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
-
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
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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
ECTree
1.8.1.9 thioredoxin-disulfide reductaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 1.8.1.9 - thioredoxin-disulfide reductase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Na2SeO3
enhances hepatic TrxR1 activity, but only on the condition that it causes liver injury
Selenite
selenium treatment results in increased expression of almost all TrxR1 mRNA variants with increasing concentrations of selenite
selenium
selenocysteine
additional information
selenium
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the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
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the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
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the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
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TrxR1 contains a selenocysteine in the active site (Gly-Cys-SeCys-Gly)
selenium
selenoprotein, expression and function depends on adequate supply of selenium
selenium
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the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
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the enzyme possesses selenium in the form of selenocysteine in the active site
selenium
selenoprotein. TrxR1 is more sensitive to Se depletion than TrxR2, greater changes in liver than kidney. There is a prioritisation of TrxR2 over TrxR1 during Se deficiency such that TrxR1 expression is more sensitive to Se supply than TrxR2 but this sensitivity of TrxR1 is not fully accounted for by TrxR1 5' or 3'-untranslated region sequences when assessed using luciferase reporter constructs
selenium
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the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
thioredoxin reductase 1 is a selenoprotein, the oxidized enzyme presents a selenenylsulfide motif in trans-configuration, with the selenium atom of selenocysteine-498 positioned beneath the side chain of Tyr-116
selenium
TrxR1 is a selenoprotein that contains a selenocysteine residue at the penultimate C-terminal
selenium
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all three isoenzymes of mammalian TrxR contain an essential selenocysteine residue, which is the target of several drugs in cancer treatment or mercury intoxication
selenium
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the enzyme possesses selenium in the form of selenocysteine in the active site
selenocysteine
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contains selenocysteine as part of the redox active selenosulfide in the active center
selenocysteine
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heparin affinity depends on the selenium content, binding can be induced by reduction of the enzyme with NADPH or tris-(2-carboxyethyl)phosphine
selenocysteine
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contains selenocysteine as part of the redox active selenosulfide in the active center
selenocysteine
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isoform 1 contains 1 selenium per subunit, the mitochondrial isoform 2 contains 0.5 selenium per subunit
selenocysteine
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contains selenocysteine as part of the redox active selenosulfide in the active center
additional information
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not a selenoenzyme, but instead contains a highly unusual redox-active Cys-Cys sequence
additional information
DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
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DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
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DmTR shows high catalytic activity without the presence of a selenocysteine
