Literature summary for 6.3.2.3 extracted from

Li, W.; Li, Z.; Yang, J.; Ye, Q.
Production of glutathione using a bifunctional enzyme encoded by gshF from Streptococcus thermophilus expressed in Escherichia coli (2011), J. Biotechnol., 154, 261-268.

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Application

Application	Comment	Organism
synthesis	at elevated concentrations of the precursor amino acids and ATP, Escherichia coli JM109 pTrc99A-gshF produces 36 mM GSH with a molar yield of 0.9 mol/mol based on added cysteine and of 0.45 mol/mol based on added ATP. When ATP is replaced with glucose, the strain produces 7 mM in 3 h. In the presence of glucose and the pmr1 mutant of Saccharomyces cerevisiae BY4742 for ATP generation, Escherichia coli JM109 pTrc99A-gshF produces 33.9 mM GSH in 12 h with a yield of 0.85 mol/mol based on added l-cysteine	Streptococcus thermophilus

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Streptococcus thermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	insensitive to feedback inhibition caused by GSH even at 20 mM	Streptococcus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Streptococcus thermophilus	D4N891	bifucntional glutamate-cysteine ligase and glutathione synthetase	-
Streptococcus thermophilus SIIM B218	D4N891	bifucntional glutamate-cysteine ligase and glutathione synthetase	-

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Release 2023.1 (January 2023)