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Literature summary extracted from

  • Zhong, L.; Holmgren, A.
    Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations (2000), J. Biol. Chem., 275, 18121-18128.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.9 cysteine part of the active site Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.9 overexpression of antisense mutant in Escherichia coli, expression of wild-type in COS-7 cells, amino acid sequence analysis Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.9 additional information truncated enzyme mutant without catalytic active C-terminus Rattus norvegicus
1.8.1.9 SeC498C antisense technique, exchange in the catalytic active selenosulfide at the C-terminus, resulting in higher pH-optimum, 100fold lower turnover number, 10fold lower Km-value, no activity with H2O2 Rattus norvegicus
1.8.1.9 SeC498G antisense technique, reduced activity Rattus norvegicus
1.8.1.9 SeC498S antisense technique, reduced activity Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.9 0.0004
-
 thioredoxin SeC498C mutant, human thioredoxin Rattus norvegicus
1.8.1.9 0.0033
-
 human thioredoxin wild-type enzyme Rattus norvegicus
1.8.1.9 2.5
-
 H2O2 wild-type enzyme, Km-value can be reduced by addition of selenocysteine Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.1.9 selenocysteine contains selenocysteine as part of the redox active selenosulfide in the active center Rattus norvegicus
1.8.1.9 selenocysteine encoded by TGA stop codon Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Rattus norvegicus
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.9 additional information
-
 several mutants with different substrates Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH i.e. DTNB Rattus norvegicus 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 5,5'-dithiobis(2-nitrobenzoic acid) + NADPH coupled assay Rattus norvegicus 2-nitro-5-thiobenzoate + NADP+
-
 ?
1.8.1.9 human thioredoxin + NADP+
-
 Rattus norvegicus human thioredoxin disulfide + NADPH + H+
-
 r
1.8.1.9 methylseleninate + H2O2 addition of selenocysteine increases the activity by 20% Rattus norvegicus ?
-
 ?
1.8.1.9 methylseleninate + H2O2 only wild-type enzyme Rattus norvegicus ?
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay with DTNB Rattus norvegicus thioredoxin disulfide + NADPH
-
 ?
1.8.1.9 thioredoxin + NADP+ coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin Rattus norvegicus thioredoxin disulfide + NADPH
-
 ?
1.8.1.9 thioredoxin + NADP+ in presence of NADPH, coupled assay Rattus norvegicus thioredoxin disulfide + NADPH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.9 TrxR
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.9 0.243
-
 thioredoxin SeC498C mutant enzyme, human thioredoxin Rattus norvegicus
1.8.1.9 41.7
-
 thioredoxin wild-type enzyme, human thioredoxin Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.9 7
-
 wild-type enzyme Rattus norvegicus
1.8.1.9 9
-
 SeC498C mutant enzyme, broad optimum Rattus norvegicus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.8.1.9 4.2 10.5 wild-type and mutant Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 FAD
-
 Rattus norvegicus
1.8.1.9 NADPH
-
 Rattus norvegicus