Protein Variants | Comment | Organism |
---|---|---|
D120N | 3000fold decrease in the value of turnover number. The structure is indistinguishable from that of the wild-type enzyme and the decrease in activity is not simply due to a strutural perturbation of active site. The ratio of turnover number to Km-value is 20750fold lower than that of the wild-type enzyme | Escherichia coli |
D76E | the ratio of turnover number to Km-value is 104fold lower than that of the wild-type enzyme,2.2fold decrease in backgroud aldolase activity compared to wild-type enzyme | Escherichia coli |
E142Q | the ratio of turnover number to Km-value is 17fold lower than that of the wild-type enzyme | Escherichia coli |
H218N | 15fold decrease in background aldolase activity compared to wild-type enzyme. The ratio of turnover number to Km-value is 296fold lower than that of the wild-type enzyme | Escherichia coli |
K42M | the ratio of turnover number to Km-value is 12969fold lower than that of the wild-type enzyme, 5.3fold increase in backgroud aldolase activity compared to wild-type enzyme | Escherichia coli |
N28A | the ratio of turnover number to Km-value is 198fold lower than that of the wild-type enzyme, 10.2fold increase in backgroud aldolase activity compared to wild-type enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.047 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, wild-type enzyme | Escherichia coli | |
0.086 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme E142Q | Escherichia coli | |
0.25 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme D76E | Escherichia coli | |
0.28 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme D120N | Escherichia coli | |
0.58 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme H218N | Escherichia coli | |
1.2 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme N28A | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes expressed in Escherichia coli Y1090 | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Ribulose 5-phosphate | - |
Escherichia coli | D-Xylulose 5-phosphate | - |
? | |
additional information | wild-type enzyme and mutant enzymes D76E and N28A display a background aldolase activity with glycolaldehyde, phosphate and dihydroxyacetone | Escherichia coli | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0057 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme D120N | Escherichia coli | |
0.81 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme H218N | Escherichia coli | |
1 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme D76E | Escherichia coli | |
1.1 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, wild-type enzyme | Escherichia coli | |
2.14 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme E142Q | Escherichia coli | |
2.5 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme N28A | Escherichia coli | |
2.94 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme E142Q | Escherichia coli | |
6.08 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, mutant enzyme H218N | Escherichia coli | |
19.4 | - |
L-ribulose 5-phosphate | 37°C, pH 7.6, wild-type enzyme | Escherichia coli |