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Information on EC 1.8.1.B1 - thioredoxin glutathione reductase
for references in articles please use BRENDA:EC1.8.1.B1preliminary BRENDA-supplied EC number
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EC Tree
1.8.1.B1 thioredoxin glutathione reductaseSpecify your search results
Word Map
- 1.8.1.B1
- schistosoma
- schistosomiasis
- worm
- mansoni
- praziquantel
- glutaredoxin
- selenocysteine
-
antischistosomal
- gssg
- auranofin
-
platyhelminth
- flatworm
- dtnb
- fluke
-
sjtgr
- fasciola
-
oxadiazole
- cysticerci
-
hysteretic
- medicine
-
taenia
-
trematode
-
echinococcus
- granulosus
-
schistosomicidal
- crassiceps
- gigantica
-
selenocysteine-containing
- furoxans
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
thioredoxin glutathione reductase, smtgr, thioredoxin-glutathione reductase, tgrsec, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cTGR
SmTGR
TGR
thioredoxin glutathione reductase
thioredoxin-glutathione reductase
thioredoxin/glutathione reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione disulfide + NADPH + H+ = 2 glutathione + NADP+
-
-
-
-
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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
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
beta-hydroxyethyl disulfide + NADPH + H+
2 2-sulfanylethan-1-ol + NADP+
-
-
-
-
?
cytosolic thioredoxin + NADP+
cytosolic thioredoxin disulfide + NADPH
-
-
-
-
r
glutathione-hydroxyethyl disulfide + NADPH + H+
glutathione + 2-sulfanylethan-1-ol + NADP+
-
-
-
-
?
mitochondrial thioredoxin + NADP+
mitochondrial thioredoxin disulfide + NADPH
-
-
-
-
r
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
absolute specificity for NADPH as electron donor
-
-
?
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+
-
-
-
-
?
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+
-
-
-
?
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+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
absolute specificity for NADPH as electron donor
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
enzyme displays hysteretic behavior
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
the enzyme plays an essential role in maintaining the redox homeostasis and antioxidant defenses in the parasite Fasciola gigantica. Parasitic flukes have a limited set of antioxidant proteins in contrast to their mammalian hosts. In platyhelminthic parasites, the two systems (glutathione/glutaredoxin system and thioredoxin system) are replaced by a single system of a multifunctional flavin containing chimeric selenoenzyme known as thioredoxin glutathione reductase, which donates electrons to both thioredoxin disulfide and glutathione disulfide in these parasites
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
the enzyme of the parasite essential for the survival of schistosomes in the mammalian host
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
the enzyme follows a two-site ping-pong bi bi kinetic mechanism, in which both substrates and products are bound in rapid equilibrium fashion
-
-
?
GSSG + NADPH + H+
glutathione + NADP+
-
absolute specificity for NADPH as electron donor
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the enzyme of the parasite essential for the survival of schistosomes in the mammalian host
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the enzyme follows a two-site ping-pong bi bi kinetic mechanism, in which both substrates and products are bound in rapid equilibrium fashion
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
Escherichia coli thioredoxin disulfide
-
-
?
additional information
?
-
-
the glutathione reductase activity of TGR exhibits hysteretic behavior regulated by the [GSSG]/[GSH] ratio. This behavior is associated with glutathionylation by GSSG and abolished by deglutathionylation
-
-
?
additional information
?
-
-
TGR promotes isomerization of disulfide bonds formed between glutathione peroxidase 4 and certain sperm proteins, generating a 46-kDa species containing glutathione peroxidase 4 from high molecular weight nonspecific cross-links
-
-
?
additional information
?
-
-
the parasite-specific enzyme thioredoxin glutathione reductase is a component of the defense system
-
-
?
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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
additional information
?
-
-
the parasite-specific enzyme thioredoxin glutathione reductase is a component of the defense system
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
the enzyme plays an essential role in maintaining the redox homeostasis and antioxidant defenses in the parasite Fasciola gigantica. Parasitic flukes have a limited set of antioxidant proteins in contrast to their mammalian hosts. In platyhelminthic parasites, the two systems (glutathione/glutaredoxin system and thioredoxin system) are replaced by a single system of a multifunctional flavin containing chimeric selenoenzyme known as thioredoxin glutathione reductase, which donates electrons to both thioredoxin disulfide and glutathione disulfide in these parasites
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
-
-
?
