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
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selenocysteine-containing
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furoxans
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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
ECTree
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General Stability
General Stability on EC 1.8.1.B1 - thioredoxin glutathione reductase
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the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis
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the urea-induced unfolding of the recombinant enzyme (FgTGRsec) and its N-terminal truncated variant (DELTANTDFgTGRsec) undergo unfolding in a three state manner. First, the protein undergoes a conformational transition rendering a near-native state with no FAD bound, and then full unfolding of the apodimer occurs without dissociation. The Grx domain stabilizes the global FgTGRsec structure and positively regulates FgTGRsec activity, and alteration in the FAD microenvironment is directly proportional to the loss of thioredoxin reductase (TrxR) and glutathione reductase
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