PMID:11012661

Citation	Arnér, ES and Holmgren, A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267:6102-9
Abstract	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 methionine sulfoxide reductases. Glutaredoxins catalyze glutathione-disulfide oxidoreductions overlapping the functions of thioredoxins and using electrons from NADPH via glutathione reductase. Thioredoxin isoforms are present in most organisms and mitochondria have a separate thioredoxin system. Plants have chloroplast thioredoxins, which via ferredoxin-thioredoxin reductase regulates photosynthetic enzymes by light. Thioredoxins are critical for redox regulation of protein function and signaling via thiol redox control. A growing number of transcription factors including NF-kappaB or the Ref-1-dependent AP1 require thioredoxin reduction for DNA binding. The cytosolic mammalian thioredoxin, lack of which is embryonically lethal, has numerous functions in defense against oxidative stress, control of growth and apoptosis, but is also secreted and has co-cytokine and chemokine activities. Thioredoxin reductase is a specific dimeric 70-kDa flavoprotein in bacteria, fungi and plants with a redox active site disulfide/dithiol. In contrast, thioredoxin reductases of higher eukaryotes are larger (112-130 kDa), selenium-dependent dimeric flavoproteins with a broad substrate specificity that also reduce nondisulfide substrates such as hydroperoxides, vitamin C or selenite. All mammalian thioredoxin reductase isozymes are homologous to glutathione reductase and contain a conserved C-terminal elongation with a cysteine-selenocysteine sequence forming a redox-active selenenylsulfide/selenolthiol active site and are inhibited by goldthioglucose (aurothioglucose) and other clinically used drugs.
Links	PubMed
Keywords	Amino Acid Sequence; Animals; Base Sequence; Humans; Signal Transduction; Thioredoxin-Disulfide Reductase/chemistry; Thioredoxin-Disulfide Reductase/genetics; Thioredoxin-Disulfide Reductase/metabolism; Thioredoxins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
9CAUD:A0A024AZS4		GO:0004748: ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	ECO:0000314:		F		This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One of its functions in nearly all organisms is DNA synthesis. "Thioredoxin is a hydrogen donor for ribonucleotide reductase"	complete CACAO 11637
9CAUD:A0A024AZS4		GO:0004791: thioredoxin-disulfide reductase activity	ECO:0000314:		F		This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One of its roles in all organisms is protein disulfide reduction. "Thioredoxin is a key player in keeping intracellular protein disulfides generally reduced."	complete CACAO 11640
9CAUD:A0A024AZS4		GO:0008379: thioredoxin peroxidase activity	ECO:0000314:		F		This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One function that it does in many organisms is the reduction of hydrogen peroxide. "oxidative stress and apoptosis induction, require reduction by thioredoxin"	complete CACAO 11642
9CAUD:A0A024AZS4		GO:0033745: L-methionine-(R)-S-oxide reductase activity	ECO:0000314:		F		This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One function it does in many organisms is repairing proteins. "Thioredoxin is hydrogen donor for methionine sulfoxide reductases".	complete CACAO 11646

References

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