glutathione disulfide + NADPH + H+
2 glutathione + NADP+
-
the enzyme of the parasite essential for the survival of schistosomes in the mammalian host
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the enzyme of the parasite essential for the survival of schistosomes in the mammalian host
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
each catalytically active unit consists of three redox centers: FAD and an N-terminal Cys57/Cys62 redox-active disulfide from one monomer and a Cys489/Cys490 C-terminal redox-active disulfide from the second monomer
FAD
-
the flavin ring of FAD cofactor binds in a hydrophobic cleft formed by Cys154, Val157, Gly158, Cys159, Pro572, Phe474, and Pro443
NADPH
-
nicotinamide moiety binds up in the hydrophobic cleft formed by Val348, Ile266, Pro264,Val292, Met315, Val316, and Pro349, etc. and the diphosphate forms H-bond with Ile391, Ser318, and Arg317. The ribose sugar formes H-bonds with Arg262, Arg322, and Tyr296
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
selenium
-
glutathione reductase and thioredoxin reductase activities are dependent on the Sec-containing redox center. The activity loss caused by the Sec-to-Cys mutation can be partially compensated by a Cys-to-Sec mutation of the neighboring residue, indicating that Sec can support catalysis at this alternative position
selenium
Sec-containing redox center. The selenium content of wild-type enzyme and C519S mutant enzyme and C574S mutant enzyme is 17%, 15%, and 15%
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(1,3-dimethyl-1H-pyrazol-4-yl)methanone]
-
-
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(4-methoxyphenyl)methanone]
-
-
(3R,5R,8R) 5-(((3-carboxy-4-nitrophenyl)disulfanyl)methyl)tetrahydro-2H-thiazolo[4,3-b]thiazole-3-carboxylic acid
-
1,8-naphthyridine-2 carboxylate
mixed inhibition. 1,8-Naphthyridine-2 carboxylate prevents Tyr296 from rotating, a process necessary for NADPH binding and enzyme reduction. It inhibits by stabilizing a protein conformation whose affinity for NADPH is greatly reduced
-
2-(4-chlorophenoxy)-6-methyl-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
-
-
2-(4-ethoxyphenoxy)-6-methyl-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
-
-
4-aminopiazthiole
inhibit the enzyme in a NADPH-dependent manner, and the inhibition appears to be irreversible even upon extensive dilution of the inhibited protein
-
5-(((3-carboxy-4-nitrophenyl)disulfanyl)methyl) (2RS,5RS)-3,3a-dihydro-benzo[d]thiazolo[4,3-b]thiazole
-
5-bromo-N-ethyl-3,4-dinitrothiophen-2-amine
-
at 0.005 microM, 100 % larval death at 48 hours
5-chloro-N-[4-[ethyl(phenyl)sulfamoyl]phenyl]-2-(methanesulfonyl)pyrimidine-4-carboxamide
-
-
-
6-methyl-2-phenoxy-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
-
-
7-[(4-methoxyphenyl)[(4-methylpyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
-
AuI-pyridine-2-thiol N-oxide
a potent inhibitor that achieves 75% inhibition at a 1:1 thioredoxin glutathione reductase:Au ratio and efficiently kills Echinococcus granulosus in vitro
-
curcumin
-
time-dependent process. An intermediary compound of curcumin oxidation, probably spiroepoxide, is responsible. Preincubation of curcumin in the presence of NADPH results in the loss of its inhibitory ability. Preincubation of curcumin with sulfhydryl compounds fully protected the enzyme from inhibition
diethyl 2-(3-bromo-6-oxo-6H-anthra[1,9-cd][1,2]oxazol-4-yl)-3-oxobutanedioate
-
-
-
glutathione disulfide
-
substrate inhibition at moderate or high concentrations. Noncompetitive mode of inhibition in which the disulfide behaves as an affinity label-like reagent through its binding and reduction at an alternative site, leading the enzyme into an inactive state
indole-3-carbinol
inhibit the enzyme in a NADPH-dependent manner, and the inhibition appears to be irreversible even upon extensive dilution of the inhibited protein
methyl (5-[1-[(tert-butoxycarbonyl)amino]-2-phenylethyl]-1,3,4-oxadiazole-2-sulfonyl)acetate
-
-
-
NOC-7
-
i.e. 1-hydroxy-2-oxo-3-(N-3-methyl-aminopropyl)-3-methyl-1-triazene, complete inhibition at 0.1 mM
P-1,3-benzothiazol-2-yl-N-(2-fluorophenyl)-P-phenylphosphinic amide
-
-
P-1,3-benzothiazol-2-yl-N-(5-chloropyridin-2-yl)-P-phenylphosphinic amide
-
-
P-1,3-benzothiazol-2-yl-P-phenyl-N-1,3-thiazol-2-ylphosphinic amide
-
-
[mu-[1-(hydroxy-1kappaO)-2-(sulfanyl-1kappaS)pyridin-1-iumato(2-)]]-[mu-[1-(hydroxy-2kappaO)-2-(sulfanyl-1kappaS)pyridin-1-iumato(2-)]]bis(triphenylphosphane)digold
-
a single gold atom binds to Cys519 and Cys573 in the AuI-enzyme complex. 7580% inhibition of thioredoxin and glutathione reductase activities is achieved at a 1:1 concentration ratio of inhibitor:enzyme
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