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Information on EC 1.8.1.9 - thioredoxin-disulfide reductase and Organism(s) Mus musculus and UniProt Accession Q9JMH6
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1.8.1.9 thioredoxin-disulfide reductaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.8.1.9
- selenium
-
selenoproteins
- selenocysteine
- gsh
- peroxiredoxins
- dismutase
- catalase
- auranofin
- glutaredoxins
- trx1
-
selenoenzyme
- hydroperoxide
- peroxidases
- fad
- ribonucleotide
-
redox-active
- cisplatin
- dithiols
-
goldi
-
se-deficient
- dtnb
-
iodothyronine
-
flavoenzyme
- ebselen
-
redox-sensitive
-
selenium-containing
-
selenols
-
deiodinases
-
thiol-dependent
-
organoselenium
-
thioredoxin-like
-
selenium-deficient
-
se-dependent
-
n-heterocyclic
-
thioredoxin-dependent
- diselenide
-
redox-regulated
-
selenium-dependent
-
thiol-disulfide
-
thiol-based
- thioredoxin-1
- ask1
-
carbene
- 1-chloro-2,4-dinitrobenzene
- sulforaphane
-
secis
-
txnip
- trypanothione
- medicine
- analysis
- na2seo3
- agriculture
-
thioredoxin-interacting
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
thioredoxin reductase, trxr, trxr1, txnrd1, thioredoxin reductase 1, trxr2, txnrd2, thioredoxin reductase-1, thioredoxin reductase 2, nadph-dependent thioredoxin reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Txnrd1
general stress protein 35
-
-
-
-
GSP35
-
-
-
-
NADP-thioredoxin reductase
-
-
-
-
NADPH-thioredoxin reductase
-
-
-
-
NADPH2:oxidized thioredoxin oxidoreductase
-
-
-
-
reductase, thioredoxin
-
-
-
-
thioredoxin reductase
thioredoxin reductase (NADPH)
-
-
-
-
TR
TR1
TR3
TrxR
TrxR2
Txnrd2
thioredoxin reductase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
additional information
-
the enzyme utilizes oxygen, requires NADH or NADPH, and readily generates the reduced paraquat radical
SYSTEMATIC NAME
IUBMB Comments
thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9074-14-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(2-amino-2-oxoethyl)carbamoyl]-6-oxo-1,2,5-dithiazocan-7-] + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-L-cysteinylglycinamide + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(2-amino-2-oxoethyl)carbamoyl]-6-oxo-1,2,5-thiaselenazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-3-selanyl-L-alanylglycinamide + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(carboxymethyl)carbamoyl]-6-oxo-1,2,5-dithiazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-L-cysteinylglycine + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(carboxymethyl)carbamoyl]-6-oxo-1,2,5-thiaselenazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-3-selanyl-L-alanylglycine + NADP+
-
-
-
-
?
Pro-Thr-Val-Thr-Gly-Cys-S-S-Cys-Gly + NADPH + H+
Pro-Thr-Val-Thr-Gly-Cys + Cys-Gly + NADP+
-
-
-
-
?
