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Literature summary for 6.3.2.3 extracted from
- Glutathione production by recombinant Escherichia coli expressing bifunctional glutathione synthetase (2016), J. Ind. Microbiol. Biotechnol., 43, 45-53 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gshF, recombinant expression in Escherichia coli strain JM109 from plasmid pTrc99A | Streptococcus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview | Streptococcus thermophilus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Streptococcus thermophilus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + gamma-L-glutamyl-L-cysteine + glycine | Streptococcus thermophilus | - |
ADP + phosphate + glutathione | - |
? | |
| ATP + gamma-L-glutamyl-L-cysteine + glycine | Streptococcus thermophilus SIIM B218 | - |
ADP + phosphate + glutathione | - |
? | |
| additional information | Streptococcus thermophilus | the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 | ? | - |
? | |
| additional information | Streptococcus thermophilus SIIM B218 | the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus thermophilus | D4N891 | - |
- |
| Streptococcus thermophilus SIIM B218 | D4N891 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + gamma-L-glutamyl-L-cysteine + glycine | - |
Streptococcus thermophilus | ADP + phosphate + glutathione | - |
? | |
| ATP + gamma-L-glutamyl-L-cysteine + glycine | - |
Streptococcus thermophilus SIIM B218 | ADP + phosphate + glutathione | - |
? | |
| additional information | the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 | Streptococcus thermophilus | ? | - |
? | |
| additional information | the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 | Streptococcus thermophilus SIIM B218 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bifunctional glutathione synthetase | - |
Streptococcus thermophilus |
| bifunctional GSH synthetase | - |
Streptococcus thermophilus |
| ghF | - |
Streptococcus thermophilus |
| GSH2 | - |
Streptococcus thermophilus |
| gshAB | gene name, UniProt | Streptococcus thermophilus |
| GshF | - |
Streptococcus thermophilus |
| L-glutathione synthetase | - |
Streptococcus thermophilus |
| More | cf. Ec 6.3.2.2 | Streptococcus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Streptococcus thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Streptococcus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Streptococcus thermophilus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a member of the ATP-grasp superfamily of enzymes | Streptococcus thermophilus |
| metabolism | the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus | Streptococcus thermophilus |
| physiological function | the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS) | Streptococcus thermophilus |
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