Cloned (Comment) | Organism |
---|---|
overexpression in Saccharomyces cerevisiae | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
P204F | site-directed mutagenesis, mutation in the hinge region of the enzyme, which plays a role in protein folding during catalysis, less well folded with considerable loss of secondary and tertiary structure, no activity | Saccharomyces cerevisiae |
P204H | site-directed mutagenesis, mutation in the hinge region of the enzyme, which plays a role in protein folding during catalysis, secondary and tertiary structure is similar to the wild-type, but the mutant is less stable to heat and guanidinium chloride denaturation, 3-4fold increase of Km for 3-phospho-D-glycerate and ATP | Saccharomyces cerevisiae |
General Stability | Organism |
---|---|
Pro204 is important for stability and catalytic mechanism of the enzyme | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Guanidinium chloride | 0.5 M, 30% loss of activity for the mutant P204H, 5% loss of activity for the wild-type, both are unfolded at 1 M | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Saccharomyces cerevisiae | |
0.33 | - |
ATP | wild-type enzyme, pH 7.5, 25°C | Saccharomyces cerevisiae | |
0.77 | - |
3-phospho-D-glycerate | wild-type enzyme, pH 7.5, 25°C | Saccharomyces cerevisiae | |
1.25 | - |
ATP | mutant P204H, pH 7.5, 25°C | Saccharomyces cerevisiae | |
2.5 | - |
3-phospho-D-glycerate | mutant P204H, pH 7.5, 25°C | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + 3-phospho-D-glyceroyl phosphate | Saccharomyces cerevisiae | - |
ATP + 3-phospho-D-glycerate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate | Pro204 is important for stability and catalytic mechanism of the enzyme | Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.4 | - |
purified mutant P204F | Saccharomyces cerevisiae |
4.5 | - |
purified mutant P204H | Saccharomyces cerevisiae |
468 | - |
purified wild-type enzyme | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + 3-phospho-D-glyceroyl phosphate | - |
Saccharomyces cerevisiae | ATP + 3-phospho-D-glycerate | - |
r | |
ATP + 3-phospho-D-glycerate | - |
Saccharomyces cerevisiae | ADP + 1,3-diphosphoglycerate | - |
r |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.4 | - |
ATP | mutant P204H, pH 7.5, 25°C | Saccharomyces cerevisiae | |
3.4 | - |
3-phospho-D-glycerate | mutant P204H, pH 7.5, 25°C | Saccharomyces cerevisiae | |
354 | - |
ATP | wild-type enzyme, pH 7.5, 25°C | Saccharomyces cerevisiae | |
354 | - |
3-phospho-D-glycerate | wild-type enzyme, pH 7.5, 25°C | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Saccharomyces cerevisiae | |
ATP | required as phosphate donor | Saccharomyces cerevisiae |