Pro-Thr-Val-Thr-Gly-Cys-S-S-selenoCys-Gly + NADPH + H+
Pro-Thr-Val-Thr-Gly-Cys + selenoCys-Gly + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
C-terminal tetrapeptide sequences is Gly-Cys-Sec-Gly. Changing the C-terminal carboxylate of mTR3 to a carboxamide increases the activity of the enzyme. If the selenium content is normalized for both samples, the carboxamide mutant has nearly twice the activity as the semisynthetic wild-type carboxylate enzyme
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
reduction of free radicals at the surface of the epidermis, enzyme may play a role in physiology of pancreatic beta-cells
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
C-terminal tetrapeptide sequences is Gly-Cys-Sec-Gly. Changing the C-terminal carboxylate of mTR3 to a carboxamide increases the activity of the enzyme. If the selenium content is normalized for both samples, the carboxamide mutant has nearly twice the activity as the semisynthetic wild-type carboxylate enzyme
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
TR3 does not have catalytic preferences for mitochondrial thioredoxin versus cytosolic thioredoxin
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme can promote oxidative stress by redox cycling of paraquat: paraquat + O2 + NADPH + H+ --> paraquat radical + O2- radical + NADP+
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
reduction of free radicals at the surface of the epidermis, enzyme may play a role in physiology of pancreatic beta-cells
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme can promote oxidative stress by redox cycling of paraquat: paraquat + O2 + NADPH + H+ --> paraquat radical + O2- radical + NADP+
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
-
NADPH
-
approximately four times more activity was evident with NADPH when compared to NADH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Na2SeO3
enhances hepatic TrxR1 activity, but only on the condition that it causes liver injury
selenium
selenium
additional information
selenium
selenoprotein, expression and function depends on adequate supply of selenium
selenium
selenoprotein, expression and function depends on adequate supply of selenium
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
-
the enzyme possesses selenium in the form of selenocysteine in the active site
additional information
DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
-
DmTR shows high catalytic activity without the presence of a selenocysteine
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calveolin
-
overexpression of caveolin 1 inhibits TrxR activity by about 50% whereas a lack of caveolin 1 activates TrxR, both in vitro and in vivo
-
cyclophosphamide
-
250 mg/kg reduces activity reversibly to 25% at 3h after treatment
ifosfamide
-
inhibition of thioredoxin reductase activity in malignant cells by ifosfamide is highly associated with its anticancer effect and the mechanism of ifosfamide systemic toxicity may be related to multi-organ inhibition of thioredoxin reductase activity
methylmercury
-
a single administration of methylmercury (1, 5, and 10 mg/kg) causes a marked inhibition of kidney TrxR activity, while significant inhibition is observed in the liver 24 h after exposure to 5 and 10 mg/kg. In the brain, methylmercury does not inhibit TrxR activity. Methylmercury can bind to selenocysteine residues present in the catalytic site of TrxR, in turn causing enzyme inhibition that can compromise the redox state of cells
cisplatin
-
at pharmacological doses inhibits TrxR activity in both ascitic hepatoma 22 cells and kidney, leading to suppression of H22 cells proliferation along with nephrotoxicity. Amifostine, a clinical used cytoprotective agent, protected against CDDP-induced TrxR inactivation in kidney but not in H22 cells
cisplatin
-
heat shock protein 27 protects L929 cells from cisplatin-induced apoptosis by enhancing Akt activation and abating suppression of thioredoxin reductase activity
additional information
-
the enzyme is not inhibited by dimedone even at 150fold excess
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
if the concentration of EDTA in the reaction mixture is higher than 0.1 mM the enzyme shows full activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
0.47
5,5'-dithiobis(2-nitrobenzoic acid)
full-length mouse enzyme with C-terminal sequence GCUG
0.83
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
2.72
5,5'-dithiobis(2-nitrobenzoic acid)
truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid
0.032
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence SCCS
0.0676
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCUG
0.123
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCCG
additional information
additional information
-
effects of paraquat on reaction kinetics of NADH and NADPH in lung cell extracts
-
additional information
additional information
KM-values of semisynthetic truncated mTR3 enzymes
-
additional information
