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Glutathione biosynthesis involves two adenosine triphosphate-dependent steps: First, γ-glutamylcysteine is synthesized from L-glutamate and L-cysteine. This conversion requires the enzyme glutamate–cysteine ligase (GCL, glutamate cysteine synthase). This reaction is the rate-limiting step in glutathione synthesis. [3]
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. [2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants. [3]
Both glutathione biosynthesis enzymes are essential in plants; knock-outs of GCL and GS are lethal to embryo and seedling, respectively. [ 30 ] As of late 2007, six structures have been solved for this class of enzymes, with PDB accession codes 1V4G , 1VA6 , 2D32 , 2D33 , 2GWC , and 2GWD .
Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism 's diet or growth media.
It reduces glutathione via glutathione reductase, which converts reactive H 2 O 2 into H 2 O by glutathione peroxidase. If absent, the H 2 O 2 would be converted to hydroxyl free radicals by Fenton chemistry, which can attack the cell. Erythrocytes, for example, generate a large amount of NADPH through the pentose phosphate pathway to use in ...
Glutathione is maintained in the reduced form by an NADPH-dependent glutathione reductase and the ratio of reduced glutathione (GSH) to oxidized glutathione (GSSG) generally exceeds a value of 7. Glutathione fulfils various roles in plant functioning. In sulfur metabolism it functions as reductant in the reduction of APS to sulfite.
γ-L-Glutamyl-L-cysteine, also known as γ-glutamylcysteine (GGC), is a dipeptide found in animals, plants, fungi, some bacteria, and archaea.It has a relatively unusual γ-bond between the constituent amino acids, L-glutamic acid and L-cysteine and is a key intermediate in the γ-glutamyl cycle first described by Meister in the 1970s.
Glutathione synthetase deficiency has an autosomal recessive pattern of inheritance. Mutations in the GSS gene cause glutathione synthetase deficiency. This gene provides instructions for making the enzyme glutathione synthetase. This enzyme is involved in a process called the gamma-glutamyl cycle, which takes place in most of the body's cells ...