Protein Variants | Comment | Organism |
---|---|---|
E841K | comparison of 15N-isotope effects in mutant and wild-type enzyme on the hydrolysis of glutamine, the rate of glutamine hydrolysis in the mutant is not affected by MgATP2 and HCO3-, with the wild-type enzyme in the absence of MgATP2 and HCO3- the isotope effect id reduced | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.15 | - |
L-glutamine | pH 7.6, 37°C, L-glutamine hydrolysis | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + L-Gln + HCO3- | Escherichia coli | - |
2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate | An ordered uni bi mechanism for glutamine hydrolysis that is consistent with the isotope effects and with the catalytic properties of the enzyme is proposed | 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 | - |
ir |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.2 | - |
wild-type enzyme | Escherichia coli |
6.6 | - |
mutant enzyme E841K | Escherichia coli |
9.3 | - |
wild-type enzyme | Escherichia coli |