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Glutaredoxin information


Glutaredoxin
Identifiers
SymbolGlutaredoxin
PfamPF00462
Pfam clanCL0172
InterProIPR002109
PROSITEPDOC00173
SCOP21kte / SCOPe / SUPFAM
OPM superfamily131
OPM protein1z9h
CDDcd02066
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Glutaredoxins[1][2][3] (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose metabolism.[4][5] Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Instead, glutaredoxins are reduced by the oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system.[6]

Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active centre disulfide bond.[7] It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulfide bond. Glutaredoxins function as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.[6] Moreover, GRX act in antioxidant defense by reducing dehydroascorbate, peroxiredoxins, and methionine sulfoxide reductase. Beside their function in antioxidant defense, bacterial and plant GRX were shown to bind iron-sulfur clusters and to deliver the cluster to enzymes on demand.[8]

  1. ^ Gleason FK, Holmgren A (December 1988). "Thioredoxin and related proteins in procaryotes". FEMS Microbiology Reviews. 54 (4): 271–97. doi:10.1111/j.1574-6968.1988.tb02747.x. PMID 3152490.
  2. ^ Holmgren A (April 1988). "Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds". Biochemical Society Transactions. 16 (2): 95–6. doi:10.1042/bst0160095. PMID 3286320.
  3. ^ Holmgren A (August 1989). "Thioredoxin and glutaredoxin systems". The Journal of Biological Chemistry. 264 (24): 13963–6. doi:10.1016/S0021-9258(18)71625-6. PMID 2668278.
  4. ^ Xing KY, Lou MF (December 2010). "Effect of age on the thioltransferase (glutaredoxin) and thioredoxin systems in the human lens". Investigative Ophthalmology & Visual Science. 51 (12): 6598–604. doi:10.1167/iovs.10-5672. PMC 3055771. PMID 20610843.
  5. ^ Berndt C, Lillig CH, Holmgren A (April 2008). "Thioredoxins and glutaredoxins as facilitators of protein folding". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Redox regulation of protein folding. 1783 (4): 641–50. doi:10.1016/j.bbamcr.2008.02.003. PMID 18331844.
  6. ^ a b Fernandes AP, Holmgren A (February 2004). "Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system". Antioxidants & Redox Signaling. 6 (1): 63–74. doi:10.1089/152308604771978354. PMID 14713336.
  7. ^ Foloppe N, Nilsson L (February 2004). "The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues". Structure. 12 (2): 289–300. doi:10.1016/j.str.2004.01.009. PMID 14962389.
  8. ^ Rouhier N, Lemaire SD, Jacquot JP (2008). "The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation" (PDF). Annual Review of Plant Biology. 59: 143–66. doi:10.1146/annurev.arplant.59.032607.092811. PMID 18444899.

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Glutaredoxin

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Glutaredoxins (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor...

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GLRX

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Glutaredoxin-1 is a protein that in humans is encoded by the GLRX gene. GLRX has been shown to interact with Wilson disease protein and ATP7A. GRCh38:...

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Glutathione

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electron donor. Other enzymes using glutathione as a substrate are glutaredoxins. These small oxidoreductases are involved in flower development, salicylic...

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Oxoglutarate dehydrogenase complex

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radicals, and can be undone after hydrogen peroxide consumption via glutaredoxin. Glutathionylation "protects" the lipoic acid of the E2 domain from undergoing...

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Intrinsically disordered proteins

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2021). "Intrinsically Disordered Region Modulates Ligand Binding in Glutaredoxin 1 from Trypanosoma Brucei". The Journal of Physical Chemistry B. 125...

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Glutathione disulfide

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hydroperoxides (ROOH): 2 GSH + ROOH → GSSG + ROH + H2O Other enzymes, such as glutaredoxins, generate glutathione disulfide through thiol-disulfide exchange with...

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Antioxidant

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ascorbate in the glutathione-ascorbate cycle, glutathione peroxidases and glutaredoxins, as well as reacting directly with oxidants. Due to its high concentration...

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Chloride channel

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conserved glutaredoxin monothiol motif, similar to the omega class GSTs. Al Khamici et al. demonstrated that CLIC proteins have glutaredoxin-like glutathione-dependent...

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Thioredoxin reductase

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and one in animals. In bacteria TrxR also catalyzes the reduction of glutaredoxin like proteins known as NrdH. Both classes are flavoproteins which function...

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List of enzymes

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Category:EC 1.20.2 Category:EC 1.20.4 Arsenate reductase (glutaredoxin) EC 1.20.4.1 Glutaredoxin Category:EC 1.20.9 Category:EC 1.20.99 Category:EC 1.21...

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Frenolicin B

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bacterium Streptomyces roseofulvus. Frenolicin B is a selective inhibitor of glutaredoxin 3 and peroxiredoxin 1. "Frenolicin B". Pubchem.ncbi.NLM.nih.gov. Bycroft...

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GRX

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GRX may refer to: Glutaredoxin, a family of enzymes GPRS Roaming Exchange, in mobile telephony Shimano GRX groupsets, bicycle components for gravel riding...

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RoGFP

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modified by redox enzymes such as glutaredoxin or thioredoxin. roGFP2 preferentially interacts with glutaredoxins and therefore reports the cellular...

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SH3BGRL3

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similarity to glutaredoxin 1 of E. coli, and all the three proteins are predicted to belong to thioredoxin-like protein family. Glutaredoxins (GRXs) are...

Word Count : 949

Persulfidation

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reducing agents such as glutathione, and proteins such as thioredoxin or glutaredoxin. M.R. Filipovic, Persulfidation (S-sulfhydration) and H2S. Handbook of...

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Thioredoxin

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electron donors to peroxidases and ribonucleotide reductase. The related glutaredoxins share many of the functions of thioredoxins, but are reduced by glutathione...

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Caspase 3

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AL, Jo H (February 2007). "Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced...

Word Count : 3392

GLRX2

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Glutaredoxin 2 (GLRX2) is an enzyme that in humans encoded by the GLRX2 gene. GLRX2, also known as GRX2, is a glutaredoxin family protein and a thiol-disulfide...

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Thioredoxin domain

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and function. Thioredoxin belongs to a structural family that includes glutaredoxin, glutathione peroxidase, bacterial protein disulfide isomerase DsbA,...

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GRXCR1

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Glutaredoxin domain-containing cysteine-rich protein 1 is a protein that in humans is encoded by the GRXCR1 gene. This gene is one of 60 loci associated...

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GLRX5

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Glutaredoxin 5, also known as GLRX5, is a protein which in humans is encoded by the GLRX5 gene located on chromosome 14. This gene encodes a mitochondrial...

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Stress granule

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RNA Export Mediator GLO1 Glyoxalase Glyoxalase GLRX3 GLRX3/Glutaredoxin 3/TNLX2 Glutaredoxin 3 GLUD1 GLUD1 Glutamate Dehydrogenase 1 GNB2 GNB2 Guanine...

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GLRX3

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Glutaredoxin-3 is a protein that in humans is encoded by the GLRX3 gene. GLRX3 has been shown to interact with PRKCQ. GRCh38: Ensembl release 89: ENSG00000108010...

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Arsenate reductase

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reductase (cytochrome c) Arsenate reductase (donor) Arsenate reductase (glutaredoxin) This set index page lists enzyme articles associated with the same name...

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