Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ammonia | - |
Escherichia coli | |
L-ornithine | - |
Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
L270K | ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is 5fold decreased in comparison to the wild-type enzyme, the glutamine binding is almost entirely abolished | Escherichia coli |
additional information | the mutants are constructed to mimic the potentially significant substitutions which is observed in the frog enzyme and to allow determination of the effects of these changes on the glutamine binding ability of enzyme | Escherichia coli |
Q273E | ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is equivalent to the wild-type enzyme, but the mutant is 10fold impaired in its L-glutamine binding ability in comparison to wild-type enzyme | Escherichia coli |
Q273E/L270K | ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is 25fold decreased in comparison to the wild-type enzyme, the glutamine binding is almost entirely abolished | Escherichia coli |
Q273E/N240S | ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is equivalent to the wild-type enzyme | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
UMP | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | comparison of Km-values for wild-type and mutant enzymes in absence and presence of ornithine | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + L-Gln + HCO3- | Escherichia coli | the enzyme catalyses the first step in the synthesis of arginine and pyrimidine | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzyme | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate | in glutamine utilizing enzymes, the hydrolysis of glutamine to yield ammonia is catalyzed at a triad-type glutamine amidotransferase domain | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + L-Gln + HCO3- | - |
Escherichia coli | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
2 ATP + L-Gln + HCO3- | the enzyme catalyses the first step in the synthesis of arginine and pyrimidine | Escherichia coli | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | comparison of kcat-values for wild-type and mutant enzymes in absence and presence of ornithine | Escherichia coli |