Genomes and Genes
Gene Symbol: gshB
Description: glutathione synthetase
Alias: ECK2942, JW2914, gsh-II
Species: Escherichia coli str. K-12 substr. MG1655
- Gushima H, Miya T, Murata K, Kimura A. Construction of glutathione-producing strains of Escherichia coli B by recombinant DNA techniques. J Appl Biochem. 1983;5:43-52 pubmed..About 5 mg/ml of glutathione was produced by E. coli cells with pGS500 from 80 mM L-glutamate, 20 mM L-cysteine, and 20 mM glycine within 3 h at 37 degrees C. ..
- Gushima H, Yasuda S, Soeda E, Yokota M, Kondo M, Kimura A. Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II. Nucleic Acids Res. 1984;12:9299-307 pubmed..These structural features found in the non-coding regions have suggested to be involved in regulatory functions for the gsh-II gene expression. ..
- Apontoweil P, Berends W. Isolation and initial characterization of glutathione-deficient mutants of Escherichia coli K 12. Biochim Biophys Acta. 1975;399:10-22 pubmed..It must be concluded that the protective role of glutathione is only significant when a chemical challenge is present. ..
- Faulkner M, Veeravalli K, Gon S, Georgiou G, Beckwith J. Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways. Proc Natl Acad Sci U S A. 2008;105:6735-40 pubmed publisher..Proteins most effectively oxidized vary between strains, potentially providing useful tools for expressing different disulfide-bonded proteins. ..
- Shen L, Wei D, Zhao Z, Zhang S, Wang E. [Cloning and expression of the genes of glutathione synthetases]. Sheng Wu Gong Cheng Xue Bao. 2001;17:98-100 pubmed..7 after the addition of 0.1 mmol/L IPTG. The expressed products were up to 25% of the total protein of the bacteria. Acetone-treated cells of the engineered strain could synthesize GSH efficiently. ..
- Tanaka T, Yamaguchi H, Kato H, Nishioka T, Katsube Y, Oda J. Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase. Biochemistry. 1993;32:12398-404 pubmed..The present results suggest that adjustability of the loop to the closed state is required for the recognition of the substrates, gamma-Glu-Cys and glycine, and for the chemical interactions with the bound substrates. ..
- Fan C, Moews P, Shi Y, Walsh C, Knox J. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Proc Natl Acad Sci U S A. 1995;92:1172-6 pubmed
- Kato H, Chihara M, Nishioka T, Murata K, Kimura A, Oda J. Homology of Escherichia coli B glutathione synthetase with dihydrofolate reductase in amino acid sequence and substrate binding site. J Biochem. 1987;101:207-15 pubmed..coli B enzyme provides the ATP binding site. This report gives experimental evidence that amino acid sequences related by sequence homology conserve functional similarity even in enzymes which differ in their catalytic mechanisms. ..
- Yamaguchi H, Kato H, Hata Y, Nishioka T, Kimura A, Oda J, et al. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution. J Mol Biol. 1993;229:1083-100 pubmed..The ATP binding site is surrounded by two sets of the structural motif that belong to those respective domains. Each motif consists of an anti-parallel beta-sheet and a glycine-rich loop. ..
- Toledano M, Kumar C, Le Moan N, Spector D, Tacnet F. The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis. FEBS Lett. 2007;581:3598-607 pubmed..We show that although prokaryotic and eukaryotic systems have a similar architecture, they profoundly differ in their overall cellular functions. ..
- Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J. Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Protein Eng. 1996;9:1083-92 pubmed..A structural motif in the N-terminal domain of GSHase has been found to be similar to the NAD-binding fold. This structural motif is shared by a number of other proteins that bind various negatively charged molecules. ..
- Helbig K, Grosse C, Nies D. Cadmium toxicity in glutathione mutants of Escherichia coli. J Bacteriol. 2008;190:5439-54 pubmed publisher..General energy conservation pathways and iron uptake were down-regulated. These findings indicated that the toxic action of Cd(2+) indeed results from the binding of the metal cation to sulfur, lending support to the hypothesis tested. ..
- Tanaka T, Nishioka T, Oda J. Nicked multifunctional loop of glutathione synthetase still protects the catalytic intermediate. Arch Biochem Biophys. 1997;339:151-6 pubmed..In conclusion, it is postulated that the two fragments of the nicked loop independently assumed the closed state to protect the catalytic intermediate and have lost the ability to accelerate glutathione synthesis. ..
- Tanaka T, Kato H, Nishioka T, Oda J. Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction. Biochemistry. 1992;31:2259-65 pubmed..These results suggest that the loop covers the active site while ATP and gamma-Glu-Cys bind there and that it protects the unstable gamma-Glu-Cys phosphate intermediate from decomposition by bulk water.(ABSTRACT TRUNCATED AT 250 WORDS) ..
