Literature summary for 6.3.2.3 extracted from

Kino, K.; Kuratsu, S.; Noguchi, A.; Kokubo, M.; Nakazawa, Y.; Arai, T.; Yagasaki, M.; Kirimura, K.
Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum (2007), Biochem. Biophys. Res. Commun., 352, 351-359.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL-21DELTA(DE3) cells	Clostridium acetobutylicum
expressed in Escherichia coli BL-21DELTA(DE3) cells	Streptococcus agalactiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
85000	-	SDS-PAGE	Clostridium acetobutylicum

Organism

Organism	UniProt	Comment	Textmining
Clostridium acetobutylicum	-	-	-
Clostridium acetobutylicum NBRC13948	-	-	-
Streptococcus agalactiae	Q8DXM9	-	-
Streptococcus agalactiae 2603 V/R	Q8DXM9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + gamma-Glu-L-Cys + Gly	-	Clostridium acetobutylicum	ADP + phosphate + glutathione	-	?
ATP + gamma-Glu-L-Cys + Gly	-	Streptococcus agalactiae	ADP + phosphate + glutathione	-	?
ATP + gamma-Glu-L-Cys + Gly	-	Streptococcus agalactiae 2603 V/R	ADP + phosphate + glutathione	-	?
ATP + gamma-Glu-L-Cys + Gly	-	Clostridium acetobutylicum NBRC13948	ADP + phosphate + glutathione	-	?

Synonyms

Synonyms	Comment	Organism
Glutathione synthetase	-	Clostridium acetobutylicum
Glutathione synthetase	-	Streptococcus agalactiae

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Clostridium acetobutylicum
ATP	-	Streptococcus agalactiae

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Release 2023.1 (January 2023)