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Class of reduction–oxidation proteins
Thioredoxin (TRX or TXN) is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes
Thioredoxin
Class of enzymes
Thioredoxin reductases (TR, TrxR) (EC 1.8.1.9) are enzymes that reduce thioredoxin (Trx). Two classes of thioredoxin reductase have been identified: one
Thioredoxin_reductase
Compound that inhibits the oxidation of other molecules
chloroplasts. The thioredoxin system contains the 12 kDa protein thioredoxin and its companion thioredoxin reductase. Proteins related to thioredoxin are present
Antioxidant
Protein family
Ferredoxin-thioredoxin reductase EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] protein that plays an important
Ferredoxin-thioredoxin reductase
Ferredoxin-thioredoxin_reductase
Type of protein fold
The thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical
Thioredoxin_fold
Protein family
Thioredoxins are small disulfide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general
Thioredoxin_domain
Protein family
reduced non-enzymatically by glutathione. In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically
Glutaredoxin
Enzyme
Adenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.10) is an enzyme that catalyzes the chemical reaction AMP + sulfite + thioredoxin disulfide ⇌ {\displaystyle
Adenylyl-sulfate reductase (thioredoxin)
Adenylyl-sulfate_reductase_(thioredoxin)
Class of enzymes
from the dithiol groups of the protein thioredoxin or thioredoxin like proteins eg NrdH. Regeneration of thioredoxin occurs when nicotinamide adenine dinucleotide
Ribonucleotide_reductase
phosphate + methylamine + thioredoxin disulfide ⇌ {\displaystyle \rightleftharpoons } N-methylglycine + phosphate + thioredoxin The 3 substrates of this
Sarcosine_reductase
Enzyme
phosphate + trimethylamine + thioredoxin disulfide ⇌ {\displaystyle \rightleftharpoons } N,N,N-trimethylglycine + phosphate + thioredoxin The 3 substrates of this
Betaine_reductase
Mammalian protein found in Homo sapiens
Thioredoxin-interacting protein is a protein that in humans is encoded by the TXNIP gene. TXNIP has been shown to interact with Thioredoxin and ZBTB32
TXNIP
selenium-containing enzyme in some plants and in animals (thioredoxin reductase) generates reduced thioredoxin, a dithiol that serves as an electron source for
Selenium_in_biology
Chemical element with atomic number 34 (Se)
is a component of the antioxidant enzymes glutathione peroxidase and thioredoxin reductase (which indirectly reduce certain oxidized molecules in animals
Selenium
Protein-coding gene in the species Homo sapiens
Thioredoxin reductase 1, cytoplasmic is an enzyme that in humans is encoded by the TXNRD1 gene. This gene encodes a member of the family of pyridine nucleotide
TXNRD1
reductase (thioredoxin) (EC 1.8.4.8) is an enzyme that catalyzes the chemical reaction adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide ⇌
Phosphoadenylyl-sulfate reductase (thioredoxin)
Phosphoadenylyl-sulfate_reductase_(thioredoxin)
Class of enzymes
reaction: 3-mercaptopyruvic acid + reduced thioredoxin H2S pyruvic acid + oxidised thioredoxin The enzyme is of interest because it provides
3-mercaptopyruvate sulfurtransferase
3-mercaptopyruvate_sulfurtransferase
Topics referred to by the same term
L-methionine:oxidized-thioredoxin S-oxidoreductase may refer to: Methionine-S-oxide reductase L-methionine (S)-S-oxide reductase This disambiguation page
L-methionine:oxidized-thioredoxin S-oxidoreductase
L-methionine:oxidized-thioredoxin_S-oxidoreductase
reaction L-methionine + thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } L-methionine (R)-S-oxide + thioredoxin The 3 substrates of this
L-methionine (R)-S-oxide reductase
L-methionine_(R)-S-oxide_reductase
acetyl phosphate + NH3 + thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } glycine + phosphate + thioredoxin The 4 substrates of this
Glycine_reductase
reaction L-methionine + thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } L-methionine (S)-S-oxide + thioredoxin The 3 substrates of this
