Protein Variants | Comment | Organism |
---|---|---|
E165C | mutant yields inter-subunit disulfide bonds connecting central loops. Inter-subunit disulfide bonds between the central loops causes no detectable changes in the KM-values for glutamate or ATP, nor the KD for either ATP or the transition state analog L-methionine sulfoximine. Covalent and quantitative adduction of the E165C mutant with iodo-acetamido-pyrene yields nearly fully active enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
ATP | wild-type enzyme | Escherichia coli | |
0.25 | - |
ATP | oxidized mutant enzyme E165C | Escherichia coli | |
0.26 | - |
ATP | reduced mutant enzyme E165C | Escherichia coli | |
3.3 | - |
L-Glu | wild-type enzyme | Escherichia coli | |
6 | - |
L-Glu | oxidized mutant enzyme E165C | Escherichia coli | |
7 | - |
L-Glu | reduced mutant enzyme E165C | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-Glu + NH4+ | Escherichia coli | - |
ADP + phosphate + L-Gln | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-Glu + NH4+ | - |
Escherichia coli | ADP + phosphate + L-Gln | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | 6 | ATP | wild-type enzyme | Escherichia coli | |
25 | - |
ATP | oxidized mutant enzyme E165C | Escherichia coli | |
27 | - |
L-Glu | oxidized mutant enzyme E165C | Escherichia coli | |
35 | - |
ATP | reduced mutant enzyme E165C | Escherichia coli | |
40 | - |
L-Glu | reduced mutant enzyme E165C | Escherichia coli |