- Apontoweil P, Berends W. Glutathione biosynthesis in Escherichia coli K 12. Properties of the enzymes and regulation. Biochim Biophys Acta. 1975;399:1-9 pubmed..The pathway is controlled by feedback inhibition and not by repression. ..
- Hibi T, Kato H, Nishioka T, Oda J, Yamaguchi H, Katsube Y, et al. Use of adenosine (5')polyphospho(5')pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B. Biochemistry. 1993;32:1548-54 pubmed..These results demonstrate the bivalent binding of AP4-PL lying across the gamma-glutamylcysteine- and ATP-binding sites. ..
- Hara T, Tanaka T, Kato H, Nishioka T, Oda J. Site-directed mutagenesis of glutathione synthetase from Escherichia coli B: mapping of the gamma-L-glutamyl-L-cysteine-binding site. Protein Eng. 1995;8:711-6 pubmed..The other mutant enzymes showed little defect in their kinetic parameters of gamma-Glu-Cys. ..
- Gushima H, Miya T, Murata K, Kimura A. Purification and characterization of glutathione synthetase from Escherichia coli B. J Appl Biochem. 1983;5:210-8 pubmed..5 and at 45 degrees C and required divalent cations such as Mg2+, Mn2+, and Co2+ for activity. The activity was inhibited by oxidized glutathione (Ki = 4.4 mM). Reduced glutathione showed no effect on glutathione synthetase activity. ..
- Junkins A, Doyle M. Demonstration of exopolysaccharide production by enterohemorrhagic Escherichia coli. Curr Microbiol. 1992;25:9-17 pubmed..E. coli O157:H7 adheres better to INT 407 cells when grown under conditions that favor high EPS production than when grown under conditions that repress EPS production. ..
- Inoue Y, Sugiyama K, Ueminami H, Izawa S, Kimura A. Modification of Escherichia coli B glutathione synthetase with polyethylene glycol for clinical application to enzyme replacement therapy for glutathione deficiency. Clin Diagn Lab Immunol. 1996;3:663-8 pubmed..For the native enzyme, strong reactions such as dyspnea and tumble were observed; however, no symptom or only a very weak reaction, such as scratching, was observed with the modified enzyme. ..
- Helbig K, Bleuel C, Krauss G, Nies D. Glutathione and transition-metal homeostasis in Escherichia coli. J Bacteriol. 2008;190:5431-8 pubmed publisher..Thus, GSH may play an important role in trace-element metabolism not only in higher organisms but also in bacteria. ..
- Smirnova G, Muzyka N, Oktyabrsky O. Effects of cystine and hydrogen peroxide on glutathione status and expression of antioxidant genes in Escherichia coli. Biochemistry (Mosc). 2005;70:926-34 pubmed..The high toxicity of H2O2 in the presence of cystine resulted in disorders of membrane functions and inhibition of the expression of genes including those responsible for neutralization of oxidants and DNA repair. ..
- Hara T, Kato H, Katsube Y, Oda J. A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution. Biochemistry. 1996;35:11967-74 pubmed..Functional aspects of the active site architecture in the substrate-binding form are discussed. ..
- Hibi T, Nishioka T, Kato H, Tanizawa K, Fukui T, Katsube Y, et al. Structure of the multifunctional loops in the nonclassical ATP-binding fold of glutathione synthetase. Nat Struct Biol. 1996;3:16-8 pubmed
- Moore W, Meister A. Enzymatic synthesis of novel glutathione analogs. Anal Biochem. 1987;161:487-93 pubmed..Fluorine-containing analogs may be used for NMR studies. The enzymatically prepared compounds may also be used as intermediates in the chemical synthesis of other analogs of glutathione and glutathione disulfide. ..
- Fuchs J, Warner H. Isolation of an Escherichia coli mutant deficient in glutathione synthesis. J Bacteriol. 1975;124:140-8 pubmed..This suggests that one role of glutathione in the cell is to maintain at least this one protein in an active state. We propose the designation gshB for the gene coding for glutathione synthetase.
- Harrop H, Held K, Michael B. The oxygen effect: variation of the K-value and lifetimes of O2-dependent damage in some glutathione-deficient mutants of Escherichia coli. Int J Radiat Biol. 1991;59:1237-51 pubmed..coli strains varied approximately in proportion to the O2 K-values, and both the rates of chemical repair and the K-values correlated approximately with the levels of non-protein sulphydryls in the various strains. ..
- Kato H, Tanaka T, Nishioka T, Kimura A, Oda J. Role of cysteine residues in glutathione synthetase from Escherichia coli B. Chemical modification and oligonucleotide site-directed mutagenesis. J Biol Chem. 1988;263:11646-51 pubmed..containing 3, 2, or no cysteine residues/subunit by replacement of cysteine codons with those of alanine in the gsh II gene using site-directed mutagenesis...