Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermococcus kodakarensis |
Crystallization (Comment) | Organism |
---|---|
sitting drop vapor diffusion method at 20°C. Crystal structure of unliganded Tk-R15Pi is solved by means of the single-wavelength anomalous dispersion method using SeMet-substituted enzyme and refined at 2.5 A resolution | Thermococcus kodakarensis |
Protein Variants | Comment | Organism |
---|---|---|
C133A | inactive mutant enzyme | Thermococcus kodakarensis |
C133S | inactive mutant enzyme | Thermococcus kodakarensis |
D202N | inactive mutant enzyme | Thermococcus kodakarensis |
R227R | mutant enzyme exhibits a decrease in molecular size of the enzyme and significantly decreases the enzymatic activity | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | Q5JFM9 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermococcus kodakarensis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
29.3 | - |
pH 8.0, 85°C, wild-type enzyme | Thermococcus kodakarensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-D-ribose 1,5-bisphosphate | the enzyme is specific for the alpha-anomer of D-ribose 1,5-bisphosphate | Thermococcus kodakarensis | D-ribulose 1,5-bisphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | - |
Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
R15Pi | - |
Thermococcus kodakarensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
assay at | Thermococcus kodakarensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Thermococcus kodakarensis |