ISOLATION AND PROPERTIES OF YEAST GLUTATHIONE SYNTHETASE

Abstract The clinical and laboratory features of a 3-mo-old black male infant with glutathione (GSH) synthetase deficiency of the generalized type was evaluated. Partial albinism, brisk hemolytic anemia, recurrent febrile episodes, and mental retardation were noted. Also, severe recurrent metabolic acidosis and marked oxoprolinemia and oxoprolinuria were found in the proband but not in his first-degree relatives. The relationship of these disease manifestations to the underlying metabolic defect is discussed.

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Alcoholic Stem Extract ofCoscinium fenestratumRegulates Carbohydrate Metabolism and Improves Antioxidant Status in Streptozotocin–Nicotinamide Induced Diabetic Rats

Evidence-based Complementary and Alternative Medicine ◽

10.1093/ecam/neh099 ◽

2005 ◽

Vol 2 (3) ◽

pp. 375-381 ◽

Cited By ~ 54

Author(s):

I. R. Punitha ◽

K. Rajendran ◽

Arun Shirwaikar ◽

Annie Shirwaikar

Keyword(s):

Carbohydrate Metabolism ◽

Antioxidant Status ◽

Diabetic Rats ◽

Antidiabetic Activity ◽

Glutathione Synthetase ◽

Alcoholic Extract ◽

Enzymatic Antioxidants ◽

Stem Extract ◽

Gluconeogenic Enzyme ◽

Glucose 6 Phosphate Dehydrogenase

Alcoholic extract of the stems ofCoscinium fenestratum, a medicinal plant indigenous to India and Sri Lanka used in ayurveda and siddha medicine for treating diabetes, was studied for its carbohydrate metabolism effect and antioxidant status in streptozotocin–nicotinamide induced type 2 diabetic rats. Oral administration ofC. fenestratumstem extract in graded doses caused a significant increase in enzymatic antioxidants such as catalase, superoxide dismutase, glutathione synthetase, peroxidase, and glutathione peroxidase and in the nonenzymatic antioxidants ascorbic acid, ceruloplasmin and tocopherol. Effects of alcoholic extract on glycolytic enzymes such as glucose-6-phosphate dehydrogenase, lactate dehydrogenase and hexokinase showed a significant increase in their levels, whereas a significant decrease was observed in the levels of gluconeogenic enzyme, glucose-6-phosphatase and alanine aminotransferase in treated diabetic rats. Serum creatinine and urea levels also declined significantly. This investigation demonstrates significant antidiabetic activity ofC. fenestratum.

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Enhancement of Glutathione Content in Glutathione Synthetase-Deficient Fibroblasts from a Patient with 5-Oxoprolinuria via Metabolic Cooperation with Normal Fibroblasts

Experimental Cell Research ◽

10.1006/excr.1994.1119 ◽

1994 ◽

Vol 212 (1) ◽

pp. 69-76 ◽

Cited By ~ 6

Author(s):

Terrance J. Kavanagh ◽

Ganesh Raghu ◽

Collin C. White ◽

George M. Martin ◽

Peter S. Rabinovitch ◽

...

Keyword(s):

Glutathione Synthetase ◽

Metabolic Cooperation

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Intestinal Barrier Function and Performance of Broiler Chickens Fed Additional Arginine, Combination of Arginine and Glutamine or an Amino Acid-Based Solution

Animals ◽

10.3390/ani11082416 ◽

2021 ◽

Vol 11 (8) ◽

pp. 2416

Author(s):

Reza Barekatain ◽

Tristan Chalvon-Demersay ◽

Clive McLaughlan ◽

William Lambert

Keyword(s):

Amino Acid ◽

Intestinal Permeability ◽

Broiler Chickens ◽

Intestinal Inflammation ◽

Intestinal Barrier ◽

Basal Diet ◽

Intestinal Barrier Function ◽

Glutathione Synthetase ◽

Feed Conversion ◽

Experimental Treatments

Two experiments were conducted to investigate the effect of arginine (Arg); the combination of Arg and glutamine (Gln); as well as an amino acid-based solution (MIX) containing Arg, Gln, threonine (Thr), and grape extract, on performance, intestinal permeability, and expression of selected mechanistic genes. Using 240 male Ross 308 off-sex broiler chickens, four experimental treatments were replicated six times with 10 birds per replicate. The experimental treatments included 5 g/kg Arg, 2.5 g/kg Arg and 2.5 g/kg Gln, and 1 g/kg MIX added to a basal diet as control. In the second study, the four dietary treatments were then given to 24 birds with or without a synthetic glucocorticoid, dexamethasone (DEX), as a gut dysfunction model. Feed conversion ratio was improved by all the supplemented treatments from day 7 to 35 of age (p < 0.001). DEX injections increased (p < 0.001) the intestinal permeability in all treatments, which tended to be reversed by Arg or MIX. Additional Arg, Arg-Gln, and MIX suppressed (p < 0.05) the overexpression of IL-1β generated by DEX. Feeding birds with MIX treatment increased (p < 0.05) expression of SGLT-1 and glutathione synthetase. In conclusion, tested amino acid supplements were effective in improving feed efficiency and restraining intestinal inflammation caused by DEX through IL-1β pathway.

