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Thioredoxin information


TXN
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTXN, TRDX, TRX, TRX1, thioredoxin, Trx80
External IDsOMIM: 187700; MGI: 98874; HomoloGene: 128202; GeneCards: TXN; OMA:TXN - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003329
NM_001244938

NM_011660

RefSeq (protein)

NP_001231867
NP_003320

NP_035790

Location (UCSC)Chr 9: 110.24 – 110.26 MbChr 4: 57.94 – 57.96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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, including redox signaling. In humans, thioredoxins are encoded by TXN and TXN2 genes.[5][6] Loss-of-function mutation of either of the two human thioredoxin genes is lethal at the four-cell stage of the developing embryo. Although not entirely understood, thioredoxin is linked to medicine through their response to reactive oxygen species (ROS). In plants, thioredoxins regulate a spectrum of critical functions, ranging from photosynthesis to growth, flowering and the development and germination of seeds. Thioredoxins play a role in cell-to-cell communication.[7]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000136810 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028367 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wollman EE, d'Auriol L, Rimsky L, Shaw A, Jacquot JP, Wingfield P, Graber P, Dessarps F, Robin P, Galibert F (October 1988). "Cloning and expression of a cDNA for human thioredoxin". The Journal of Biological Chemistry. 263 (30): 15506–12. doi:10.1016/S0021-9258(19)37617-3. PMID 3170595.
  6. ^ "Entrez Gene: TXN2 thioredoxin 2".
  7. ^ Meng L, Wong JH, Feldman LJ, Lemaux PG, Buchanan BB (February 2010). "A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication". Proceedings of the National Academy of Sciences of the United States of America. 107 (8): 3900–5. Bibcode:2010PNAS..107.3900M. doi:10.1073/pnas.0913759107. PMC 2840455. PMID 20133584.

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Thioredoxin

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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...

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Thioredoxin reductase

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Thioredoxin reductases (TR, TrxR) (EC 1.8.1.9) are enzymes that reduce thioredoxin (Trx). Two classes of thioredoxin reductase have been identified: one...

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Antioxidant

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chloroplasts. The thioredoxin system contains the 12-kDa protein thioredoxin and its companion thioredoxin reductase. Proteins related to thioredoxin are present...

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Thioredoxin domain

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Thioredoxins are small disulfide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general...

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Thioredoxin fold

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The thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical...

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T7 DNA polymerase

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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...

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Glycine reductase

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acetyl phosphate + NH3 + thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } glycine + phosphate + thioredoxin The 4 substrates of this...

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TXNIP

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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...

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Selenium

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is a component of the antioxidant enzymes glutathione peroxidase and thioredoxin reductase (which indirectly reduce certain oxidized molecules in animals...

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Sulfur

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December 2001). "Physiological functions of thioredoxin and thioredoxin reductase: Thioredoxin and thioredoxin reductase". European Journal of Biochemistry...

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Ribonucleotide reductase

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electrons donated from the dithiol groups of the protein thioredoxin. Regeneration of thioredoxin occurs when nicotinamide adenine dinucleotide phosphate...

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Betaine reductase

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phosphate + trimethylamine + thioredoxin disulfide ⇌ {\displaystyle \rightleftharpoons } N,N,N-trimethylglycine + phosphate + thioredoxin The 3 substrates of this...

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Sarcosine reductase

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phosphate + methylamine + thioredoxin disulfide ⇌ {\displaystyle \rightleftharpoons } N-methylglycine + phosphate + thioredoxin The 3 substrates of this...

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Glutathione

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potential Glutathione-ascorbate cycle Bacterial glutathione transferase Thioredoxin, a cysteine-containing small proteins with very similar functions as...

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TXNRD1

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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...

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Calvin cycle

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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;...

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SNARE protein

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reduction of this disulfide bond is mediated by the NADPH-thioredoxin reductase-thioredoxin system. The light chain of BoNT acts as a metalloprotease...

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Tetanus toxin

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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...

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Selenium in biology

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selenium-containing enzyme in some plants and in animals (thioredoxin reductase) generates reduced thioredoxin, a dithiol that serves as an electron source for...

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