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Literature summary for 3.5.1.78 extracted from
- Comparison of the functions of glutathionylspermidine synthetase/amidase from E. coli and its predicted homologues YgiC and YjfC (2012), Int. J. Biochem. Mol. Biol., 3, 302-312.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gsp, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C59A | site-directed mutagenesis, inactive catalytic site mutant | Escherichia coli |
| additional information | construction of a gene disruption mutant that does not produce glutathionylspermidine | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | - |
2 * 45000, SDS-PAGE, homodimer in which each monomer consists of two distinct domains. The C-terminal domain is responsible for the synthesis of glutathionylspermidine while the N-terminal domain catalyzes the hydrolysis of the conjugate | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathionylspermidine + H2O | Escherichia coli | - |
glutathione + spermidine | GspSA catalyzes the formation of a peptide bond between GSH and spermidine, cf. EC 6.3.1.8 | r | |
| additional information | Escherichia coli | bifunctional enzyme that catalyzes the ATP-dependent formation and hydrolysis of glutathionylspermidine, a conjugate of glutathione and spermidine. Proteins YgiC and YjfC, encoded by genes ygiC and yjfC, show ATPase activity, but are not glutathionylspermidine synthetases | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AES0 | gene gsp | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathionylspermidine + H2O | - |
Escherichia coli | glutathione + spermidine | GspSA catalyzes the formation of a peptide bond between GSH and spermidine, cf. EC 6.3.1.8 | r | |
| glutathionylspermidine + H2O | the N-terminal domain catalyzes the hydrolysis of the conjugate | Escherichia coli | glutathione + spermidine | GspSA catalyzes the formation of a peptide bond between GSH and spermidine, cf. EC 6.3.1.8 | r | |
| additional information | bifunctional enzyme that catalyzes the ATP-dependent formation and hydrolysis of glutathionylspermidine, a conjugate of glutathione and spermidine. Proteins YgiC and YjfC, encoded by genes ygiC and yjfC, show ATPase activity, but are not glutathionylspermidine synthetases | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 45000, SDS-PAGE, homodimer in which each monomer consists of two distinct domains. The C-terminal domain is responsible for the synthesis of glutathionylspermidine while the N-terminal domain catalyzes the hydrolysis of the conjugate | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Glutathionylspermidine synthetase/amidase | - |
Escherichia coli |
| GspSA | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | - |
purified recombinant enzyme, pH 6.8, 3 min, inactivation | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | signature amino acid residues of ATP-grasp domain, R316, K498, K533, are responsible for the ATP binding | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the synthetase domain of GspSA belongs to the class of ATP-grasp structural domains. Proteins YgiC and YjfC proteins show 51% identity between themselves and 28% identity to the synthetase domain of the GspSA enzyme, but do not show any glutathionylspermidine synthetase/amidase enzyme activity | Escherichia coli |
| additional information | comparison of catalytic properties of recombinant purified proteins GspSA, YgiC, and YjfC, overview | Escherichia coli |
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