[1] Hopkins F G. On glutathione: a reinvestigation. J Biol Chem, 1929, 84(1): 269-320.
[2] Kendall E C, McKenzie B F, Mason H L. A study of glutathione. Its preparation in crystalline form and its identification. J Biol Chem, 1929, 84(2): 657-674.
[3] Kaplowitz N, Aw T Y, Ookhtens M. The regulation of hepatic glutathione. Annu Rev Pharmacol Toxicol, 1985, 25(1): 715-744.
[4] Carmel-Harel O, Storz G. Roles of the glutathione and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu Rev Microbiol, 2000, 54(1): 439-461.
[5] Penninckx M J. An overview on glutathione in Saccharomyces versus non-conventional yeasts. FEMS Yeast Res, 2002, 2(3): 295-305.
[6] Meister A, Tate S S. Glutathione and related γ-glutamyl compounds: biosynthesis and utilization. Annu Rev Biochem, 1976, 45(1): 559-604.
[7] Meister A, Anderson M E. Glutathione. Annu Rev Biochem, 1983, 52(1): 711-760.
[8] Jones D P. Redefining oxidative stress. Antioxid Redox Signal, 2006, 8(9-10): 1865-1879.
[9] Bock K W, Lilienblum W, Fischer G, et al. The role of conjugation reactions in detoxication. Arch Toxicol, 1987, 60(1-3): 22-29.
[10] Ketterer B, Coles B, Meyer D J. The role of glutathione in detoxication. Environ Health Perspect, 1983, 49: 59.
[11] Orlowski M, Meister A. The γ-glutamyl cycle: a possible transport system for amino acids. Proc Natl Acad Sci U S A, 1970, 67(3): 1248-1255.
[12] Pallardó F V, Markovic J, García J L, et al. Role of nuclear glutathione as a key regulator of cell proliferation. Mol Aspects Med, 2009, 30(1): 77-85.
[13] Hall A G. The role of glutathione in the regulation of apoptosis. Eur J Clin Invest, 1999, 29(3): 238-245.
[14] Liu R M, Gaston Pravia K A. Oxidative stress and glutathione in TGF-β-mediated fibrogenesis. Free Radic Biol Med, 2010, 48(1): 1-15.
[15] Forman H J, Fukuto J M, Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol, 2004, 287(2): C246-256.
[16] Chen L, Patel R P, Teng X, et al. Mechanisms of cystic fibrosis transmembrane conductance regulator activation by S-nitrosoglutathione. J Biol Chem, 2006, 281(14): 9190-9199.
[17] Dröge W, Breitkreutz R. Glutathione and immune function. Proc Nutr Soc, 2000, 59(4): 595-600.
[18] Hopkins F G. On an autoxidisable constituent of the cell. Biochem J, 1921, 15(2): 286-305.
[19] Harington C R, Mead T H. Synthesis of glutathione. Biochem J, 1935, 29(7): 1602-1611.
[20] Soomets U, Zilmer M, Langel U. Manual solid-phase synthesis of glutathione analogs: a laboratory-based short course. Methods Mol Biol, 2005, 298:241-257.
[21] Bloch K. The synthesis of glutathione in isolated liver. J Biol Chem, 1949, 179(3): 1245-1254.
[22] Richman PG, Meister A. Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione. J Biol Chem, 1975, 250(4): 1422-1426.
[23] Copley S D, Dhillon J K. Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes. Genome Biol, 2002, 3(5): 1-16.
[24] Meister A. Glutathione metabolism and its selective modification. J Biol Chem, 1988, 263(33): 17205-17208.
[25] Yan N, Meister A. Amino acid sequence of rat kidney gamma-glutamylcysteine synthetase. J Biol Chem, 1990, 265(3): 1588-1593.
[26] Huang C S, Anderson M E, Meister A. Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase. J Biol Chem, 1993, 268(27): 20578-20583.
[27] Gipp J J, Chang C, Timothy M R. Cloning and nucleotide sequence of a full-length cDNA for human liver γ-glutamylcysteine synthetase. Biochem Biophys Res Commun, 1992, 185(1): 29-35.
[28] Gipp J J, Bailey H H, Mulcahy R T. Cloning and sequencing of the cDNA for the light subunit of human liver γ-Glutamylcysteine synthetase and relative RNA levels for heavy and light subunits in human normal tissues. Biochem Biophys Res Commun, 1995, 206(2): 584-589.
[29] Seelig G F, Simondsen R P, Meister A. Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits. J Biol Chem, 1984, 259(15): 9345-9347.
[30] Huang C S, Chang L S, Anderson M E, et al. Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase. J Biol Chem, 1993, 268(26): 19675-19680.
[31] Dalton T P, Chen Y, Schneider S N, et al. Genetically altered mice to evaluate glutathione homeostasis in health and disease. Free Radic Biol Med, 2004, 37(10): 1511-1526.
[32] Newton G L, Arnold K, Price M S, et al. Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J Bacteriol, 1996, 178(7): 1990-1995.
[33] Gopal S, Borovok I, Ofer A, et al. A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis. J Bacteriol, 2005, 187(11): 3839-3847.
[34] Janowiak B E, Griffith O W. Glutathione Synthesis in Streptococcus agalactiae one protein accounts for γ-glutamylcysteine synthetase and glutathione synthetase activities. J Biol Chem, 2005, 280(12): 11829-11839.
