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Literature summary for 1.8.1.B1 extracted from

  • Bonilla, M.; Denicola, A.; Novoselov, S.V.; Turanov, A.A.; Protasio, A.; Izmendi, D.; Gladyshev, V.N.; Salinas, G.
    Platyhelminth mitochondrial and cytosolic redox homeostasis is controlled by a single thioredoxin glutathione reductase and dependent on selenium and glutathione (2008), J. Biol. Chem., 283, 17898-17907.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.B1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Echinococcus granulosus

Protein Variants

Protein Variants Comment Organism
additional information analysis of TGR mutants reveales that the glutaredoxin domain is required for the glutathione reductase activity but does not affect the thioredoxin reductase activity. In contrast, both glutathione reductase and thioredoxin reductase activities are dependent on the Sec-containing redox center. The activity loss caused by the Sec-to-Cys mutation can be partially compensated by a Cys-to-Sec mutation of the neighboring residue, indicating that Sec can support catalysis at this alternative position Echinococcus granulosus

Inhibitors

Inhibitors Comment Organism Structure
auranofin the TGR inhibitor, killes larval worms in vitro Echinococcus granulosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0095
-
 mitochondial thioredoxin pH 7.0, 25°C, wild-type enzyme Echinococcus granulosus
0.012
-
 mitochondial thioredoxin pH 7.0, 25°C, Sec-to-Cys mutant enzyme Echinococcus granulosus
0.034
-
 cytosolic thioredoxin pH 7.0, 25°C, wild-type enzyme Echinococcus granulosus

Metals/Ions

Metals/Ions Comment Organism Structure
selenium glutathione reductase and thioredoxin reductase activities are dependent on the Sec-containing redox center. The activity loss caused by the Sec-to-Cys mutation can be partially compensated by a Cys-to-Sec mutation of the neighboring residue, indicating that Sec can support catalysis at this alternative position Echinococcus granulosus

Organism

Organism UniProt Comment Textmining
Echinococcus granulosus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the glutathione reductase activity of TGR exhibits hysteretic behavior regulated by the [GSSG]/[GSH] ratio. This behavior is associated with glutathionylation by GSSG and abolished by deglutathionylation. TGR is glutathionylated at two Cys residues: Cys88 and Cys354 after 1 min incubation with 1 mM GSSG and NADPH. Absence of NADPH did not prevent glutathionylation Echinococcus granulosus

Purification (Commentary)

Purification (Comment) Organism
-
 Echinococcus granulosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
 Echinococcus granulosus 2-nitro-5-thiobenzoate + NADP+
-
 ?
cytosolic thioredoxin + NADP+
-
 Echinococcus granulosus cytosolic thioredoxin disulfide + NADPH
-
 r
GSSG + NADPH + H+
-
 Echinococcus granulosus GSH + NADP+
-
 ?
mitochondrial thioredoxin + NADP+
-
 Echinococcus granulosus mitochondrial thioredoxin disulfide + NADPH
-
 r
additional information the glutathione reductase activity of TGR exhibits hysteretic behavior regulated by the [GSSG]/[GSH] ratio. This behavior is associated with glutathionylation by GSSG and abolished by deglutathionylation Echinococcus granulosus ?
-
 ?
thioredoxin + NADP+
-
 Echinococcus granulosus thioredoxin disulfide + NADPH + H+
-
 ?

Synonyms

Synonyms Comment Organism
TGR
-
 Echinococcus granulosus
thioredoxin glutathione reductase
-
 Echinococcus granulosus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.4
-
 mitochondial thioredoxin pH 7.0, 25°C, Sec-to-Cys mutant enzyme Echinococcus granulosus
118
-
 5,5'-dithiobis(2-nitrobenzoic acid) pH 7.0, 25°C, wild-type enzyme Echinococcus granulosus
131
-
 mitochondial thioredoxin pH 7.0, 25°C, wild-type enzyme Echinococcus granulosus
197
-
 cytosolic thioredoxin pH 7.0, 25°C, wild-type enzyme Echinococcus granulosus