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Surface Display of a Bifunctional Glutathione Synthetase on Saccharomyces cerevisiae for Converting Chicken Feather Hydrolysate into Glutathione

Molecular Biotechnology ◽

10.1007/s12033-014-9750-4 ◽

2014 ◽

Vol 56 (8) ◽

pp. 726-730 ◽

Cited By ~ 6

Author(s):

Zhiqi Qiu ◽

Hongming Tan ◽

Shining Zhou ◽

Lixiang Cao

Keyword(s):

Saccharomyces Cerevisiae ◽

Surface Display ◽

Glutathione Synthetase ◽

Chicken Feather ◽

Bifunctional Glutathione Synthetase

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Glutathione replenishment capacity is lower in isolated perivenous than in periportal hepatocytes

Biochemical Journal ◽

10.1042/bj2540411 ◽

1988 ◽

Vol 254 (2) ◽

pp. 411-417 ◽

Cited By ~ 42

Author(s):

Y Kera ◽

K E Penttilä ◽

K O Lindros

Keyword(s):

Glutathione Synthetase ◽

Synthetase Activity ◽

Gamma Glutamyl Transpeptidase ◽

Zonal Distribution ◽

Significant Difference ◽

Glutamylcysteine Synthetase ◽

Gsh Metabolism ◽

Collagenase Perfusion ◽

Sulphur Amino Acids ◽

Glutamyl Transpeptidase

The zonal distribution of GSH metabolism was investigated by comparing hepatocytes obtained from the periportal (zone 1) or perivenous (zone 3) region by digitonin/collagenase perfusion. Freshly isolated periportal and perivenous cells had similar viability (dye exclusion, lactate dehydrogenase leakage and ATP content) and GSH content (2.4 and 2.7 mumol/g respectively). During incubation, periportal cells slowly accumulated GSH (0.35 mumol/h per g), whereas in perivenous cells a decrease occurred (-0.14 mumol/h per g). Also, in the presence of either L-methionine or L-cysteine (0.5 mM) periportal hepatocytes accumulated GSH much faster (3.5 mumol/h per g) than did perivenous cells (1.9 mumol/h per g). These periportal-perivenous differences were also found in cells from fasted rats. Efflux of GSH was faster from perivenous cells than from periportal cells, but this difference only explained 10-20% of the periportal-perivenous difference in accumulation. Furthermore, periportal cells accumulated GSH to a plateau 26-40% higher than in perivenous cells. There was no significant difference in gamma-glutamylcysteine synthetase or glutathione synthetase activity between the periportal and perivenous cell preparations. The periportal-perivenous difference in GSH accumulation was unaffected by inhibition of gamma-glutamyl transpeptidase or by 5 mM-glutamate or -glutamine, but was slightly diminished by 2 mM-L-methionine. This suggests differences between periportal and perivenous cells in their metabolism and/or transport of (sulphur) amino acids. Our results suggest that a lower GSH replenishment capacity of the hepatocytes from the perivenous region may contribute to the greater vulnerability of this region to xenobiotic damage.

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Glutathione Synthetase Deficiency

Encyclopedia of Molecular Mechanisms of Disease ◽

10.1007/978-3-540-29676-8_711 ◽

2009 ◽

pp. 726-727

Author(s):

David J. Timson ◽

Richard J. Reece ◽

James B. Thoden ◽

Hazel M. Holden ◽

Andrea L. Utz ◽

...

Keyword(s):

Glutathione Synthetase ◽

Synthetase Deficiency ◽

Glutathione Synthetase Deficiency

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Structural biology of plant sulfur metabolism: from sulfate to glutathione

Journal of Experimental Botany ◽

10.1093/jxb/erz094 ◽

2019 ◽

Vol 70 (16) ◽

pp. 4089-4103 ◽

Cited By ~ 4

Author(s):

Joseph M Jez

Keyword(s):

Structural Biology ◽

Protein Interactions ◽

Sulfur Metabolism ◽

Essential Element ◽

Glutathione Synthetase ◽

Protein Protein Interactions ◽

Glutathione Biosynthesis ◽

Wide Range ◽

Aps Reductase ◽

Level Information

Abstract Sulfur is an essential element for all organisms. Plants must assimilate this nutrient from the environment and convert it into metabolically useful forms for the biosynthesis of a wide range of compounds, including cysteine and glutathione. This review summarizes structural biology studies on the enzymes involved in plant sulfur assimilation [ATP sulfurylase, adenosine-5'-phosphate (APS) reductase, and sulfite reductase], cysteine biosynthesis (serine acetyltransferase and O-acetylserine sulfhydrylase), and glutathione biosynthesis (glutamate-cysteine ligase and glutathione synthetase) pathways. Overall, X-ray crystal structures of enzymes in these core pathways provide molecular-level information on the chemical events that allow plants to incorporate sulfur into essential metabolites and revealed new biochemical regulatory mechanisms, such as structural rearrangements, protein–protein interactions, and thiol-based redox switches, for controlling different steps in these pathways.

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