crucial role in the activation of the NDH-dependent electron flow in darkness (chlororespiration) and during dark to light transitions. The enzyme stimulates the activity of NDH-dependent cyclic electron flow and is involved in the regulation of generation of proton motive force, thylakoid conductivity to protons, and redox balance between the thylakoid electron transfer chain and the stroma during changes in light conditions
physiological function
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
physiological function
the mitochondrial thioredoxin/peroxiredoxin system encompasses NADPH, thioredoxin reductase 2 (TrxR2), thioredoxin 2, and peroxiredoxins 3 and 5 (Prx3 and Prx5) and is crucial to regulate cell redox homeostasis via the efficient catabolism of peroxides. Endothelial TrxR2 controls both the steady-state concentration of peroxynitrite, the product of the reaction of superoxide radical and nitric oxide, and the integrity of the vascular system
physiological function
the NADPH-dependent chloroplast thioredoxin system (NTRC) contributes to downregulation of a slow-relaxing constituent of NPQ, whose induction is independent of lumenal acidification. Overexpression of NTRC enhances the ability to adjust the excitation balance between photosystem II (PSII) and photosystem I (PSI), and improves the ability to oxidize the electron transfer chain during changes in light conditions
physiological function
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the thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. This reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system
physiological function
thioredoxin reductase system provides the minimal cytosolic components required for reducing proteins within the ER lumen
physiological function
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thioredoxin reductase Trr1p controls TORC1-regulated processes. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation
physiological function
TrxR from the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H. In Thermococcus onnurineus NA1, the frhAGB-encoded hydrogenase, a homologue of the F420-reducing hydrogenase of methanogens, interacts with thioredoxin reductase (TrxR). Electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to TrxR and reduced Pdo (protein disulfide oxidoreductase, UniProt ID B6YTB7), a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR is 7fold less efficient than when NADPH is the electron donor. TrxR can use H2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NADPH in Thermococcus onnurineus strain NA. The frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologue, F420-reducing hydrogenases of methanogens. The TrxR (TON_1603) of the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is a typical prokaryotic NADP-dependent thioredoxin reductase (NTR) with a preference for NADPH over NADH. The TrxR/Pdo redox couple is capable of reducing cystine to cysteine, which subsequently reduced dimethyl sulfoxide (DMSO) to dimethylsulfide (DMS). Because growth is enhanced by substituting DMSO for elemental sulfur (S0) as an electron sink for excess reducing power
physiological function
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transcriptional activation of aniA and norB under microaerobic conditions is dependent on thioredoxin reductase, TrxB plays an important role in promoting the survival of gonococci during cervical infection
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physiological function
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enzyme YpdA participates in stress response upon exposure to specific physiologically relevant stresses. Role of YpdA in regulating BSH and BSSB levels, the enzyme is responsible for the recycling of oxidized bacillithiol disulfide (BSSB) to the reduced form (BSH). Enzyme YpdA plays in protecting Staphylococcus aureus cells from the oxidative killing by human neutrophils (PMNs)
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physiological function
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Bdr (YpdA) functions as an NADPH-dependent bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue
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physiological function
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NTRC regulates several key processes, including chlorophyll biosynthesis and the shikimate pathway, in chloroplasts. NTRC has a critical role in the regulation of photoperiod-dependent metabolic and developmental processes in Arabidopsis
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physiological function
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the thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. This reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system
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physiological function
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NTRC is maintained at a constant level during hardening and functions as an antioxidant with 2-Cys peroxiredoxin in the acquisition of freezing tolerance of Chlorella
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physiological function
Staphylococcus aureus PS 47
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enzyme YpdA participates in stress response upon exposure to specific physiologically relevant stresses. Role of YpdA in regulating BSH and BSSB levels, the enzyme is responsible for the recycling of oxidized bacillithiol disulfide (BSSB) to the reduced form (BSH). Enzyme YpdA plays in protecting Staphylococcus aureus cells from the oxidative killing by human neutrophils (PMNs)
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