Literature summary extracted from
Noinaj, N.; Wattanasak, R.; Lee, D.Y.; Wally, J.L.; Piszczek, G.; Chock, P.B.; Stadtman, T.C.; Buchanan, S.K.
Structural insights into the catalytic mechanism of Escherichia coli selenophosphate synthetase (2012), J. Bacteriol., 194, 499-508.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.9.3 |
expressed in Escherichia coli BL21(DE3) cells |
Escherichia coli |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.9.3 |
mutant enzyme C17S in apo form, hanging drop vapor diffusion method, using 50 mM Tris-HCl (pH 8.25), 50 mM MgCl2, and 32% (w/v) PEG MME 550 |
Escherichia coli |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.9.3 |
D227A |
inactive |
Escherichia coli |
2.7.9.3 |
D51A |
inactive |
Escherichia coli |
2.7.9.3 |
D68A |
inactive |
Escherichia coli |
2.7.9.3 |
D91A |
inactive |
Escherichia coli |
2.7.9.3 |
N87A |
inactive |
Escherichia coli |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.9.3 |
K+ |
dependent on |
Escherichia coli |
|
2.7.9.3 |
Mg2+ |
dependent on |
Escherichia coli |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.9.3 |
Escherichia coli |
P16456 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.9.3 |
Ni-agarose column chromatography |
Escherichia coli |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.9.3 |
ATP + selenide + H2O |
- |
Escherichia coli |
AMP + selenophosphate + phosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.9.3 |
dimer |
sedimentation velocity analysis |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.9.3 |
selenophosphate synthetase |
- |
Escherichia coli |
2.7.9.3 |
SPS |
- |
Escherichia coli |