additional information
-
KM-values of semisynthetic truncated mTR3 enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.6
5,5'-dithiobis(2-nitrobenzoic acid)
truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid
20.83
5,5'-dithiobis(2-nitrobenzoic acid)
full-length mouse enzyme with C-terminal sequence GCUG
20.85
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
48.42
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
1.183
hydrogen peroxide
semisynthetic enzyme with 91% content of selenium
0.083
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence SCCS
0.13
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCCG
37
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCUG
additional information
additional information
turnover number of semisynthetic truncated mTR3 enzymes
-
additional information
additional information
-
turnover number of semisynthetic truncated mTR3 enzymes
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45.33
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
58.33
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000171
methylmercury
Mus musculus
-
TrxR from liver, pH and temperature not specified in the publication
0.000078
methylmercury
Mus musculus
-
TrxR from kidney, pH and temperature not specified in the publication
0.000158
methylmercury
Mus musculus
-
TrxR from brain, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
the truncated enzyme shows a pH optimum for the reduction of 5,5'-dithiobis(2-nitrobenzoic acid) at pH 6.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
pH 6.5: about 40% of maximal activity, pH 9.0: about 50% of maximal activity, wild-type enzyme
6.5 - 9.5
pH 6.5: 45% of maximal activity, pH 9.5: about 50% of maximal activity, mutant enzyme Sec489C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Bach1 repression of ferritin and thioredoxin reductase1 is heme-sensitive in cells and in vitro and coordinates expression with heme oxygenase1, beta-globin, and NADP(H) quinone (oxido) reductase1
mice lacking Txnrd1 in the nervous system are significantly smaller and display ataxia and tremor. A strikingly patterned cerebellar hypoplasia is observed. Proliferation of the external granular layer is strongly reduced and fissure formation and laminar organisation of the cerebellar cortex is impaired in the rostral portion of the cerebellum. Purkinje cells are ectopically located and their dendrites stunted. The Bergmann glial network is disorganized and shows a pronounced reduction in fiber strength. Neuron-specific inactivation of Txnrd1 does not result in cerebellar hypoplasia, suggesting a vital role for Txnrd1 in Bergmann glia or neuronal precursor cells
TR1 is uniquely overexpressed in cancer cells and its knockdown in a mouse cancer cell line driven by oncogenic k-ras results in orphological changes characteristic of parental (normal) cells, without significant effect on cell growth under normal growth conditions. When grown in serum-deficient medium, TR1 deficient cancer cells lose self-sufficiency of growth, manifest a defective progression in their S phase and a decreased expression of DNA polymerase alpha
development and differentiation of the cells from transgenic mice lacking Txnrd2 expression is not significantly impaired
nervous system-specific Txnrd2 null mice develop normally
development and differentiation of the cells from transgenic mice lacking Txnrd2 expression is not significantly impaired
mouse embryos homozygous for a targeted null mutation of the txnrd1 gene, encoding the cytosolic thioredoxin reductase, are viable at embryonic day 8.5 (E8.5) but not at E9.5. Txnrd1 is required for correct patterning of the early embryo and progression to later development
-
prolonged selenium-deficient diet in MsrA knockout mice lowers thioredoxin reductase activity
-
thioredoxin reductase activity is significantly increased by Picual extra virgin olive oil, but not by Arbequina extra virgin olive oil as compared with palm oil intervention
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
there is a higher nuclear expression of thioredoxin reductase 1 in proliferating cells than in nonproliferating cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Txnrd1 gene is essential for normal development during embryogenesis
malfunction
physiological function
malfunction
-
ablation of cytosolic thioredoxin reductase (Txnrd1) or mitochondrial thioredoxin reductase (Txnrd2) yields embryonic lethal phenotypes
malfunction
-
cells deficient in isoformTR1 are particularly sensitive to diamide, while isoform TR3-knockdown cells are more sensitive to hydrogen peroxide
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
physiological function
Txnrd2 gene is essential for normal development during embryogenesis
physiological function
-
isoform Txnrd1 but not Txnrd2 is required for cerebellar development
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TRXR1_MOUSE
613
0
67084
