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Enzyme Nomenclature
Information on EC 1.8.1.B1 - thioredoxin glutathione reductase
Word Map on EC 1.8.1.B1
- 1.8.1.B1
- parasite
- schistosoma
- schistosomiasis
- mansoni
- glutaredoxin
-
worm
- selenocysteine
- praziquantel
- japonicum
-
oxadiazole
-
antischistosomal
- medicine
- gssg
- auranofin
-
platyhelminth
-
flatworm
-
echinococcus
- dtnb
- granulosus
-
hysteretic
-
thiol-disulfide
- fasciola
- fluke
-
taenia
- furoxans
-
deglutathionylation
- cysticerci
- crassiceps
-
selenocysteine-containing
- tapeworm
-
trematode
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.8.1.B1
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme plays a crucial role in maintaining redox homeostasis
physiological function
-
the enzyme is able to protect glutamine synthetase from oxidative inactivation, suggesting that the enzyme is competent to contend with oxidative stress
physiological function
-
the enzyme is essential for maintaining the thiol-disulfide redox homeostasis of Schistosoma japonicum
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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'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
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+
-
absolute specificity for NADPH as electron donor
-
-
?
GSSG + NADPH + H+
glutathione + NADP+
-
absolute specificity for NADPH as electron donor
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
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 SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
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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
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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
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INHIBITORS
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]
-
-
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
-
-
6-methyl-2-phenoxy-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
-
-
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
-
-
additional information
-
the recombinant plasmid DNA vaccine pVAX1/SjTGR lowers enzymatic activity in vivo and in vitro
-
auranofin
-
auranofin at 0.005 mg/ml (0.0074 mM) reduces 57.1% of the thioredoxin reductase activity and 71% of the glutathione reductase activity in the Schistosoma japonicum adult worms
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.792
2-hydroxyethyl disulfide
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
additional information
additional information
-
kinetic properties of the Grx domain of TGR
-
0.043
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.107
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.1451
5,5'-dithiobis(2-nitrobenzoic acid)
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
0.169
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.187
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.23
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.319
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.375
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.406
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.013
GSSG
-
mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.016
GSSG
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.023
GSSG
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.024
GSSG
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.031
GSSG
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.036
GSSG
-
mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.042
GSSG
-
wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.071
GSSG
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.189
GSSG
-
mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.012
mitochondial thioredoxin
-
pH 7.0, 25°C, Sec-to-Cys mutant enzyme
-
0.01097
NADPH
-
with glutaredoxin as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
0.02142
NADPH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
0.08324
NADPH
-
with GSSG as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
0.00324
thioredoxin disulfide
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
0.007
thioredoxin disulfide
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.008
thioredoxin disulfide
-
mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.015
thioredoxin disulfide
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.019
thioredoxin disulfide
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.022
thioredoxin disulfide
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.65
2-hydroxyethyl disulfide
Schistosoma japonicum
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
4
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
5
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
6
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
8
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
8.16
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma japonicum
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
16
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
118
5,5'-dithiobis(2-nitrobenzoic acid)
Echinococcus granulosus
-
pH 7.0, 25°C, wild-type enzyme
0.6
GSSG
Schistosoma mansoni
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.7
GSSG