[35] Vergauwen B, De Vos D, Van Beeumen J J. Characterization of the bifunctional γ-glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida. J Biol Chem, 2006, 281(7): 4380-4394.
[36] Veeravalli K, Boyd D, Iverson B L, et al. Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways. Nat Chem Biol, 2011, 7(2): 101-105.
[37] Spector D, Labarre J, Toledano M B. A Genetic Investigation of the Essential Role of Glutathione mutations in tne proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast. J Biol Chem, 2001, 276(10): 7011-7016.
[38] Lehmann C, Doseeva V, Pullalarevu S, et al. YbdK is a carboxylate-amine ligase with a γ-glutamyl: Cysteine ligase activity: Crystal structure and enzymatic assays. Proteins, 2004, 56(2): 376-383.
[39] Johnson T, Newton G L, Fahey R C, et al. Unusual production of glutathione in Actinobacteria. Arch Microbiol, 2009, 191(1): 89-93.
[40] Elskens MT, Jaspers CJ, Penninckx MJ. Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae. J Gen Microbiol, 1991, 137(3):637-644.
[41] Ganguli D, Kumar C, Bachhawat A K. The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae. Genetics, 2007, 175(3): 1137-1151.
[42] Wellner V P, Sekura R, Meister A, et al. Glutathione synthetase deficiency, an inborn error of metabolism involving the γ-glutamyl cycle in patients with 5-oxoprolinuria (pyroglutamic aciduria). Proc Natl Acad Sci USA, 1974, 71(6): 2505-2509.
[43] Jaspers C J, Gigot D, Penninckx M J. Pathways of glutathione degradation in the yeast Saccharomyces cerevisiae. Phytochemistry, 1985, 24(4): 703-707.
[44] Breslow E, Meister A. The amino acid sequence of rat kidney 5-oxo-L-prolinase determined by cDNA cloning. J Biol Chem, 1996, 271(50): 32293-32300.
[45] Li Y, Wei G, Chen J. Glutathione: a review on biotechnological production. Appl Microbiol Biotechnol, 2004, 66(3): 233-242.
[46] Liao X Y, Shen W, Chen J, et al. Improved glutathione production by gene expression in Escherichia coli. Lett Appl Microbiol, 2006, 43(2): 211-214.
[47] Fei L, Wang Y, Chen S. Improved glutathione production by gene expression in Pichia pastoris. Bioproc Biosyst Eng, 2009, 32(6): 729-735.
[48] Kiriyama K, Hara K Y, Kondo A. Extracellular glutathione fermentation using engineered Saccharomyces cerevisiae expressing a novel glutathione exporter. Appl Microbiol Biot, 2012, 96(4): 1021-1027.
[49] Fan X, He X, Guo X, et al. Increasing glutathione formation by functional expression of the γ-glutamylcysteine synthetase gene in Saccharomyces cerevisiae. Biotechnol Lett, 2004, 26(5): 415-417.
[50] Murata K, Kimura A. Cloning of a gene responsible for the biosynthesis of glutathione in Escherichia coli B. Appl Environ Microb, 1982, 44(6): 1444-1448.
[51] Gushima H, Miya T, Murata K, et al. Construction of glutathione-producing strains of Escherichia coli B by recombinant DNA techniques. J Appl Biochem, 1982, 5(1-2): 43-52.
[52] Li W, Li Z, Yang J, et al. Production of glutathione using a bifunctional enzyme encoded by gshF from Streptococcus thermophilus expressed in Escherichia coli. J biotechnol, 2011, 154(4): 261-268.
[53] Ge S, Zhu T, Li Y. Expression of Bacterial GshF in Pichia pastoris for Glutathione Production. Appl Environ Microb, 2012, 78(15): 5435-5439.
[54] Li Y, Hugenholtz J, Sybesma W, et al. Using Lactococcus lactis for glutathione overproduction. Appl Microbiol Biot, 2005, 67(1): 83-90.
[55] Alfafara C G, Kanda A, Shioi T, et al. Effect of amino acids on glutathione production by Saccharomyces cerevisiae. Appl Microbiol Biot, 1992, 36(4): 538-540.
[56] Wen S, Zhang T, Tan T. Utilization of amino acids to enhance glutathione production in Saccharomyces cerevisiae. Enzyme Microb Tech, 2004, 35(6): 501-507.
[57] Gutiérrez-Alcalá G, Gotor C, Meyer A J, et al. Glutathione biosynthesis in Arabidopsis trichome cells. Proc Natl Acad Sci U S A, 2000, 97(20): 11108-11113.
[58] Ask M, Mapelli V, Höck H, et al. Engineering glutathione biosynthesis of Saccharomyces cerevisiae increases robustness to inhibitors in pretreated lignocellulosic materials. Microb Cell Fact, 2013, 12(87).
[59] Suzuki T, Yokoyama A, Tsuji T, et al. Identification and characterization of genes involved in glutathione production in yeast. J Biosci Bioeng, 2011, 112(2): 107-113.
[60] Hara K Y, Kiriyama K, Inagaki A, et al. Improvement of glutathione production by metabolic engineering the sulfate assimilation pathway of Saccharomyces cerevisiae. Appl Microb Biot, 2012, 94(5): 1313-1319.
[61] Ballatori N, Hammond C L, Cunningham J B, et al. Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins. Toxicol Appl Pharm, 2005, 204(3): 238-255.
|