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
U489C
barely detectable activity towards thioredoxin and hydrogen peroxide
additional information
additional information
the mutant in the which Sec and Cys residues are switched (TR-GUCG), shows activity similar to that of the Sec489Cys mutant (TR-GCCG). Replacement of the Cys-Sec dyad with a Sec-Sec dyad (TR-GUUG) results in a mutant enzyme with very low catalytic activity. Even if the kcat values are normalized for selenium content, the TR-GUCG and TR-GUUG mutants have catalytic activity 90fold and 185fold lower, respectively, than that of the wild-type enzyme. The mutants in which alanine residues are inserted to increase the ring size (TR-GCAUG and TR-GCAAUG) show only a modest decrease in catalytic activity, 6fold and 4fold, respectively
additional information
-
the mutant in the which Sec and Cys residues are switched (TR-GUCG), shows activity similar to that of the Sec489Cys mutant (TR-GCCG). Replacement of the Cys-Sec dyad with a Sec-Sec dyad (TR-GUUG) results in a mutant enzyme with very low catalytic activity. Even if the kcat values are normalized for selenium content, the TR-GUCG and TR-GUUG mutants have catalytic activity 90fold and 185fold lower, respectively, than that of the wild-type enzyme. The mutants in which alanine residues are inserted to increase the ring size (TR-GCAUG and TR-GCAAUG) show only a modest decrease in catalytic activity, 6fold and 4fold, respectively
additional information
the truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
-
the truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2',5'-ADP-agarose affinity chromatography and Superose size exclusion chromatography
-
chitin resin column chromatography and DEAE anion exchange column chromatography
DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography
-
HisBind HiTrap metal-affinity column chromatography, 2',5'-ADP-Sepharose column chromatography, and CNBr-activated Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli ER2566 cells
the full-length Sec489Cys mutant as well as the truncated mTR3 missing the C-terminal CUG tripeptide sequence is expressed as a TR-intein-chitin binding domain fusion protein in Escherichia coli
truncated form of thioredoxin reductase (missing the C-terminal eight amino acids-TRtrunc), is produced by amplifying the coding region
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
TR1 acts largely as a pro-cancer protein and it is a primary target in cancer therapy
medicine
-
both pharmacological and toxicological effects of anti-cancer drug cisplatin involve TrxR inactivation, and the large enhancement on cisplatin cure rate in H22 ascites model by using amifostine is, at least in part, ascribed to its selective modulation on TrxR
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grankvist, K.; Holmgren, A.; Luthman, M.; Tljedal, I.B.
Thioredoxin and thioredoxin reductase in pancreatic islets may participate in diabetogenic free-radical production
Biochem. Biophys. Res. Commun.
107
1412-1418
1982
Bos taurus, Escherichia coli, Mus musculus
Sun, Q.A.; Zappacosta, F.; Factor, V.M.; Wirth, P.J.; Hatfield, D.L.; Gladyshev, V.N.
Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing
J. Biol. Chem.
276
3106-3114
2001
Drosophila melanogaster, Drosophila melanogaster (P91938), Homo sapiens, Homo sapiens (Q9NNW7), Mus musculus, Mus musculus (Q9JMH6), Rattus norvegicus
Gromer, S.; Gross, J.H.
Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase: implications for the antitumor effects of selenium
J. Biol. Chem.
277
9701-9706
2002
Drosophila melanogaster, Homo sapiens, Mus musculus, Plasmodium falciparum
Eckenroth, B.; Harris, K.; Turanov, A.A.; Gladyshev, V.N.; Raines, R.T.; Hondal, R.J.
Semisynthesis and characterization of mammalian thioredoxin reductase
Biochemistry
45
5158-5170
2006
Mus musculus (Q9JLT4), Mus musculus
Turanov, A.A.; Su, D.; Gladyshev, V.N.
Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase
J. Biol. Chem.
281
22953-22963
2006
Homo sapiens, Mus musculus
Gray, J.P.; Heck, D.E.; Mishin, V.; Smith, P.J.; Hong, J.Y.; Thiruchelvam, M.; Cory-Slechta, D.A.; Laskin, D.L.; Laskin, J.D.
Paraquat increases cyanide-insensitive respiration in murine lung epithelial cells by activating an NAD(P)H: paraquat oxidoreductase: Identification of the enzyme as thioredoxin reductase
J. Biol. Chem.
282
7939-7949
2007
Mus musculus
Biterova, E.I.; Turanov, A.A.; Gladyshev, V.N.; Barycki, J.J.
Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism
Proc. Natl. Acad. Sci. USA
102
15018-15023
2005
Mus musculus (Q9JLT4), Mus musculus
Wang, X.; Zhang, J.; Xu, T.
Cyclophosphamide as a potent inhibitor of tumor thioredoxin reductase in vivo
Toxicol. Appl. Pharmacol.
218
88-95
2007
Mus musculus
Thandavarayan, R.A.; Watanabe, K.; Ma, M.; Veeraveedu, P.T.; Gurusamy, N.; Palaniyandi, S.S.; Zhang, S.; Muslin, A.J.; Kodama, M.; Aizawa, Y.
14-3-3 protein regulates Ask1 signaling and protects against diabetic cardiomyopathy
Biochem. Pharmacol.
