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Literature summary for 6.3.2.3 extracted from
- Novel kinetics of mammalian glutathione synthetase: characterization of gamma-glutamyl substrate cooperative binding (2000), Biochem. Biophys. Res. Commun., 275, 577-581.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli BL21(DE3) | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Rattus norvegicus | |
| 0.037 | - |
ATP | recombinant enzyme, pH 8.2, 37°C | Rattus norvegicus |  |
| 0.042 | - |
gamma-L-Glu-L-alpha-aminobutyrate | recombinant enzyme, pH 8.2, 37°C | Rattus norvegicus | |
| 0.913 | - |
glycine | recombinant enzyme, pH 8.2, 37°C | Rattus norvegicus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Rattus norvegicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + gamma-L-Glu-L-Cys + Gly | Rattus norvegicus | second step in the biosynthesis of glutahione | ADP + phosphate + glutathione | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant from Escherichia coli BL21(DE3), to homogeneity | Rattus norvegicus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione | substrate binding kinetics and mechanism, negative cooperativity of gamma-L-Glu-L-Cys | Rattus norvegicus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 11 | - |
purified recombinant enzyme | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + gamma-L-Glu-L-alpha-aminobutyrate + Gly | - |
Rattus norvegicus | ADP + phosphate + glutathione | - |
r | |
| ATP + gamma-L-Glu-L-Cys + Gly | wild-type enzyme shows negative cooperativity in binding of gamma-L-Glu-L-Cys | Rattus norvegicus | ADP + phosphate + glutathione | - |
r | |
| ATP + gamma-L-Glu-L-Cys + Gly | second step in the biosynthesis of glutahione | Rattus norvegicus | ADP + phosphate + glutathione | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | one active site for each subunit | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Glutathione synthetase | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Rattus norvegicus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 13 | - |
ATP | recombinant enzyme, pH 8.2, 37°C | Rattus norvegicus | |
| 13 | - |
glycine | recombinant enzyme, pH 8.2, 37°C | Rattus norvegicus | |
| 13 | - |
gamma-L-Glu-L-alpha-aminobutyrate | recombinant enzyme, pH 8.2, 37°C | Rattus norvegicus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.2 | - |
assay at | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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