Crystallization (Comment) | Organism |
---|---|
wild-type and mutant enzyme E197betaA, hanging drop vapour diffusion method | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
E197betaA | mutant enzyme with very low activity. The mutant protein is crystallized in the same space group as the wild-type enzyme. Crystals of the mutant enzyme grew as plates rather than as cubes which are the usual crystal habit for the wild-type enzyme | Escherichia coli |
E197betaD | the Km-values and turnover numbers are comparable to those of the wild-type enzyme | Escherichia coli |
E197betaQ | the KM-value for each substrate is comparable to that of the wild-type enzyme, except for GTP, whose Km-value is reduced by a factor of 20. 3000fold decrease in turnover number for reaction with ATP, 7000fold decrease in turnover-number when using GTP | Escherichia coli |
E208alphaD | Km-values for succinate, CoA, GTP and ATP are comparable to those observed with wild-type enzyme. The turnover-numbers for ATP and GTP are comparable to the wild-type value | Escherichia coli |
E208alphaQ | Km-values for succinate, CoA and ATP are comparable to those observed with wild-type enzyme. The KM-value for GTP is 36times lower than that of the wild-type enzyme. The turnover-numbers for ATP and GTP are reduced approximately 5000fold compared to the wild-type enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0013 | - |
CoA | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
0.0018 | - |
CoA | pH 7.4, 22°C, mutant enzyme E197betaQ | Escherichia coli | |
0.002 | - |
CoA | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli | |
0.0027 | - |
CoA | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
0.011 | - |
GTP | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
0.02 | - |
GTP | pH 7.4, 22°C, mutant enzyme E197betaQ | Escherichia coli | |
0.041 | - |
ATP | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
0.063 | - |
GTP | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli | |
0.106 | - |
ATP | pH 7.4, 22°C, mutant enzyme E197betaQ | Escherichia coli | |
0.116 | - |
ATP | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli | |
0.137 | - |
ATP | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
0.26 | - |
succinate | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli | |
0.27 | - |
succinate | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
0.311 | - |
GTP | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
0.4 | - |
succinate | pH 7.4, 22°C, mutant enzyme E197betaQ | Escherichia coli | |
0.87 | - |
succinate | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + succinate + CoA | during the reaction a His residue at the alpha-subunit is transiently phosphorylated. Glu208alpha and Glu197beta, are crucial for phosphorylation and dephosphorylation of the active-site His | Escherichia coli | ADP + phosphate + succinyl-CoA | - |
? | |
GTP + succinate + CoA | - |
Escherichia coli | GDP + phosphate + succinyl-CoA | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.21 | - |
GTP | pH 7.4, 22°C, mutant enzyme E197betaQ | Escherichia coli | |
0.28 | - |
GTP | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
0.57 | - |
ATP | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
0.85 | - |
ATP | pH 7.4, 22°C, mutant enzyme E197betaQ | Escherichia coli | |
6.08 | - |
ATP | pH 7.4, 22°C, mutant enzyme E208alphaQ | Escherichia coli | |
302 | - |
GTP | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli | |
1775 | - |
ATP | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
1775 | - |
GTP | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
1780 | - |
ATP | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
1780 | - |
GTP | pH 7.4, 22°C, mutant enzyme E197betaD | Escherichia coli | |
2340 | - |
ATP | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli | |
2343 | - |
ATP | pH 7.4, 22°C, mutant enzyme E208alphaD | Escherichia coli |