75
1797-1806
2008
Mus musculus
Eckenroth, B.E.; Rould, M.A.; Hondal, R.J.; Everse, S.J.
Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases
Biochemistry
46
4694-4705
2007
Drosophila melanogaster (P91938), Drosophila melanogaster, Mus musculus (Q8BTW3), Mus musculus
Eckenroth, B.E.; Lacey, B.M.; Lothrop, A.P.; Harris, K.M.; Hondal, R.J.
Investigation of the C-terminal redox center of high-Mr thioredoxin reductase by protein engineering and semisynthesis
Biochemistry
46
9472-9483
2007
Caenorhabditis elegans, Drosophila melanogaster, Mus musculus (Q8BTW3), Mus musculus
Geisberger, R.; Kiermayer, C.; Hoemig, C.; Conrad, M.; Schmidt, J.; Zimber-Strobl, U.; Brielmeier, M.
B- and T-cell-specific inactivation of thioredoxin reductase 2 does not impair lymphocyte development and maintenance
Biol. Chem.
388
1083-1090
2007
Mus musculus (Q9JLT4), Mus musculus
Kiermayer, C.; Michalke, B.; Schmidt, J.; Brielmeier, M.
Effect of selenium on thioredoxin reductase activity in Txnrd1 or Txnrd2 hemizygous mice
Biol. Chem.
388
1091-1097
2007
Mus musculus (Q9JLT4), Mus musculus (Q9JMH6)
Zhang, J.; Wang, X.; Lu, H.
Amifostine increases cure rate of cisplatin on ascites hepatoma 22 via selectively protecting renal thioredoxin reductase
Cancer Lett.
260
127-136
2008
Mus musculus
Zhang, Y.; Shen, X.
Heat shock protein 27 protects L929 cells from cisplatin-induced apoptosis by enhancing Akt activation and abating suppression of thioredoxin reductase activity
Clin. Cancer Res.
13
2855-2864
2007
Mus musculus
Wang, X.; Zhang, J.; Xu, T.
Thioredoxin reductase inactivation as a pivotal mechanism of ifosfamide in cancer therapy
Eur. J. Pharmacol.
579
66-73
2008
Mus musculus
Bondareva, A.A.; Capecchi, M.R.; Iverson, S.V.; Li, Y.; Lopez, N.I.; Lucas, O.; Merrill, G.F.; Prigge, J.R.; Siders, A.M.; Wakamiya, M.; Wallin, S.L.; Schmidt, E.E.
Effects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome
Free Radic. Biol. Med.
43
911-923
2007
Mus musculus (Q9JMH6), Mus musculus
Moskovitz, J.
Prolonged selenium-deficient diet in MsrA knockout mice causes enhanced oxidative modification to proteins and affects the levels of antioxidant enzymes in a tissue-specific manner
Free Radic. Res.
41
162-171
2007
Mus musculus
Hintze, K.J.; Katoh, Y.; Igarashi, K.; Theil, E.C.
Bach1 repression of ferritin and thioredoxin reductase1 is heme-sensitive in cells and in vitro and coordinates expression with heme oxygenase1, beta-globin, and NADP(H) quinone (oxido) reductase1
J. Biol. Chem.
282
34365-34371
2007
Mus musculus (Q9JMH6)
Flemer, S.; Lacey, B.M.; Hondal, R.J.
Synthesis of peptide substrates for mammalian thioredoxin reductase
J. Pept. Sci.
14
637-647
2008
Mus musculus
Arbones-Mainar, J.M.; Ross, K.; Rucklidge, G.J.; Reid, M.; Duncan, G.; Arthur, J.R.; Horgan, G.W.; Navarro, M.A.; Carnicer, R.; Arnal, C.; Osada, J.; de Roos, B.
Extra virgin olive oils increase hepatic fat accumulation and hepatic antioxidant protein levels in APOE-/- mice
J. Proteome Res.
6
4041-4054
2007
Mus musculus
Yoo, M.H.; Xu, X.M.; Carlson, B.A.; Patterson, A.D.; Gladyshev, V.N.; Hatfield, D.L.
Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication
PLoS ONE
2
e1112
2007
Homo sapiens (Q16881), Mus musculus (Q9JMH6), Mus musculus
Soerensen, J.; Jakupoglu, C.; Beck, H.; Foerster, H.; Schmidt, J.; Schmahl, W.; Schweizer, U.; Conrad, M.; Brielmeier, M.
The role of thioredoxin reductases in brain development
PLoS ONE
3
e1813
2008
Mus musculus (Q9JLT4), Mus musculus (Q9JMH6)
Zhang, J.; Wang, H.; Peng, D.; Taylor, E.W.
Further insight into the impact of sodium selenite on selenoenzymes: high-dose selenite enhances hepatic thioredoxin reductase 1 activity as a consequence of liver injury
Toxicol. Lett.
176
223-229
2008
Mus musculus (Q9JMH6)
Lacey, B.M.; Eckenroth, B.E.; Flemer, S.; Hondal, R.J.
Selenium in thioredoxin reductase: a mechanistic perspective
Biochemistry
47
12810-12821
2008
Anopheles gambiae, Caenorhabditis elegans, Drosophila melanogaster, Mus musculus, Rattus norvegicus
Conrad, M.
Transgenic mouse models for the vital selenoenzymes cytosolic thioredoxin reductase, mitochondrial thioredoxin reductase and glutathione peroxidase 4
Biochim. Biophys. Acta
1790
1575-1585
2009
Mus musculus
Arner, E.S.
Focus on mammalian thioredoxin reductases--important selenoproteins with versatile functions
Biochim. Biophys. Acta
1790
495-526
2009
Homo sapiens, Mus musculus (Q9JLT4), Mus musculus (Q9JMH6), Mus musculus
Volonte, D.; Galbiati, F.
Inhibition of thioredoxin reductase 1 by caveolin 1 promotes stress-induced premature senescence
EMBO Rep.
10
1334-1340
2009
Mus musculus, Homo sapiens (Q16881)
Singh, S.S.; Li, Y.; Ford, O.H.; Wrzosek, C.S.; Mehedint, D.C.; Titus, M.A.; Mohler, J.L.
Thioredoxin reductase 1 expression and castration-recurrent growth of prostate cancer
Transl. Oncol.
1
153-157
2008
Mus musculus (Q9JMH6)
Hondal, R.J.; Ruggles, E.L.
Differing views of the role of selenium in thioredoxin reductase
Amino Acids
41
73-89
2011
Mus musculus, Rattus norvegicus
Turanov, A.A.; Kehr, S.; Marino, S.M.; Yoo, M.H.; Carlson, B.A.; Hatfield, D.L.; Gladyshev, V.N.
Mammalian thioredoxin reductase 1: roles in redox homoeostasis and characterization of cellular targets
Biochem. J.
430
285-293
2010
Mus musculus, Rattus norvegicus (O89049), Homo sapiens (Q16881)
Wagner, C.; Sudati, J.H.; Nogueira, C.W.; Rocha, J.B.
In vivo and in vitro inhibition of mice thioredoxin reductase by methylmercury
Biometals
23
1171-1177
2010
Mus musculus
Turanov, A.A.; Hatfield, D.L.; Gladyshev, V.N.
Characterization of protein targets of mammalian thioredoxin reductases
Methods Enzymol.
474
245-254
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Snider, G.; Grout, L.; Ruggles, E.L.; Hondal, R.J.
Methaneseleninic acid is a substrate for truncated mammalian thioredoxin reductase: implications for the catalytic mechanism and redox signaling
Biochemistry
49
10329-10338
2010
Mus musculus
Kameritsch, P.; Singer, M.; Nuernbergk, C.; Rios, N.; Reyes, A.M.; Schmidt, K.; Kirsch, J.; Schneider, H.; Mueller, S.; Pogoda, K.; Cui, R.; Kirchner, T.; de Wit, C.; Lange-Sperandio, B.; Pohl, U.; Conrad, M.; Radi, R.; Beck, H.
The mitochondrial thioredoxin reductase system (TrxR2) in vascular endothelium controls peroxynitrite levels and tissue integrity
Proc. Natl. Acad. Sci. USA
118
e1921828118
2021
Mus musculus (Q9JLT4)
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