Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Bacillus anthracis |
Crystallization (Comment) | Organism |
---|---|
protein is composed of two structural and functiional domains, the phosphatase and the transferase. Comparison with the structurally similar domains of in Bacillus stearothermophilus | Bacillus anthracis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | Q81X77 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant protein | Bacillus anthracis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2-phospho-D-glycerate = 3-phospho-D-glycerate | in the phospho-D-glycerate-free state the enzyme assumes an open conformation. Upon substrate binding the enzyme closes to the catalytically functional conformation, in the closed form the enzyme catalyzes 2/3-phospho-D-glycerate isomerization resulting in product release. Product release causes opening of the enzyme and return to the open conformation | Bacillus anthracis |
Source Tissue | Comment | Organism | Textmining |
---|
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
37 | - |
23°C | Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | - |
Bacillus anthracis | 3-phospho-D-glycerate | - |
r | |
3-phospho-D-glycerate | - |
Bacillus anthracis | 2-phospho-D-glycerate | - |
r |