Experts and Doctors on glutathione synthase in Japan

Summary

Locale: Japan
Topic: glutathione synthase

Top Publications

  1. Momose Y, Iwahashi H. Bioassay of cadmium using a DNA microarray: genome-wide expression patterns of Saccharomyces cerevisiae response to cadmium. Environ Toxicol Chem. 2001;20:2353-60 pubmed
    ..Based on these results, we concluded that DNA microarrays are very useful instruments for creating new bioassay systems and finding genetic promoters of stress indicators. ..
  2. 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. ..
  3. 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. ..
  4. 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. ..
  5. 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. ..
  6. 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. ..
  7. 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. ..
  8. Inoue Y, Sugiyama K, Izawa S, Kimura A. Molecular identification of glutathione synthetase (GSH2) gene from Saccharomyces cerevisiae. Biochim Biophys Acta. 1998;1395:315-20 pubmed
    ..The GSH2 gene was not essential for growth of yeast cell, and glutathione was not detected from the gsh2 disrupter. ..
  9. Tsuboi S, Kiyono K, Ono B, Sakaue T, Ogata K. S-(1,2-Dicarboxyethyl)glutathione in yeast: partial purification of its synthesizing enzyme. Biol Pharm Bull. 1999;22:21-5 pubmed
    ..The enzyme had a pH optimum of 7.5. DCE-GS levels in yeast cells were significantly higher in aerobic cultures than in anaerobic ones. DCE-GS was synthesized in cells cultured between 20 and 35 degrees C...

More Information

Publications16

  1. 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) ..
  2. Mutoh N, Nakagawa C, Ando S, Tanabe K, Hayashi Y. Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe. Biochem Biophys Res Commun. 1991;181:430-6 pubmed
  3. Kato H, Yamaguchi H, Hata Y, Nishioka T, Katsube Y, Oda J. Crystallization and preliminary X-ray studies of glutathione synthetase from Escherichia coli B. J Mol Biol. 1989;209:503-4 pubmed
    ..0 A, c = 164.2 A, and gamma = 120 degrees. The enzyme is a tetramer (Mr = 143,000) with 222 symmetry, and the asymmetric unit contains one subunit molecule (Mr = 35,600). The crystals diffract to at least 2.5 A resolution. ..
  4. 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
    ..Replacement of Cys-122 to Ala-122 enhanced the reactivity of Cys-289 with sulfhydryl reagents. ..
  5. Kato H, Tanaka T, Yamaguchi H, Hara T, Nishioka T, Katsube Y, et al. Flexible loop that is novel catalytic machinery in a ligase. Atomic structure and function of the loopless glutathione synthetase. Biochemistry. 1994;33:4995-9 pubmed
    ..These studies support the fact that the loop enhances the recognition of glycine as well as stabilizes the acyl phosphate intermediate so that the intermediate rapidly reacts with glycine. ..
  6. 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. ..
  7. 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. ..