Biochemical and Biophysical Research Communications
Characterization of cysteine residues of glutathione S-transferase P : Evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47
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2015, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Cys-47 and cys-101 are accessible because these residues are located close to the GSH-binding site and at the surface of the dimeric protein [29,30], respectively, whereas cys-14 is considered somewhat less accessible due its presence in a hydrophobic region of the protein [26]. Modification of these cysteines was observed by reactive intermediates of MFA and the electrophile MCB in this work, and by a wide variety of chemically reactive compounds in other studies [11,12,23,26–29,31–33]. Bioactivation of APAP by CYP102A1M11H or HLMs was reported to result in modification of cys-47 of hGST P1-1 [11,13,23].
Modulating Catalytic Activity by Unnatural Amino Acid Residues in a GSH-Binding Loop of GST P1-1
2008, Journal of Molecular BiologyChemical modification at subunit 1 of rat kidney Alpha class glutathione transferase with 2,3,5,6-tetrachloro-1,4-benzoquinone: Close structural connectivity between glutathione conjugation activity and non-substrate ligand binding
2006, Biochemical PharmacologyCitation Excerpt :Crystallographic B factors suggest that α-helix 1 is the least flexible part of subunits 1 and 4 [14,15,19]. Site-directed mutagenesis and chemical modification have previously been used to probe the roles of cysteines in GSTs [20–22] (reviewed in Ref. [23]). Modification of Alpha class GST 2-2 by N-ethyl maleimide (NEM) resulted in partial inactivation but did not affect GST 1-2.
Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site
2004, Journal of Biological ChemistryCitation Excerpt :Kinetic Properties of Mutant Enzymes—Because the affinity labeling study points to Tyr103 as the residue responsible for inactivation toward BITC as substrate, mutant enzymes were constructed with substitutions at position 103 to provide insights into the role of this residue in catalysis. Nishihira et al. (39), Park et al. (14), and Ricci et al. (40) have previously studied mutant enzymes with replacements for Cys47; therefore, this residue was not studied further. Because Tyr103 has both an aromatic and a hydroxyl group, two mutants were constructed as follows: Y103F, to retain the aromatic moiety while eliminating the hydroxyl group, and Y103S, to retain the hydroxyl group while eliminating the aromatic component.
Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone
2002, Journal of Biological ChemistryCitation Excerpt :Electrophoresis was performed at a polyacrylamide concentration of 12.5% in the presence of 0.1% SDS. In cases (see Figs. 1 and 2) where fine separation of proteins smaller than 20 kDa was required, the Tris-Tricine system at a polyacrylamide concentration of 10% was employed (39). Separated proteins were stained with Coomassie Brilliant Blue.