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Literature summary for 1.8.1.B1 extracted from

  • Brandstaedter, C.; Fritz-Wolf, K.; Weder, S.; Fischer, M.; Hecker, B.; Rahlfs, S.; Becker, K.
    Kinetic characterization of wild-type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms (2018), FEBS J., 285, 542-558 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Protein Variants

Protein Variants Comment Organism
U642C in the wild-type enzyme, the KM value for NADPH is significantly higher than in the mutant enzyme, whereas the KM value for the oxidizing substrate thioredoxin disulfide in the wild-type enzyme is significantly lower than the Km-value of the mutant enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0051
-
NADPH mutant enzyme U642C, cosubstrate: thioredoxin disulfide, pH 7.4, 25°C Homo sapiens
0.0075
-
thioredoxin disulfide recombinant wild-type enzyme, pH 7.4, 25°C Homo sapiens
0.0166
-
NADPH recombinant wild-type enzyme, cosubstrate: thioredoxin disulfide, pH 7.4, 25°C Homo sapiens
0.0205
-
thioredoxin disulfide mutant enzyme U642C, pH 7.4, 25°C Homo sapiens
0.0208
-
NADPH recombinant wild-type enzyme, cosubstrate: glutathione disulfide, pH 6.9, 25°C Homo sapiens
0.0208
-
glutathione disulfide recombinant wild-type enzyme, pH 6.9, 25°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
selenium selenoprotein Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glutathione disulfide + NADPH + H+ Homo sapiens
-
2 glutathione + NADP+
-
?
thioredoxin disulfide + NADPH + H+ Homo sapiens
-
thioredoxin + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q86VQ6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinantly produced human enzyme (hTGR), 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 Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0125
-
substrate: glutathione disulfide, recombinant wild-type enzyme, pH 6.9, 25°C Homo sapiens
0.0599
-
substrate: thioredoxin disulfide, mutant enzyme U642C,pH 7.4, 25°C Homo sapiens
0.0947
-
substrate: thioredoxin disulfide, recombinant wild-type enzyme, pH 7.4, 25°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione disulfide + NADPH + H+
-
Homo sapiens 2 glutathione + NADP+
-
?
thioredoxin disulfide + NADPH + H+
-
Homo sapiens thioredoxin + NADP+
-
?

Synonyms

Synonyms Comment Organism
TGR
-
Homo sapiens
thioredoxin glutathione reductase
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.015
-
NADPH 25°C, pH 7.4, mutant enzyme U642C, cosubstrate: thioredoxin disulfide Homo sapiens
0.02
-
thioredoxin disulfide 25°C, pH 7.4, mutant enzyme U642C Homo sapiens
0.11
-
glutathione disulfide 25°C, pH 6.9, recombinant wild-type enzyme Homo sapiens
0.14
-
NADPH 25°C, pH 6.9, recombinant wild-type enzyme, cosubstrate: thioredoxin disulfide Homo sapiens
0.18
-
thioredoxin disulfide 25°C, pH 7.4, recombinant wild-type enzyme Homo sapiens
0.2
-
NADPH 25°C, pH 7.4, recombinant wild-type enzyme, cosubstrate: thioredoxin disulfide Homo sapiens