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Physiological functions of thioredoxin and thioredoxin reductase [PDF]

FEBS Journal, 2000
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 reductases, thioredoxin peroxidases (peroxiredoxins) and ...
Arne Holmgren, Elias Arnér
exaly   +3 more sources

Thioredoxin reductase [PDF]

FEBS Journal, 2000
The mammalian thioredoxin reductases (TrxRs) are a family of selenium-containing pyridine nucleotide-disulphide oxidoreductases with mechanistic and sequence identity, including a conserved -Cys-Val-Asn-Val-Gly-Cys- redox catalytic site, to glutathione reductases.
Katja Becker, M L Ludwig, Donna M Veine
exaly   +3 more sources

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Measurement of Thioredoxin and Thioredoxin Reductase

Current Protocols in Toxicology, 2005
AbstractThe thioredoxin system is ubiquitous, providing reducing equivalents to essential biosynthetic enzymes like ribonucleotide reductase. It is essential for cellular redox regulation, control of oxidative stress, and protection against oxidative damage.
E S, Arnér, A, Holmgren
openaire   +2 more sources

Thioredoxins and thioredoxin reductase in chloroplasts: A review

Gene, 2019
The chloroplastic thioredoxins (Trxs), a family of thiol-disulphide oxidoreductases, are reduced by either ferredoxin (Fd)-dependent Trx reductase (FTR) or reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent Trx reductase (NTR). Two Trx systems are present in chloroplasts including Trxs, Trx-like proteins, and reductase FTR and NTRC ...
Zhenhui Kang, Tong Qin, Zhiping Zhao
openaire   +2 more sources

Thioredoxin Superfamily and Thioredoxin‐Inducing Agents

Annals of the New York Academy of Sciences, 2002
Abstract: Mammalian thioredoxin (TRX) with redox‐active dithiol in the active site plays multiple roles in intracellular signaling and resistance against oxidative stress. TRX is induced by a variety of stresses including infectious agents as well as hormones and chemicals.
Kiichi, Hirota, Hajime, Nakamura, Hiroshi, Masutani, Junji, Yodoi   +3 more
openaire   +2 more sources

Thioredoxins in chloroplasts

Current Genetics, 2007
Thioredoxins (TRXs) are small disulfide oxidoreductases of ca. 12 kDa found in all free living organisms. In plants, two chloroplastic TRXs, named TRX f and TRX m, were originally identified as light dependent regulators of several carbon metabolism enzymes including Calvin cycle enzymes.
Lemaire SD, Michelet L, ZAFFAGNINI, MIRKO, Massot V, Issakidis Bourguet E.   +4 more
openaire   +3 more sources

Intron Position as an Evolutionary Marker of Thioredoxins and Thioredoxin Domains

Journal of Molecular Evolution, 1996
In contrast to prokaryotes, which typically possess one thioredoxin gene per genome, three different thioredoxin types have been described in higher plants. All are encoded by nuclear genes, but thioredoxins m and f are chloroplastic while thioredoxins h have no transit peptide and are probably cytoplasmic.
M, Sahrawy, V, Hecht, J, Lopez-Jaramillo, A, Chueca, Y, Chartier, Y, Meyer   +5 more
openaire   +2 more sources

Preparation and assay of mammalian thioredoxin and thioredoxin reductase

1999
Publisher Summary This chapter describes the preparation and assay of mammalian thioredoxin and thioredoxin reductase (TrxR). The amino acid sequences of mammalian TrxR revealed a strikingly high homology to glutathione reductase. 14,19 The conserved features of all the structural components of glutathione reductase are preserved in mammalian TrxR ...
E S, Arnér, L, Zhong, A, Holmgren
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Cytosolic, Mitochondrial Thioredoxins and Thioredoxin Reductases in Arabidopsis Thaliana

Photosynthesis Research, 2004
Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during the transition between light and dark phases.
Bréhélin, Claire, Laloi, Christophe, Setterdahl, Aaron, Knaff, David, Meyer, Yves   +4 more
openaire   +3 more sources