Protein Variants | Comment | Organism |
---|---|---|
E231betaA | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
E231betaW | strong decrease in activity | Escherichia coli |
E231betaW/Q247betaW/E249betaW | strong decrease in activity | Escherichia coli |
E29betaD/E33betaA/S36betaA | activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact | Escherichia coli |
E33betaA/S36betaA | activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact | Escherichia coli |
E33betaA/S36betaA/K66betaA | activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact | Escherichia coli |
E4betaK/R14betaD//R70betaG/E231betaW/Q247betaW/E24 | strong decrease in activity | Escherichia coli |
E74betaK | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
K66betaA | activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact | Escherichia coli |
M156betaD/Y1258betaD/R161betaE/E162betaR | mutant enzyme with alphabeta-dimer subunit structure | Escherichia coli |
Q247betaK | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R14betaD | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R14betaD/E231betA | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R14betaD/R70betaG/E74betaK | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R14betaD/R70betaG/E74betaK/E231betaA/Q247betaK | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R29betaA/E33betaA/S36betaA/K66betaA | strong decrease in activity | Escherichia coli |
R29betaD | activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact | Escherichia coli |
R70betaG | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R70betaG/E74betaK | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
R70betaG/E74betaK/Q247betaK | activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + succinyl-CoA | Escherichia coli | the enzyme carries out the substrate-level phosphorylation in the citric acid cycle | ATP + succinate + CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + succinyl-CoA | the enzyme carries out the substrate-level phosphorylation in the citric acid cycle | Escherichia coli | ATP + succinate + CoA | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 2 * alpha + 2 * beta. The dimerization of the alphabeta-dimer is not a prerequisite for catalytic competency nor for alternating sites cooperativity in the tetramer | Escherichia coli |