L-methionine (S)-S-oxide reductase
L-methionine_(S)-S-oxide_reductase
Type of protein
characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein
Selenoprotein
Use of related sequences to construct an ancestral-like gene
observations should be taken with caution. One example is the reconstruction of thioredoxin enzymes from up to 4 billion year old organisms. Whereas the chemical
Ancestral sequence reconstruction
Ancestral_sequence_reconstruction
Chemical element with atomic number 16 (S)
December 2001). "Physiological functions of thioredoxin and thioredoxin reductase: Thioredoxin and thioredoxin reductase". European Journal of Biochemistry
Sulfur
Protein-coding gene in humans
produce it. PRXL2B catalyzes the following reaction: thioredoxin + prostaglandin H2 thioredoxin disulfide + prostaglandin F2alpha while, AKR1C3
PRXL2B
reduction of their substrates. Examples of such proteins include thioredoxin, thioredoxin reductase, glutathione reductase, glutaredoxin, glutathione peroxidase
Thiol_oxidoreductase
PDC MEKA phosducin PDCL PhLP1 phosducin-like PDCL2 GCPHLP phosducin-like 2 PDCL3 PhLP2A phosducin-like 3 TXNDC9 PhLP3 thioredoxin domain containing 9
Phosducin_family
Ubiquitous antioxidant compound in living organisms
potential Glutathione-ascorbate cycle Bacterial glutathione transferase Thioredoxin, a cysteine-containing small protein with very similar functions to reducing
Glutathione
Light-independent reactions in photosynthesis
regulation systems at work when the cycle must be turned on or off: the thioredoxin/ferredoxin activation system, which activates some of the cycle enzymes;
Calvin_cycle
reductase, L-methionine:oxidized-thioredoxin S-oxidoreductase) is an enzyme with systematic name L-methionine:thioredoxin-disulfide S-oxidoreductase. This
Methionine-S-oxide_reductase
Protein-coding gene in the species Homo sapiens
Thioredoxin-related transmembrane protein 1 is a protein that in humans is encoded by the TMX1 gene. GRCh38: Ensembl release 89: ENSG00000139921 – Ensembl
TMX1
Selenium-containing amino acid
example glutathione peroxidases, tetraiodothyronine 5′ deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases, selenophosphate
Selenocysteine
Chemical compound
PGF2α. The synthase enzyme uses thioredoxin as its reducing agent. thioredoxin + prostaglandin H2 thioredoxin disulfide + prostaglandin
Prostaglandin_F2alpha
Protein family
reduction of this disulfide bond is mediated by the NADPH-thioredoxin reductase-thioredoxin system. The light chain of BoNT acts as a metalloprotease
SNARE_protein
Enzyme
existing ones. The T7 DNA polymerase requires a host factor, E. coli thioredoxin, in order to carry out its function. This helps stabilize the binding
T7_DNA_polymerase
Iron–sulfur proteins
with first four β-strands and two α-helices adopting a variant of the thioredoxin fold. UniProt categorizes these as the "2Fe2S Shethna-type ferredoxin"
Ferredoxin
Tube that connects a testicle to a vas deferens
glutathione-S-transferases, peroxiredoxins, superoxide dismutases, thioredoxin reductase and thioredoxins. Deficiencies in the availability of these antioxidant proteins
Epididymis
Swedish professor (born 1966)
cancer, with particular emphasis on the mammalian thioredoxin system and the selenoprotein thioredoxin reductase 1. Arnér is professor of biochemistry in
Elias_Arnér
chemical reaction thioredoxin + prostaglandin H2 thioredoxin disulfide + prostaglandin F2alpha This enzyme uses thioredoxin as a reducing
Prostamide/prostaglandin F2alpha synthase
Prostamide/prostaglandin_F2alpha_synthase
Proteinogenic amino acid
folded structure. Reduction of disulfinide protein can be done by thioredoxin or thioredoxin reductase. It common in secreted and membrane proteins that require
Cysteine
Family of transient receptor potential cation channels in animals
the membrane and TRPC5 channels are activated by extracellular reduced thioredoxin. It has long been proposed that TRPC channels underlie the calcium release
