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Literature summary for 2.7.9.3 extracted from
- Binding of ATP and its derivatives to selenophosphate synthetase from Escherichia coli (2009), Biochemistry (Moscow), 74, 910-916.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| into the vector pCR2.1 and subsequently into pKK233.2 for expression in Escherichia coli MB08 cells | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C17S | catalytically inactive mutant | Escherichia coli |
| SPS238 | C-terminally truncated mutant containing the N-terminal 238 amino acids of the 348-amino-acid protein | Escherichia coli |
| SPS262 | C-terminally truncated mutant containing the N-terminal 262 amino acids of the 348-amino-acid protein | Escherichia coli |
| SPS332 | C-terminally truncated mutant containing the N-terminal 332 amino acids of the 348-amino-acid protein | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.6 | - |
ATP | Mn-ATP, wild-type enzyme | Escherichia coli |  |
| 5.2 | - |
ATP | Mn-ATP, mutant SPS332 | Escherichia coli | |
| 7.7 | - |
ATP | Mn-ATP, mutant SPS262 | Escherichia coli | |
| 10.3 | - |
ATP | Mn-ATP, mutant SPS238 | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
| Mn2+ | - |
Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 25000 | - |
mutant SPS238 | Escherichia coli |
| 29000 | - |
mutant SPS262 | Escherichia coli |
| 34000 | - |
mutant SPS332 | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + selenide + H2O | Escherichia coli | - |
AMP + selenophosphate + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| DEAE-Sepharose chromatography is used after an ammonium sulfate fractionation step followed by phenyl-Sepharose and butyl-Sepharose chromatography | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + selenide + H2O | - |
Escherichia coli | AMP + selenophosphate + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| selenophosphate synthetase | - |
Escherichia coli |
| SPS | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
activity assay | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
2'(3')-O-(2,4,6-trinitrophenyl)-ATP binding to wild-type and mutant SPS | Escherichia coli |
| 8 | - |
activity assay | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Escherichia coli | wild-type enzyme | - |
5.2 |
| Escherichia coli | mutant SPS262 | - |
5.78 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | selenophosphate synthetase is a key enzyme of the selenium pathway in the cell | Escherichia coli |
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