GLRX

Glutaredoxin (thioltransferase)

PDB rendering based on 1b4q.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1B4Q, 1JHB, 4RQR

Identifiers

Symbols

GLRX ; GRX; GRX1

External IDs

OMIM: 600443 MGI: 2135625 HomoloGene: 37566 GeneCards: GLRX Gene

EC number

1.8.4.1

Gene ontology
Molecular function	• electron carrier activity • glutathione disulfide oxidoreductase activity • protein N-terminus binding • glutathione oxidoreductase activity
Cellular component	• nucleus • mitochondrion • cytosol • extracellular exosome
Biological process	• nucleobase-containing small molecule interconversion • small molecule metabolic process • cell redox homeostasis • positive regulation of membrane potential • nucleobase-containing small molecule metabolic process • oxidation-reduction process • protein deglutathionylation • positive regulation of sodium ion transmembrane transporter activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
95.75 – 95.82 Mb

Chr 13:
75.84 – 75.85 Mb

PubMed search

Glutaredoxin-1 is a protein that in humans is encoded by the GLRX gene.^[1]^[2]

Interactions

GLRX has been shown to interact with Wilson disease protein^[3] and ATP7A.^[3]

References

↑ Padilla CA, Bajalica S, Lagercrantz J, Holmgren A (Feb 1997). "The gene for human glutaredoxin (GLRX) is localized to human chromosome 5q14". Genomics 32 (3): 455–7. doi:10.1006/geno.1996.0141. PMID 8838810.
↑ "Entrez Gene: GLRX glutaredoxin (thioltransferase)".
1 2 Lim, Chris M; Cater Michael A; Mercer Julian F B; La Fontaine Sharon (Sep 2006). "Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases". Biochem. Biophys. Res. Commun. (United States) 348 (2): 428–36. doi:10.1016/j.bbrc.2006.07.067. ISSN 0006-291X. PMID 16884690.

Lou MF (2003). "Redox regulation in the lens.". Progress in retinal and eye research 22 (5): 657–82. doi:10.1016/S1350-9462(03)00050-8. PMID 12892645.
Sykes MC, Mowbray AL, Jo H (2007). "Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death.". Circ. Res. 100 (2): 152–4. doi:10.1161/01.RES.0000258171.08020.72. PMID 17272816.
Padilla CA, Martínez-Galisteo E, Bárcena JA; et al. (1995). "Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.". Eur. J. Biochem. 227 (1-2): 27–34. doi:10.1111/j.1432-1033.1995.tb20356.x. PMID 7851394.
Bandyopadhyay S, Gronostajski RM (1994). "Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins.". J. Biol. Chem. 269 (47): 29949–55. PMID 7961993.
Fernando MR, Sumimoto H, Nanri H; et al. (1994). "Cloning and sequencing of the cDNA encoding human glutaredoxin.". Biochim. Biophys. Acta 1218 (2): 229–31. doi:10.1016/0167-4781(94)90019-1. PMID 8018729.
Papov VV, Gravina SA, Mieyal JJ, Biemann K (1994). "The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells.". Protein Sci. 3 (3): 428–34. doi:10.1002/pro.5560030307. PMC 2142694. PMID 8019414.
Padilla CA, Spyrou G, Holmgren A (1996). "High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein.". FEBS Lett. 378 (1): 69–73. doi:10.1016/0014-5793(95)01413-6. PMID 8549805.
Park JB, Levine M (1996). "Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin.". Biochem. J. 315. ( Pt 3): 931–8. PMC 1217296. PMID 8645179.
Davis DA, Newcomb FM, Starke DW; et al. (1997). "Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro.". J. Biol. Chem. 272 (41): 25935–40. doi:10.1074/jbc.272.41.25935. PMID 9325327.
Park JB, Levine M (1997). "The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis.". Gene 197 (1-2): 189–93. doi:10.1016/S0378-1119(97)00262-X. PMID 9332366.
Bandyopadhyay S, Starke DW, Mieyal JJ, Gronostajski RM (1998). "Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I.". J. Biol. Chem. 273 (1): 392–7. doi:10.1074/jbc.273.1.392. PMID 9417094.
Sun C, Berardi MJ, Bushweller JH (1998). "The NMR solution structure of human glutaredoxin in the fully reduced form.". J. Mol. Biol. 280 (4): 687–701. doi:10.1006/jmbi.1998.1913. PMID 9677297.
Yang Y, Jao S, Nanduri S; et al. (1999). "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.". Biochemistry 37 (49): 17145–56. doi:10.1021/bi9806504. PMID 9860827.
Balijepalli S, Tirumalai PS, Swamy KV; et al. (1999). "Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization.". J. Neurochem. 72 (3): 1170–8. doi:10.1046/j.1471-4159.1999.0721170.x. PMID 10037490.
Barrett WC, DeGnore JP, König S; et al. (1999). "Regulation of PTP1B via glutathionylation of the active site cysteine 215.". Biochemistry 38 (20): 6699–705. doi:10.1021/bi990240v. PMID 10350489.
García-Pardo L, Granados MD, Gaytán F; et al. (1999). "Immunolocalization of glutaredoxin in the human corpus luteum.". Mol. Hum. Reprod. 5 (10): 914–9. doi:10.1093/molehr/5.10.914. PMID 10508218.
Mallis RJ, Poland BW, Chatterjee TK; et al. (2000). "Crystal structure of S-glutathiolated carbonic anhydrase III.". FEBS Lett. 482 (3): 237–41. doi:10.1016/S0014-5793(00)02022-6. PMID 11024467.
Balijepalli S, Boyd MR, Ravindranath V (2001). "Human brain thioltransferase: constitutive expression and localization by fluorescence in situ hybridization.". Brain Res. Mol. Brain Res. 85 (1-2): 123–32. doi:10.1016/S0169-328X(00)00206-0. PMID 11146114.
Qiao F, Xing K, Liu A; et al. (2001). "Human lens thioltransferase: cloning, purification, and function.". Invest. Ophthalmol. Vis. Sci. 42 (3): 743–51. PMID 11222536.

PDB gallery

1b4q: SOLUTION STRUCTURE OF HUMAN THIOLTRANSFERASE COMPLEX WITH GLUTATHIONE

1jhb: HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase

This article is issued from Wikipedia - version of the Wednesday, May 06, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

GLRX

Interactions

References

Further reading