Schistosoma mansoni
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
3.5
GSSG
Schistosoma mansoni
-
mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
4
GSSG
Schistosoma mansoni
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
5
GSSG
Schistosoma mansoni
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
7
GSSG
Schistosoma mansoni
-
mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
19.4
GSSG
Schistosoma mansoni
-
wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
25
GSSG
Schistosoma mansoni
-
mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
6.4
mitochondial thioredoxin
Echinococcus granulosus
-
pH 7.0, 25°C, Sec-to-Cys mutant enzyme
-
4.87
NADPH
Schistosoma japonicum
-
with GSSG as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
10.92
NADPH
Schistosoma japonicum
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
14.93
NADPH
Schistosoma japonicum
-
with glutaredoxin as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
3.5
thioredoxin disulfide
Schistosoma mansoni
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
4.78
thioredoxin disulfide
Schistosoma japonicum
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
8
thioredoxin disulfide
Schistosoma mansoni
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C; mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
9
thioredoxin disulfide
Schistosoma mansoni
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
2-hydroxyethyl disulfide
Schistosoma japonicum
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
6426
119
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma japonicum
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
221
58.5
NADPH
Schistosoma japonicum
-
with GSSG as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
5
510
NADPH
Schistosoma japonicum
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
5
1360
NADPH
Schistosoma japonicum
-
with glutaredoxin as cosubstrate, at 25°C in 0.1 M potassium phosphate (pH 7.4)
5
1480
thioredoxin disulfide
Schistosoma japonicum
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
476
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00129 - 0.00408
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(1,3-dimethyl-1H-pyrazol-4-yl)methanone]
0.00055
2-(4-chlorophenoxy)-6-methyl-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
Schistosoma mansoni
-
-
0.0006
2-(4-ethoxyphenoxy)-6-methyl-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
Schistosoma mansoni
-
-
0.004
6-methyl-2-phenoxy-2,3-dihydro-1,3,2-diazaphosphinin-4(1H)-one 2-oxide
Schistosoma mansoni
-
-
0.009
diethyl (3-bromo-6-oxo-6H-anthra[1,9-cd]isoxazol-5-yl)propanedioate
Schistosoma mansoni
-
-
0.00008
dimethyl (3-bromo-6-oxo-6H-anthra[1,9-cd]isoxazol-5-yl)propanedioate
Schistosoma mansoni
-
-
0.008
LS826
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH; pH 7.4, 25°C, substrates: GSSG + NADPH
0.000789 - 0.00154
P-1,3-benzothiazol-2-yl-N-(5-chloropyridin-2-yl)-P-phenylphosphinic amide
0.000038
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis(2-furylmethanone)
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.000082
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis(2-furylmethanone)
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.000042
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis(2-thienylmethanone)
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.00051
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis(2-thienylmethanone)
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.00129
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(1,3-dimethyl-1H-pyrazol-4-yl)methanone]
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.002
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(1,3-dimethyl-1H-pyrazol-4-yl)methanone]
Schistosoma mansoni
-
-
0.00408
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(1,3-dimethyl-1H-pyrazol-4-yl)methanone]
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.00006
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(4-methoxyphenyl)methanone]
Schistosoma mansoni
-
-
0.000105
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(4-methoxyphenyl)methanone]
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.00244
(2-oxido-1,2,5-oxadiazole-3,4-diyl)bis[(4-methoxyphenyl)methanone]
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.0005
3-DAP
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.00032
4-phenyl-1,2,5-oxadiazole-3-carbonitrile 2-oxide
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.00167
4-phenyl-1,2,5-oxadiazole-3-carbonitrile 2-oxide
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.0000032
auranofin
Schistosoma mansoni
-
wild type enzyme, with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.0000054
auranofin
Schistosoma mansoni
-
wild type enzyme, with GSSG as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.000007
auranofin
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.0000083
auranofin
Schistosoma mansoni
-
wild type enzyme, with thioredoxin disulfide as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.00007
aurothioglucose
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.00009
aurothiomalate
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.025
CDE16-2
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.007
CDE4
