Literature summary for 6.3.2.2 extracted from

Hothorn, M.; Wachter, A.; Gromes, R.; Stuwe, T.; Rausch, T.; Scheffzek, K.
Structural basis for the redox control of plant glutamate cysteine ligase (2006), J. Biol. Chem., 281, 27557-27565.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystal structure at 2.1 A resolution	Brassica juncea

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-glutamate + L-cysteine	Brassica juncea	rate-limiting step in the biosynthesis of GSH. The regulatory mechanism is based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of Brassica juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of the glutamate-cysteine ligase that is associated with a significant inactivation of the enzyme	ADP + phosphate + gamma-L-glutamyl-L-cysteine	-	?

Organism

Organism	UniProt	Comment	Textmining
Brassica juncea	O23736	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Brassica juncea

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate + L-cysteine	rate-limiting step in the biosynthesis of GSH. The regulatory mechanism is based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of Brassica juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of the glutamate-cysteine ligase that is associated with a significant inactivation of the enzyme	Brassica juncea	ADP + phosphate + gamma-L-glutamyl-L-cysteine	-	?

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Release 2023.1 (January 2023)