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SRP6082

Sigma-Aldrich

TRXB from Escherichia coli

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Sinónimos:

TRXR, Thioredoxin reductase

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

Escherichia coli

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

liquid

mol wt

34.6 kDa

packaging

pkg of 100 μg

NCBI accession no.

P0A9P4

shipped in

dry ice

storage temp.

−70°C

Gene Information

Escherichia coli ... TRXB(949054)

General description

Thioredoxin reductase (TrxR) is encoded by TRXB gene. TrxR is one of the member of flavoprotein family of pyridine nucleotide-disulphide oxidoreductases, which also includes lipoamide dehydrogenase, glutathione reductase and mercuric ion reductase. Escherichia coli TrxR is a 70-kDa homodimeric flavoprotein, each monomer of this protein contains a FAD prosthetic group, an NADPH domain and an active site with redox-active disulphide. The catalytic site (-Cys-Ala-Thr-Cys-) in Escherichia coli TrxB is localized on the NADPH domain, whereas in humans TrxB catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) is part of the FAD domain.[1][2]

Biochem/physiol Actions

Thioredoxin reductase (TRXB) catalyzes the reduction of oxidized thioredoxin using nicotinamide adenine dinucleotide phosphate (NADPH).[1][3] In thioredoxin pathway, this reduced thioredoxin reduce disulfide bonds in proteins localized in the cytoplasm and is implicated in the recycling of an essential enzyme ribonucleotide reductase. TrxR is essentially involved in protection against oxidation stress, cell growth and transformation, and the recycling of ascorbate from its oxidized form.[1]

Physical form

1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol and 1mM DTT.

Preparation Note

Centrifuge the vial prior to opening.

Other Notes

MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.

Pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H319

Hazard Classifications

Eye Irrit. 2

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Thioredoxin reductase
Debbie MUSTACICH and Garth POWIS
The Biochemical Journal, 346, 1-8 (2000)
Characterization of two active site mutations of thioredoxin reductase from Escherichia coli.
Prongay AJ
The Journal of Biological Chemistry, 264(5), 2656-2664 (1989)
E S Arnér et al.
European journal of biochemistry, 267(20), 6102-6109 (2000-09-30)
Thioredoxin, thioredoxin reductase and NADPH, the thioredoxin system, is ubiquitous from Archea to man. Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide

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