Disease relevance of GLRX1

• Recombinant pig liver thioltransferase expressed in Escherichia coli was crystallized in its oxidized form by vapor diffusion technique [1].
• Pig liver thioltransferase was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide [2].
• Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity [3].

High impact information on GLRX1

• The P. furiosus protein can reduce disulfide bonds in L-cystine in the presence of GSH (the thioltransferase activity) with an optimum pH of 8 [4].
• The amino acid sequence derived from the DNA sequence contains the CPYC sequence, which is typical of the active site of glutaredoxin (also called thioltransferase) [4].
• The active site cysteine of pig liver thioltransferase was identified as Cys22 [5].
• The complete amino acid sequence of pig liver thioltransferase has been determined [6].
• The sequence of pig liver thioltransferase displays close homology (82%) with calf thymus glutaredoxin, suggesting that they belong to the same evolutionary family [6].

Biological context of GLRX1

• Identification and reactivity of the catalytic site of pig liver thioltransferase [5].
• The TT cDNA was obtained by screening a commercial (Clonetech) pig liver cDNA library in lambda gt11, using polyclonal antibodies raised in rabbits against pig liver TT [7].
• Induction of thioltransferase and thioredoxin/thioredoxin reductase systems in cultured porcine lenses under oxidative stress [8].
• 0. The plots of thioltransferase activity as a function of S-sulfocysteine, 2-hydroxyethyl disulfide, and reduced glutathione concentrations did not display Michaelis-Menten kinetics [9].

Anatomical context of GLRX1

• TTase was absent in the vitreous body [10].
• RESULTS: Among all the ocular tissues tested, iris showed the highest TTase activity (35 mU/mg protein) followed by conjunctiva, corneal epithelial cells, and corneal endothelial cells [10].
• Characterization and partial purification of a cytoplasmic glutathione: disulfide oxidoreductase (thioltransferase) from adenohypophysis [11].
• A glutathione-dependent thioltransferase (thiol : disulfide oxidoreductase) has been partially purified (70-fold) from anterior pituitary cytosol, and characterized [11].

Associations of GLRX1 with chemical compounds

• Pig liver thioltransferase is a single polypeptide with 105 amino acid residues and an acetylated glutamine N terminus [6].
• This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase [3].
• This study suggests that thioltransferase (glutaredoxin) plays a significant role in the cytotoxicity of alloxan in vulnerable tissues [3].
• These GSTs have poor activity with common GST substrates, but exhibit novel glutathione-dependent thioltransferase, dehydroascorbate reductase and monomethylarsonate reductase activities, and modulate Ca release by ryanodine receptors [12].
• When thioltransferase was not reduced, inhibition by preincubation with the platinum complexes required molar excesses of 1,300 and 675 to one for cis-platin and trans-platin, respectively or 400-500 microM for 50% inhibition [13].

Other interactions of GLRX1

• The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin) [14].

Analytical, diagnostic and therapeutic context of GLRX1

• We report here the first three-dimensional structure of a mammalian thioltransferase as determined by single crystal X-ray crystallography at 2.2 A resolution [1].
• Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis [15].
• The selected peptides purified by reversed phase high performance liquid chromatography or ion exchange fast protein liquid chromatography were subjected to reaction with the polyclonal antibodies against pig liver thioltransferase [2].

References