Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain L673 | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D334A | site-directed mutagenesis, the mutation has essentially no effect on the Km for L-glutamine | Escherichia coli |
N311A | site-directed mutagenesis, the mutant shows increased Km for L-glutamine compared to the wild-type enzyme | Escherichia coli |
Q310A | site-directed mutagenesis, the mutant shows increased Km for L-glutamine compared to the wild-type enzyme | Escherichia coli |
Q351A | site-directed mutagenesis, the mutant shows highly increased Km for L-glutamine compared to the wild-type enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of wild-type and mutant enzymes in L-glutamine-dependent and bicarbonate-dependent ATPase activities, overview | Escherichia coli | |
0.027 | - |
ATP | pH 7.6, 25°C, mutant D334A, L-glutamine hydrolysis | Escherichia coli | |
0.044 | - |
ATP | pH 7.6, 25°C, wild-type enzyme, L-glutamine hydrolysis | Escherichia coli | |
0.052 | - |
ATP | pH 7.6, 25°C, mutant Q351A, L-glutamine hydrolysis | Escherichia coli | |
0.067 | - |
ATP | pH 7.6, 25°C, mutant Q310A, L-glutamine hydrolysis | Escherichia coli | |
0.075 | - |
ATP | pH 7.6, 25°C, mutant N311A, L-glutamine hydrolysis | Escherichia coli | |
0.13 | - |
L-glutamine | pH 7.6, 25°C, wild-type enzyme, L-glutamine hydrolysis | Escherichia coli | |
0.15 | - |
L-glutamine | pH 7.6, 25°C, mutant Q351A, L-glutamine hydrolysis | Escherichia coli | |
1.99 | - |
L-glutamine | pH 7.6, 25°C, mutant Q310A, L-glutamine hydrolysis | Escherichia coli | |
3.45 | - |
L-glutamine | pH 7.6, 25°C, mutant N311A, L-glutamine hydrolysis | Escherichia coli | |
18.87 | - |
L-glutamine | pH 7.6, 25°C, mutant D334A, L-glutamine hydrolysis | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + HCO3- + H2O | Escherichia coli | - |
ADP + phosphate + L-glutamate + carbamoyl phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate | mechanism for the generation of ammonia within the L-glutamine amidotransferase domain of CPS, detailed overview | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + HCO3- + H2O | - |
Escherichia coli | ADP + phosphate + L-glutamate + carbamoyl phosphate | - |
? | |
ATP + L-glutamine + HCO3- + H2O | evolutionarily conserved triad glutamine amidotransferase, GAT, domains catalyze the cleavage of L-glutamine to yield ammonia and sequester the ammonia in a tunnel until delivery to a variety of acceptor substrates in synthetase domains of variable structure. The Cys269 and His353 catalytic triad residues are essential for L-glutamine hydrolysis, whereas Glu355 is not critical for eCPS activity, Gln351 plays a key role in L-glutamine binding, overview | Escherichia coli | ADP + phosphate + L-glutamate + carbamoyl phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
carbamoyl phosphate synthetase | - |
Escherichia coli |
CPS | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.53 | - |
L-glutamine | pH 7.6, 25°C, mutant Q351A, L-glutamine hydrolysis | Escherichia coli | |
1.05 | - |
L-glutamine | pH 7.6, 25°C, mutant N311A, L-glutamine hydrolysis | Escherichia coli | |
1.17 | - |
L-glutamine | pH 7.6, 25°C, mutant D334A, L-glutamine hydrolysis | Escherichia coli | |
1.33 | - |
ATP | pH 7.6, 25°C, mutant D334A, L-glutamine hydrolysis | Escherichia coli | |
1.6 | - |
L-glutamine | pH 7.6, 25°C, mutant Q310A, L-glutamine hydrolysis | Escherichia coli | |
2.13 | - |
ATP | pH 7.6, 25°C, mutant N311A, L-glutamine hydrolysis | Escherichia coli | |
2.13 | - |
L-glutamine | pH 7.6, 25°C, wild-type enzyme, L-glutamine hydrolysis | Escherichia coli | |
3.19 | - |
ATP | pH 7.6, 25°C, mutant Q351A, L-glutamine hydrolysis | Escherichia coli | |
4.79 | - |
ATP | pH 7.6, 25°C, wild-type enzyme, L-glutamine hydrolysis | Escherichia coli | |
5.75 | - |
ATP | pH 7.6, 25°C, mutant Q310A, L-glutamine hydrolysis | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |