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T7915

Sigma-Aldrich

Thioredoxin Reductase from Escherichia coli

ammonium sulfate suspension, >25 units/mg protein (Bradford)

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Synonym(s):
NADPH:oxidized thioredoxin oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.32

biological source

Escherichia coli

Quality Level

form

ammonium sulfate suspension

specific activity

>25 units/mg protein (Bradford)

mol wt

70 kDa

technique(s)

activity assay: suitable

UniProt accession no.

storage temp.

2-8°C

Gene Information

Escherichia coli K12 ... trxB(949054)

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vibrant-m

T0910

Thioredoxin from Escherichia coli

biological source

Escherichia coli

biological source

Escherichia coli

biological source

rat liver

biological source

Escherichia coli

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

Gene Information

Escherichia coli K12 ... trxB(949054)

Gene Information

Escherichia coli K12 ... trxA(948289)

Gene Information

rat ... Txnrd1(58819)

Gene Information

-

UniProt accession no.

P0A9P4

UniProt accession no.

P0AA25

UniProt accession no.

O89049

UniProt accession no.

-

mol wt

70 kDa

mol wt

11.7 kDa

mol wt

-

mol wt

-

Application

Thioredoxin Reductase from Escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of Cys-based thiol peroxidases. The product was used for determining the enzymatic activity of His6-Ahp1p.
Thioredoxin reductase from Escherichia coli has been used in thioredoxin reductase activity and peroxiredoxin assay.
It has also been used to study the synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes.

Biochem/physiol Actions

An FAD-containing enzyme involved in the transfer of hydrogen from E. coli thioredoxin to other proteins thus providing a powerful disulfide reductase system.
Thioredoxin reductase is a FAD containing enzyme, which transfers the reducing equivalent from NADPH to the disulphide bond of the enzyme by using FAD moiety within the Cys-Ala-Thr-Cys sequence. It can also reduce Trx-S2 to Trx-(SH)2 by using NADPH.
Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide.

Unit Definition

One unit will cause an increase in absorbance of 1.0 at 412 nm (when measured in a coupled assay with E. coli thioredoxin and DTNB) per min per mL at pH 7.0 at 25 °C.

Physical form

Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Purification and characterization of ferredoxin-NAD (P)+ reductase from the green sulfur bacterium Chlorobium tepidum
Seo D, et al.
Biochim. Biophys. Acta Gen. Subj., 1597(1), 123-132 (2002)
Valérie Prouzet-Mauléon et al.
The Journal of biological chemistry, 277(7), 4823-4830 (2001-11-24)
Yeasts lacking cytoplasmic superoxide dismutase (Cu,Zn-SOD) activity are permanently subjected to oxidative stress. We used two-dimensional PAGE to examine the proteome pattern of Saccharomyces cerevisiae strains lacking Cu,Zn-SOD. We found a new stable form of alkyl hydroperoxide reductase 1 (Ahp1)
Functional characterization of Clostridium difficile spore coat proteins
Permpoonpattana P, et al.
Journal of Bacteriology, JB-02104 (2013)
Synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes
Li D, et al.
Food Chemistry, 110(1), 193-198 (2008)
Thioredoxin and thioredoxin reductase.
A Holmgren et al.
Methods in enzymology, 252, 199-208 (1995-01-01)

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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