TRPC
Chemical compound
glutathione reductase (GR) and thioredoxin reductase (Trx1), and two mitochondrial enzymes, lipoamide dehydrogenase and thioredoxin reductase (Trx2), reduce
Lipoic_acid
Late day confusion syndrome common among dementia patients
decrease in neuron energy production and an increase in neuron damage. Thioredoxin reductase is an antioxidant that neutralizes oxidative free radicals
Sundowning
Chemical compound
lack catalase. Since the trypanosomatids also lack an equivalent of thioredoxin reductase, trypanothione reductase is the sole path that electrons can
Trypanothione
Protein-coding gene in the species Homo sapiens
Endoplasmic reticulum resident protein 44 (ERp44) also known as thioredoxin domain-containing protein 4 (TXNDC4) is a protein that in humans is encoded
ERP44
Protein-coding gene in the species Homo sapiens
Thioredoxin-like protein 1 is a protein that in humans is encoded by the TXNL1 gene. GRCh38: Ensembl release 89: ENSG00000091164 – Ensembl, May 2017 GRCm38:
TXNL1
Extremely potent neurotoxin
bond to separate thiols occurs, mainly by the enzyme NADPH-thioredoxin reductase-thioredoxin. The light chain is then free to cleave the Gln76-Phe77 bond
Tetanus_toxin
Class of enzymes
and bacterial homologues, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases. Four cysteine residues and one residue, which
Vitamin_K_epoxide_reductase
Chinese botanist
known for discovering a novel form of cellular communication in plants. Thioredoxin, while known to play an important role in biological processes such as
Ling_Meng
Protein-coding gene in the species Homo sapiens
exchange is catalyzed by the thioredoxin domain. The two domains are linked together by a flexible linker that allows the thioredoxin domain to first interact
QSOX1
Enzyme
In these organisms, glutathione reduction is performed by either the thioredoxin or the trypanothione system, respectively. Glutathione plays a key role
Glutathione_reductase
Protein-coding gene in the species Homo sapiens
Thioredoxin-like protein 4A is a protein that is encoded by the TXNL4A gene in humans. TXNL4A has been shown to interact with PQBP1. GRCh38: Ensembl release
TXNL4A
Proteins performing more than one function
antioxidant thioredoxin protein is another example of a moonlighting protein. Upon infection with the bacteriophage T7, E. coli thioredoxin forms a complex
Protein_moonlighting
Topics referred to by the same term
txn, abbreviation for Database transaction TXN (gene), a gene encoding Thioredoxin IATA code for Huangshan Tunxi International Airport, China ISO 639 code
TXN
Protein-coding gene in the species Homo sapiens
Biochemically, PRDX5 is a peroxidase that can use cytosolic or mitochondrial thioredoxins to reduce alkyl hydroperoxides or peroxynitrite with high rate constants
PRDX5
Category of polymers, in which the monomers are joined together by ester links
Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain". Applied Sciences. 11 (18): 8315. doi:10.3390/app11188315
Polyester
Poisoning caused by mercury chemicals
inhibition of selenoenzymes, such as thioredoxin reductase (IC50 = 9 nM). Although it has many functions, thioredoxin reductase restores vitamins C and E
Mercury_poisoning
Type of lectin
ricin and ricin A-chain immunotoxins by protein disulfide isomerase and thioredoxin reductase". Biochemical Pharmacology. 67 (9): 1721–1731. doi:10.1016/j
Ricin
Protein-coding gene in the species Homo sapiens
Thioredoxin, mitochondrial also known as thioredoxin-2 is a protein that in humans is encoded by the TXN2 gene on chromosome 22. This nuclear gene encodes
TXN2
Class of enzymes
and β-sheets (both parallel and antiparallel). The protein cofactor thioredoxin can provide the required reducing equivalents for the reaction in the
Adenylyl-sulfate_reductase
Species of virus
uses E. coli's endogenous thioredoxin, a REDOX protein, as a sliding DNA clamp during phage DNA replication (though thioredoxin normally has a different
T7_phage
Protein-coding gene in the species Homo sapiens
