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生物来源
Escherichia coli
重组
expressed in E. coli
方案
≥90% (SDS-PAGE)
表单
liquid
分子量
34.6 kDa
包装
pkg of 100 μg
NCBI登记号
运输
dry ice
储存温度
−70°C
基因信息
Escherichia coli ... TRXB(949054)
一般描述
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.
生化/生理作用
Thioredoxin reductase (TRXB) catalyzes the reduction of oxidized thioredoxin using nicotinamide adenine dinucleotide phosphate (NADPH). 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.
外形
1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol and 1mM DTT.
制备说明
Centrifuge the vial prior to opening.
其他说明
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.
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Characterization of two active site mutations of thioredoxin reductase from Escherichia coli.
Prongay AJ
The Journal of Biological Chemistry, 264(5), 2656-2664 (1989)
Thioredoxin reductase
Debbie MUSTACICH and Garth POWIS
The Biochemical Journal, 346, 1-8 (2000)
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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