Literature summary for 6.3.2.3 extracted from

Gogos, A.; Shapiro, L.
Large conformational changes in the catalytic cycle of glutathione synthase (2002), Structure, 10, 1669-1676.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization by vapour-diffusion hanging-drop method of the free enzyme or the enzyme liganded to substrate gamma-glutamylcysteine and non-hydrolyzable ATP-substrate-analogue AMP-PNP, 17 mg/ml enzyme in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, plus equal volume of reservoir solution: for crystals of free enzyme with 1.97 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400 at 22°C, or for the liganded enzyme with 3 mM AMP-PNP, 10 mM MgCl2, 3 mM gamma-glutamylcysteine against a well solution of 2.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400, 5 mM TCEP, 40 mM MgCl2, at 22°C, X-ray diffraction structure determination and analysis at 2.3 A and 1.8 A, respectively	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

crystallization by vapour-diffusion hanging-drop method of the free enzyme or the enzyme liganded to substrate gamma-glutamylcysteine and non-hydrolyzable ATP-substrate-analogue AMP-PNP, 17 mg/ml enzyme in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, plus equal volume of reservoir solution: for crystals of free enzyme with 1.97 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400 at 22°C, or for the liganded enzyme with 3 mM AMP-PNP, 10 mM MgCl2, 3 mM gamma-glutamylcysteine against a well solution of 2.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400, 5 mM TCEP, 40 mM MgCl2, at 22°C, X-ray diffraction structure determination and analysis at 2.3 A and 1.8 A, respectively

Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required, binding structure	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + gamma-L-Glu-L-Cys + Gly	Saccharomyces cerevisiae	final step in glutathione biosynthesis	ADP + phosphate + glutathione	-	ir

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q08220	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	determination of reaction and substrate binding mechanisms, large conformational changes in the catalytic cycle	Saccharomyces cerevisiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + gamma-L-Glu-L-Cys + Gly	-	Saccharomyces cerevisiae	ADP + phosphate + glutathione	-	ir
ATP + gamma-L-Glu-L-Cys + Gly	final step in glutathione biosynthesis	Saccharomyces cerevisiae	ADP + phosphate + glutathione	-	ir

Subunits

Subunits	Comment	Organism
dimer	homodimer, crystal structure	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
GS	-	Saccharomyces cerevisiae
More	enzyme belongs to the ATP-grasp enzyme superfamily	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
ATP	dependent on, binding structure	Saccharomyces cerevisiae