Thioredoxin domain-containing protein 2 is a protein that in humans is encoded by the TXNDC2 gene. GRCh38: Ensembl release 89: ENSG00000168454 – Ensembl
TXNDC2
Protein found in humans
D (Aug 1995). "Localization of TDPX1, a human homologue of the yeast thioredoxin-dependent peroxide reductase gene (TPX), to chromosome 13q12". Genomics
Peroxiredoxin_2
Swedish biochemist (1940–2020)
Holmgren's research pioneered the structure and function of thioredoxin and thioredoxin reductase and discovered glutaredoxins. His investigations clarified
Arne_Holmgren
Protein found in humans
Rhee SG, Jeang KT (December 1997). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation". The Journal of Biological Chemistry
Peroxiredoxin_1
Topics referred to by the same term
prescriptions (TRx), see Pharmaceutical marketing TRX, an identifier for Thioredoxin TRX System, suspension training Tun Razak Exchange, Kuala Lumpur, Malaysia
TRX
Protein-coding gene in humans
binding protein binding ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor identical protein binding purine nucleotide binding
RRM1
Structural element of proteins
expression. The reductive signaling activity is carried by the ferredoxin-thioredoxin system, channeling electrons from the light reactions of photosystem
Disulfide_(biochemistry)
Modifying a protein amino acid by adding sulfur
biological reducing agents such as glutathione, and proteins such as thioredoxin or glutaredoxin. M.R. Filipovic, Persulfidation (S-sulfhydration) and
Persulfidation
Chemical compound
Entamoeba histolytica, the protozoan agent of human amebiasis. Assays of thioredoxin reductase and transcriptional profiling suggest that the effect of auranofin
Auranofin
Medicated adhesive patch delivers medication into the skin
residues with a high affinity for Cu(I)). These residues are present in the thioredoxin; which is the solubilizing fusion partner conjugated to the 4RepCT protein
Dermal_patch
Coenzyme, notable for its synthesis and oxidation role
important role. This process is termed protein deCoAlation. Thioredoxin A and Thioredoxin-like protein (YtpP), two bacterial proteins, are shown to deCoAlate
Coenzyme_A
Chemical compounds containing sulfur and selenium
part of various peroxidase enzymes, such as glutathione peroxidase and thioredoxin reductase. They are formed by the oxidative coupling of selenocysteine
Selenosulfide
Chemical compound
fRmsr, however, catalyzes the reduction of free methionine-R-sulfoxide. Thioredoxin serves to recycle by reduction some of the methionine sulfoxide reductase
Methionine_sulfoxide
Chemical compound
Motexafin gadolinium (proposed tradename Xcytrin) is an inhibitor of thioredoxin reductase and ribonucleotide reductase. It has been proposed as a possible
Motexafin_gadolinium
British biochemist
protein kinases and they elucidated the unexpected roles of thioredoxin and thioredoxin reductase in protein synthesis. With Ruderman and Rosenthal,
Tim_Hunt
Chemical compound
ME, Hudemann C, Lillig CH (December 2005). "Thiol redox control via thioredoxin and glutaredoxin systems". Biochem. Soc. Trans. 33 (Pt 6): 1375–7. doi:10
Glutathione_disulfide
Protein found in humans
reference expression data Gene ontology Molecular function selenium binding thioredoxin-disulfide reductase activity oxidoreductase activity Cellular component
Selenoprotein_T
Protein-coding gene in the species Homo sapiens
HZ, Rhee SG, Jeang KT (Jan 1998). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation". J. Biol. Chem. 272 (49): 30952–61
PRDX4
Protein-coding gene in the species Homo sapiens
localized to the endoplasmic reticulum (ER) that contains an N-terminal thioredoxin-like domain. Functionally, TUSC3 has roles in N-linked glycosylation
TUSC3
Protein without a fixed 3D structure
simulation of the glutaredoxin 1 from Trypanosoma brucei. The globular thioredoxin fold is depicted in blue, while the disordered N-tail in green. According
Intrinsically disordered proteins
Intrinsically_disordered_proteins
