Glutaredoxin (GLRX)

GRX; GRX1; Thioltransferase

SPN	P769
HGNC	4330
MGI	2135625
PubMed	17172268
RGD	70951
UniProt	P35754
Wiki	Glutaredoxin

Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. Padilla et al. (1995) purified a human placental glutaredoxin to homogeneity and showed that its amino acid sequence was similar to that of other known mammalian glutaredoxins (about 80% identity), with some important differences. A cDNA that encodes the entire GRX open reading frame (ORF) and flanking sequences was isolated from a human spleen cDNA library. Glutaredoxin is a small protein of 12 kD. Using a genomic clone for fluorescence in situ hybridization, Padilla et al. (1996) mapped the GLRX gene to 5q14. This localization was in agreement with that arrived at by somatic cell hybrid analysis.

Reference

"Cloning and sequencing of the cDNA encoding human glutaredoxin."
Biochim. Biophys. Acta 1218:229-231(1994) [PubMed] [Europe PMC] [Abstract]

"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin."
Eur. J. Biochem. 227:27-34(1995) [PubMed] [Europe PMC] [Abstract]

"Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin."
Biochem. J. 315:931-938(1996) [PubMed] [Europe PMC] [Abstract]

"The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis."
Gene 197:189-193(1997) [PubMed] [Europe PMC] [Abstract]

"Human lens thioltransferase: cloning, purification, and function."
Invest. Ophthalmol. Vis. Sci. 42:743-751(2001) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells."
Protein Sci. 3:428-434(1994) [PubMed] [Europe PMC] [Abstract]

"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"The NMR solution structure of human glutaredoxin in the fully reduced form."
J. Mol. Biol. 280:687-701(1998) [PubMed] [Europe PMC] [Abstract]

"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 37:17145-17156(1998) [PubMed] [Europe PMC] [Abstract]