1.8.1.B1: thioredoxin glutathione reductase
This is an abbreviated version!
For detailed information about thioredoxin glutathione reductase, go to the full flat file.
Word Map on EC 1.8.1.B1
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1.8.1.B1
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schistosoma
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schistosomiasis
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worm
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mansoni
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praziquantel
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glutaredoxin
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selenocysteine
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antischistosomal
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gssg
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auranofin
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platyhelminth
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flatworm
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dtnb
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fluke
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sjtgr
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fasciola
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oxadiazole
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cysticerci
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hysteretic
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medicine
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taenia
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trematode
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echinococcus
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granulosus
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schistosomicidal
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crassiceps
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gigantica
-
selenocysteine-containing
-
furoxans
-
analysis
- 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
Reaction
Synonyms
cTGR, DmTrxR, EgTGR, mTGR, SmTGR, TGR, TGRsec, thioredoxin glutathione reductase, thioredoxin-glutathione reductase, thioredoxin/glutathione reductase
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Posttranslational Modification on EC 1.8.1.B1 - thioredoxin glutathione reductase
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
additional information
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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
