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Literature summary for 1.8.1.9 extracted from

  • Eckenroth, B.; Harris, K.; Turanov, A.A.; Gladyshev, V.N.; Raines, R.T.; Hondal, R.J.
    Semisynthesis and characterization of mammalian thioredoxin reductase (2006), Biochemistry, 45, 5158-5170.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli ER2566 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
U489C barely detectable activity towards thioredoxin and hydrogen peroxide Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.6
-
thioredoxin mutant enzyme U489C Mus musculus
6.6
-
hydrogen peroxide semisynthetic enzyme with 91% content of selenium Mus musculus
35
-
thioredoxin semisynthetic enzyme with 63% content of selenium Mus musculus
67.6
-
thioredoxin semisynthetic enzyme with 91% content of selenium Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q9JLT4
-
-

Purification (Commentary)

Purification (Comment) Organism
chitin resin column chromatography and DEAE anion exchange column chromatography Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thioredoxin + NADP+
-
Mus musculus thioredoxin disulfide + NADPH
-
?

Synonyms

Synonyms Comment Organism
thioredoxin reductase
-
Mus musculus
TR
-
Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
thioredoxin mutant enzyme U489C Mus musculus
1.183
-
hydrogen peroxide semisynthetic enzyme with 91% content of selenium Mus musculus
6.08
-
hydrogen peroxide semisynthetic enzyme with 91% content of selenium Mus musculus
25
-
thioredoxin semisynthetic enzyme with 63% content of selenium Mus musculus
37
-
thioredoxin semisynthetic enzyme with 91% content of selenium Mus musculus