Protein-coding gene in humans
oxidoreductase activity ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Cellular component mitochondrion nucleus nucleoplasm
RRM2B
Class of enzymes
active site of the enzyme. Reduction of this regulatory disulfide bond by thioredoxin incites a conformational change in the active site, activating the enzyme
Sedoheptulose-bisphosphatase
Species of fish
characterized in Channa striatus includes Chemokine, Chemokine receptors, Thioredoxin, Superoxide dismutase, Serine Protease, Cathepsin, Lectin. The Bathini
Channa_striata
Protein family
Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. Like other thioredoxin-based enzymes, DsbA's catalytic
DsbA
Protein-coding gene in the species Homo sapiens
Thioredoxin-dependent peroxide reductase, mitochondrial is an enzyme that in humans is encoded by the PRDX3 gene. It is a member of the peroxiredoxin
PRDX3
Species of bacterium
(19 March 2010). "Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum"
Treponema_pallidum
Protein-coding gene in the species Homo sapiens
Thioredoxin-like protein 4B is a protein that in humans is encoded by the TXNL4B gene. TXNL4B has been shown to interact with PRPF6. GRCh38: Ensembl release
TXNL4B
peptide-L-methionine + thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } peptide-L-methionine (R)-S-oxide + thioredoxin The 3 substrates of
Peptide-methionine (R)-S-oxide reductase
Peptide-methionine_(R)-S-oxide_reductase
Protein-coding gene in the species Homo sapiens
Thioredoxin domain-containing protein 5 is a protein that in humans is encoded by the TXNDC5 gene. This gene encodes a protein disulfide-isomerase. Its
TXNDC5
Class of enzymes
+ thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } peptide-L-methionine (S)-S-oxide + thioredoxin (2) L-methionine + thioredoxin disulfide
Peptide-methionine (S)-S-oxide reductase
Peptide-methionine_(S)-S-oxide_reductase
The following is a partial list of the "D" codes for Medical Subject Headings (MeSH), as defined by the United States National Library of Medicine (NLM)
List_of_MeSH_codes_(D12.776)
Family of enzymes
commonly used. The glutathione binding site, or "G-site", is located in the thioredoxin-like domain of both cytosolic and mitochondrial GSTs. The region containing
Glutathione_S-transferase
Family of antioxidant enzymes
enzyme classes. 2-Cys peroxiredoxins are reduced by thiols such as thioredoxins, thioredoxin-like proteins, or possibly glutathione, whereas the 1-Cys enzymes
Peroxiredoxin
Negative regulation (or limiting) of body weight and cell proliferation
overexpression of H19 positively regulates post-transcriptionally thioredoxin. Thioredoxin is a protein crucial to the reduction-oxidation reactions involved
H19_(gene)
Organic compounds containing amine and carboxylic groups
PMID 12775843. S2CID 10363908. Gromer S, Urig S, Becker K (January 2004). "The thioredoxin system--from science to clinic". Medicinal Research Reviews. 24 (1):
Amino_acid
Chemical compound
dithiolethione: Biochemical considerations". Biothiols Part B: Glutathione and Thioredoxin: Thiols in Signal Transduction and Gene Regulation. Methods in Enzymology
Anethole_trithione
thioredoxin 2'-oxidoreductase) is an enzyme with systematic name 2'-deoxyribonucleoside-triphosphate:thioredoxin-disulfide 2'-oxidoreductase
Ribonucleoside-triphosphate reductase
Ribonucleoside-triphosphate_reductase
Class of enzymes which convert a molecule between isomeric forms
through a single transmembrane helix, for example isomerases with the thioredoxin domain, and certain prolyl isomerases. Enzyme nomenclature, 1978 recommendations
Isomerase
Nucleotide containing ribose as its pentose component
requires two other proteins: thioredoxin and thioredoxin reductase. Ribonucleoside diphosphate (NDP) is reduced by thioredoxin to a deoxyribonucleoside diphosphate
Ribonucleotide
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THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
THIOREDOXIN
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