Cloned (Comment) | Organism |
---|---|
- |
Fasciola gigantica |
General Stability | Organism |
---|---|
activities | Fasciola gigantica |
the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis | Fasciola gigantica |
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 | Fasciola gigantica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
selenium | role of selenocysteine in maintaining structure-function | Fasciola gigantica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fasciola gigantica | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Fasciola gigantica |
Synonyms | Comment | Organism |
---|---|---|
TGRsec | - |
Fasciola gigantica |
thioredoxin glutathione reductase | - |
Fasciola gigantica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoprotein | Fasciola gigantica |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme plays a principal role in redox homeostasis maintenance | Fasciola gigantica |