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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

Cloned

Cloned on EC 1.8.1.B1 - thioredoxin glutathione reductase

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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
expresion in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
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
expresssion in Escherichia coli, truncated form without the last two residues Sec597Gly598
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
-
the human enzyme is recombinantly produced (hTGR) by fusing its open reading frame with a bacterial selenocysteine insertion sequence element and coexpressing the construct in Escherichia coli together with the selA, selB, and selC genes. Additionally, the Sec->Cys mutant (hTGRU642C) of the full-length protein, the isolated TrxR domain (hTGR151-643) and the Grx domain containing a monothiol active site (hTGR1-150) are produced
the ORF of Ov-TGR is inserted into pABC2 plasmid and transformed into Escherichia coli strain C321.DETLTAA to facilitate selenocysteine incorporation