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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

Reaction

glutathione disulfide
+
NADPH
+
H+
= 2 glutathione +
NADP+

Synonyms

cTGR, DmTrxR, EgTGR, mTGR, SmTGR, TGR, TGRsec, thioredoxin glutathione reductase, thioredoxin-glutathione reductase, thioredoxin/glutathione reductase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.B1 thioredoxin glutathione reductase

General Stability

General Stability on EC 1.8.1.B1 - thioredoxin glutathione reductase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activities
-
continuous freezing and thawing results in loss of the enzyme activity
-
the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis
-
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
-