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.003
furoxan
Schistosoma mansoni
-
wild type enzyme, with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.0032
furoxan
Schistosoma mansoni
-
wild type enzyme, with GSSG as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.0054
furoxan
Schistosoma mansoni
-
wild type enzyme, with thioredoxin disulfide as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.0005
JD159
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.0025
naphthazarin
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.08
OPZ
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.012
P-1,3-benzothiazol-2-yl-N-(2-fluorophenyl)-P-phenylphosphinic amide
Schistosoma mansoni
-
-
0.0151
P-1,3-benzothiazol-2-yl-N-(2-fluorophenyl)-P-phenylphosphinic amide
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.0203
P-1,3-benzothiazol-2-yl-N-(2-fluorophenyl)-P-phenylphosphinic amide
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.000789
P-1,3-benzothiazol-2-yl-N-(5-chloropyridin-2-yl)-P-phenylphosphinic amide
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.0008
P-1,3-benzothiazol-2-yl-N-(5-chloropyridin-2-yl)-P-phenylphosphinic amide
Schistosoma mansoni
-
-
0.00154
P-1,3-benzothiazol-2-yl-N-(5-chloropyridin-2-yl)-P-phenylphosphinic amide
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.0000212
P-1,3-benzothiazol-2-yl-P-phenyl-N-1,3-thiazol-2-ylphosphinic amide
Schistosoma mansoni
-
pH 7, thioredoxin reductase activity
0.000025
P-1,3-benzothiazol-2-yl-P-phenyl-N-1,3-thiazol-2-ylphosphinic amide
Schistosoma mansoni
-
-
0.000121
P-1,3-benzothiazol-2-yl-P-phenyl-N-1,3-thiazol-2-ylphosphinic amide
Schistosoma mansoni
-
pH 7, glutathione reductase activity
0.000051
PAT
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
0.000008
potassium antimony tartrate
Schistosoma mansoni
-
wild type enzyme, with GSSG as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.000009
potassium antimony tartrate
Schistosoma mansoni
-
wild type enzyme, with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.000045
potassium antimony tartrate
Schistosoma mansoni
-
wild type enzyme, with thioredoxin disulfide as substrate, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.004
RMA35
Schistosoma mansoni
-
pH 7.4, 25°C, substrates: 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.11
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, at pH 7.4 and 25°C
35
-
crude extract, using 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, at pH 7.8 and 25°C
128.5
-
crude extract, using hydroxyethyl disulfide as substrate, at pH 7.8 and 25°C
229
-
after 31fold purification, using GSSG as substrate, at pH 7.8 and 25°C
1091
-
after 31fold purification, using 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, at pH 7.8 and 25°C
2243
-
after 31fold purification, using hydroxyethyl disulfide as substrate, at pH 7.8 and 25°C
additional information
-
1536-well based kinetic absorbance assay for thioredoxin glutathione reductase. The assay uses the catalytic reduction of DTNB by NADPH in the presence of thioredoxin glutathione reductase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
thioredoxin glutathione reductase appears to be the major, if not the sole enzyme for these activities in adult worms, completely replacing thioredoxin reductase and glutathione reductase
-
TGR is regulated by both selenium availability and selenocysteine tRNA status. This regulation is more pronounced in liver, whereas in testes, the expression level is only slightly affected
-
TGR is not detected in the testes of a 20-day-old mouse. It is highly expressed in 7-month-old mouse testes. The enzyme accumulates in testes after puberty. The protein is particularly abundant in elongating spermatids at the site of mitochondrial sheath formation but is absent in mature sperm
-
TGR is regulated by both selenium availability and selenocysteine tRNA status. This regulation is more pronounced in liver, whereas in testes, the expression level is only slightly affected
much higher number of TGR transcripts in testis than in the rest of organs
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mitochondrial and cytosolic variants of TGR are generated from a single TGR gene
-
mitochondrial and cytosolic variants of TGR are generated from a single TGR gene
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
66000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 64900, calculated from amino acid sequence; x * 65000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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. TGR is glutathionylated at two Cys residues: Cys88 and Cys354 after 1 min incubation with 1 mM GSSG and NADPH. Absence of NADPH did not prevent glutathionylation
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.2 A resolution of TGR, deleted in the last two residues
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2',5'-ADP Sepharose column chromatography and Sephadex G-25 gel filtration
-
ammonium sulfate precipitation, Ni-NTA column chromatography, GSH-Sepharose column chromatography, and 2',5'-ADP-Sepharose column chromatography
DEAE-Sephacel gel filtration, hydroxyapatite chromatography column chromatography, and Cibacron blue chromatography column chromatography
-
