Literature summary for 6.3.2.3 extracted from

Hibi, T.; Kato, H.; Nishioka, T.; Oda, J.; Yamaguchi, H.; Katsube, Y.; Tanizawa, K.; Fukui, T.
Use of adenosine(5�)poylphospho(5�)pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B (1993), Biochemistry, 32, 1548-1554.

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Cloned(Commentary)

Cloned (Comment)	Organism
Escherichia coli B enzyme overproduced in Escherichia coli JM109	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
adenosine-5'-tetraphospho-5'-pyridoxal	when incubated with an adenosine-5'-polyphospho-5'-pyridoxal or pyridoxal phosphate in the presence of Mg2+ and then reduced with sodium borohydride, it is most rapidly inactivated by adenosine-5'-tetraphospho-5'-pyridoxal, addition of either ATP or gamma-glutamylcysteine protects from inactivation	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	B	-
Escherichia coli	-	Escherichia coli B enzyme overproduced in Escherichia coli JM109	-
Escherichia coli B / ATCC 11303	-	B	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + gamma-Glu-L-Cys + Gly	-	Escherichia coli	ADP + phosphate + glutathione	-	?
ATP + gamma-Glu-L-Cys + Gly	-	Escherichia coli B / ATCC 11303	ADP + phosphate + glutathione	-	?

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Release 2023.1 (January 2023)