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Literature summary for 1.8.1.9 extracted from

  • Hudson, A.L.; Sotirchos, I.M.; Davey, M.W.
    Substrate specificity of the mitochondrial thioredoxin reductase of the parasitic nematode Haemonchus contortus (2010), Parasitol. Res., 107, 487-493.
    View publication on PubMed
Search for more literature for 1.8.1.9

Inhibitors

Inhibitors Comment Organism Structure
auranofin
-
 Haemonchus contortus
curcumin
-
 Haemonchus contortus
theaflavin
-
 Haemonchus contortus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm isoform TrxR1 Haemonchus contortus 5737
-
mitochondrion isoform TrxR2 Haemonchus contortus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
selenium TrxR1 contains a selenocysteine in the active site (Gly-Cys-SeCys-Gly) Haemonchus contortus

Organism

Organism UniProt Comment Textmining
Haemonchus contortus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
 Haemonchus contortus 2-nitro-5-thiobenzoate + NADP+
-
 ?
additional information isoform TrxR1 shows broad activity with thioredoxins from Escherichia coli, sheep, and Haemonchus contortus, while isoform TrxR2 has high activity only with the mitochondrial Haemonchus contortus thioredoxin Haemonchus contortus ?
-
 ?
selenite + NADPH + H+
-
 Haemonchus contortus ? + NADP+
-
 ?
thioredoxin disulfide + NADPH + H+
-
 Haemonchus contortus thioredoxin + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
thioredoxin reductase
-
 Haemonchus contortus
TrxR1 isoform Haemonchus contortus
TrxR2 isoform Haemonchus contortus

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Haemonchus contortus
NADPH
-
 Haemonchus contortus