Literature summary for 6.3.2.2 extracted from

Hibi, T.; Nii, H.; Nakatsu, T.; Kimura, A.; Kato, H.; Hiratake, J.; Oda, J.
Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis (2004), Proc. Natl. Acad. Sci. USA, 101, 15052-15057.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapor diffusion method, crystal structure of unliganded enzyme and enzyme complexed with a sulfoximine-based transition-state analog inhibitor at resolutions of 2.5 and 2.1 A, respectively. In the crystal structure of the complex, the bound inhibitor is phosphorylated at the sulfoximido nitrogen and is coordinated to three Mg2+ ions	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-glutamate + L-cysteine	Escherichia coli	rate-limiting enzyme in glutathione biosynthesis, plays a central role in glutathione homeostasis	ADP + phosphate + gamma-L-glutamyl-L-cysteine	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate + L-cysteine	rate-limiting enzyme in glutathione biosynthesis, plays a central role in glutathione homeostasis	Escherichia coli	ADP + phosphate + gamma-L-glutamyl-L-cysteine	-	?

Synonyms

Synonyms	Comment	Organism
gamma-Glutamylcysteine synthetase	-	Escherichia coli
gammaGCS	-	Escherichia coli

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Release 2023.1 (January 2023)