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The glutathione synthetase deficiency, inborn error of metabolism of autosomal recessive inheritance, is a rare disease (70 patients described in the world). The outcome of these patients and potential complications of this disease are not, to date, yet all known and described.
Observational Model: Cohort, Time Perspective: Retrospective
The Glutathione Synthetase Deficiency
Not yet recruiting
University Hospital, Strasbourg, France
Published on BioPortfolio: 2016-07-14T00:38:22-0400
This is a double-blind, placebo-controlled crossover study to evaluate the safety and efficacy of glutathione alone or glutathione, vitamin C and NAC treatment in children with autism who ...
Varied food intake, disease, and genetic differences result in complex diet-health interactions. In principle, information-rich metabolic analyses combined with bioinformatic tools provid...
Previous literature has found potential association between selenium deficiency and inactivated glutathione peroxidase and deiodinase, which may contribute to subsequent elevation of T4 an...
The aim of the study is to determine mechanisms leading to glutathione deficiency in low birth weight newborn babies. Compared to full term neonates, depletion in this population may be d...
The aim of this study is to determine the effects of glutathione supplement on the immune cell response and symptomatology of upper respiratory health, and antioxidant capacity in healthy ...
The glutathione synthetase system (GSS) is an important pathway of glutathione synthesis and plays a key role in heavy metal resistance. In this work, the response of Acidithiobacillus ferrooxidans to...
Mutations in the human gene, which encodes the enzyme glutamine synthetase (GS), may cause congenital glutamine synthetase deficiency. The disease was first described in 2005 and only three patients ...
Glutathione has diverse physiological functions, and therefore, the demand for it has increased recently. Currently, industrial mass production of glutathione is performed from D-glucose via fermentat...
Bifunctional glutathione synthetase (GshF) has recently been reported to simultaneously catalyze the 2-step ATP-dependent biosynthesis of reduced glutathione (GSH). In this work, 19 putative gshF were...
Glutathione (GSH) is an important bioactive tripeptide and widely used in food, medicine and other industries. Recently, the bifunctional glutathione synthetase, GshF, has been applied for efficient G...
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 126.96.36.199.
The neonatal form of MULTIPLE CARBOXYLASE DEFICIENCY that is caused by a defect or deficiency in holocarboxylase synthetase. HLCS is the enzyme that covalently links biotin to the biotin dependent carboxylases (propionyl-CoA-carboxylase, pyruvate carboxylase, and beta-methylcrotonyl-CoA carboxylase).
A synthetic amino acid that depletes glutathione by irreversibly inhibiting gamma-glutamylcysteine synthetase. Inhibition of this enzyme is a critical step in glutathione biosynthesis. It has been shown to inhibit the proliferative response in human T-lymphocytes and inhibit macrophage activation. (J Biol Chem 1995;270(33):1945-7)
A deficiency in the activities of biotin-dependent enzymes (propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and PYRUVATE CARBOXYLASE) due to one of two defects in BIOTIN metabolism. The neonatal form is due to HOLOCARBOXYLASE SYNTHETASE DEFICIENCY. The late-onset form is due to BIOTINIDASE DEFICIENCY.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 188.8.131.52.