small amounts of the soluble enzyme are obtained by purifying it from a large quantity of cells, in which protein synthesis is induced slowly for a period of 24 h at a low temperature
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of two trans-spliced mRNA variants that encode thioredoxin glutathione reductases (mitochondrial and cytosolic selenocysteine-containing isoforms) that possess identical glutaredoxin and thioredoxin reductase domains and differ exclusively in their N-termini; cloning of two trans-spliced mRNA variants that encode thioredoxin glutathione reductases (mitochondrial and cytosolic selenocysteine-containing isoforms) that possess identical glutaredoxin and thioredoxin reductase domains and differ exclusively in their N-termini
-
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli as a six-histidine tagged protein. Recombinant His-SmTGR, which would not have a penultimate selenocysteine when expressed in Escherichia coli, has no measurable activity in the insulin reduction assay
-
recombinant enzyme with a fused bacterial-type SECIS element is expressed in Escherichia coli strain BL21(DE3)
-
recombinant TGR is mostly insoluble when expressed in Escherichi coli, and neither cloning of the enzyme that contain various tags nor coexpression of TGR with chaperones increases its solubility
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression levels in 35-day-old worms and 42-day-old female worms are approximately 7times higher than the 7- and 14-day-old worms, and over 2times higher than 21- and 28-day-old worms and 42-day-old male worms
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H464Q
-
mutant enzyme has only 2% of the wild-type activity. The pH dependence of Vmax for wild-type DmTrxR has pKa values of 6.4 and 9.3 on the DmTrxR-DmTrx-2 complex, whereas H464Q DmTrxR only has an observable pKa at 6.4, indicating that the pKa at pH 9.3 is contributed mainly by His464. The pKa at pH 6.4 is assigned to Cys57 and Cys490. The thiolate on Cys490 is the nucleophile in the reduction of Trx. In contrast to wild-type DmTrxR, H464Q DmTrxR does not stabilize a thiolate-FAD charge-transfer complex in the presence of excess NADPH. The rates of steps in both the reductive and the oxidative half-reactions are markedly diminished in H464Q DmTrxR as compared to those of wild-type enzyme, indicating that His464 is involved in both half-reactions
C31S
-
the mutant has negligible deglutathionylase and GR activities when compared with wild type enzyme
C34S
-
both the deglutathionylase and GR activities of the mutant are only slightly lower when compared with wild type enzyme
C28A
-
compared to the wild type enzyme, the mutant shows 38% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 4% activity with GSSG, and 74% activity with thioredoxin disulfide
C28A/C31A
-
compared to the wild type enzyme, the mutant shows 50% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 3% activity with GSSG, and 79% activity with thioredoxin disulfide
C31A
-
compared to the wild type enzyme, the mutant shows 38% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 18% activity with GSSG, and 100% activity with thioredoxin disulfide
C31S
-
compared to the wild type enzyme, the mutant shows 100% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 129% activity with GSSG, and 105% activity with thioredoxin disulfide
C520A
-
compared to the wild type enzyme, the mutant shows 31% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 26% activity with GSSG, and 47% activity with thioredoxin disulfide
C520A/C574A
-
compared to the wild type enzyme, the mutant shows 38% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 26% activity with GSSG, and 42% activity with thioredoxin disulfide
C574A
-
compared to the wild type enzyme, the mutant shows 38% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 37% activity with GSSG, and 42% activity with thioredoxin disulfide
U597C
additional information
-
analysis of TGR mutants reveales that the glutaredoxin domain is required for the glutathione reductase activity but does not affect the thioredoxin reductase activity. In contrast, both 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
U597C
-
compared to the wild type enzyme, the mutant shows 25% activity with 5,5'-dithiobis(2-nitrobenzoic acid), 21% activity with GSSG, and 18% activity with thioredoxin disulfide
U597C
-
the mutant displays significantly decreased enzyme activities compared to the wild type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
the enzyme presents a target for anti-schistosomiasis drug development
medicine
-
identification of oxadiazole 2-oxides (TGR inhibitors) as new lead compounds for schistosomiasis chemotherapy
medicine
-
quantitative high-throughput screen identifies inhibitors of the Schistosoma mansoni redox cascade, several of which are highly potent and should serve both as mechanistic tools for probing the redox balance in Schistosome mansoni, and starting points for developing medicinal leads for treatments for schistosomiasis
medicine
the enzyme is a promising target for anti Fasciola treatments
medicine
-
the enzyme is a potential target for development of novel agents against schistosomes
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.B1)
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