Experts and Doctors on glutathione synthase in Japan
Topic: glutathione synthase
- 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) ..
- 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
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..