glutathione synthetase - ترجمة إلى العربية
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glutathione synthetase - ترجمة إلى العربية

CLASS OF ENZYMES
Glutathione synthase; EC 6.3.2.3; Gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming)
  • cofactor]] for a number of [[antioxidant]] and detoxifying enzymes.<ref name="Ribas 2014"/>
  • Key residues that interact with ATP near the active site. Magnesium ions are shown in black. Generated from 2HGS.<ref name="Polekhina_1999"/>
  •  doi-access = free }}</ref> [[Glutamate]] and [[cysteine]] side chains are shown in red and green, respectively.

glutathione synthetase         
‎ مُخَلِّقَةُ الغلوتاثَيون‎
glutathione synthetase deficiency         
HUMAN DISEASE
Deficiency of glutathione synthase; Deficiency of glutathione synthetase; 5-oxoprolinemia; 5-oxoprolinuria; Pyroglutamic acidemia; Pyroglutamic aciduria
‎ عَوَزُ مُخَلِّقَةِ الغلُوتاثَيون‎
5-oxoprolinuria         
HUMAN DISEASE
Deficiency of glutathione synthase; Deficiency of glutathione synthetase; 5-oxoprolinemia; 5-oxoprolinuria; Pyroglutamic acidemia; Pyroglutamic aciduria
بِيلَةُ ال5ـ أُوكْسوبْرُولين

تعريف

snog
to kiss lustily, a REALLY wet kiss
Buffy snogged Selma Blair in Cruel Intentions.

ويكيبيديا

Glutathione synthetase

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. Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants.

In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, increased rate of haemolysis, and defective function of the central nervous system. Deficiencies in GSS can cause a spectrum of deleterious symptoms in plants and human beings alike.

In eukaryotes, this is a homodimeric enzyme. The substrate-binding domain has a three-layer alpha/beta/alpha structure. This enzyme utilizes and stabilizes an acylphosphate intermediate to later perform a favorable nucleophilic attack of glycine.