Crystallization (Comment) | Organism |
---|---|
crystal structure of 6-diazo-5-oxonorleucine inactivated enzyme at 2.3 A resolution | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
R26H | extremely labile enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic constants of Arg73 and Tyr74 mutants for basal and total glutaminase activity | Escherichia coli | |
0.64 | - |
L-glutamine | N101G mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli | |
1.42 | - |
L-glutamine | N101D mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli | |
1.72 | - |
L-glutamine | 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutamine hydrolysis | Escherichia coli | |
1.72 | - |
L-glutamine | wild-type enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli | |
2.1 | - |
L-glutamine | - |
Escherichia coli | |
2.43 | - |
L-glutamine | G102A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli | |
6.03 | - |
L-glutamine | N101G mutant enzyme, aminotransferase activity | Escherichia coli | |
6.08 | - |
L-glutamine | D127A mutant enzyme, aminotransferase activity | Escherichia coli | |
7.31 | - |
L-glutamine | R73L mutant enzyme, aminotransferase activity | Escherichia coli | |
7.34 | - |
NH3 | - |
Escherichia coli | |
7.34 | - |
L-glutamine | wild-type enzyme, aminotransferase activity | Escherichia coli | |
7.67 | - |
L-glutamine | G102A mutant enzyme, aminotransferase activity | Escherichia coli | |
9.17 | - |
L-glutamine | N101D mutant enzyme, aminotransferase activity | Escherichia coli | |
9.76 | - |
L-glutamine | R73H mutant enzyme, aminotransferase activity | Escherichia coli | |
101 | - |
L-glutamine | R73H mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli | |
110 | - |
L-glutamine | R73L mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli | |
193 | - |
glutamine | 5-phospho-alpha-D-ribose 1-diphosphate-independent glutamine hydrolysis | Escherichia coli | |
236 | - |
L-glutamine | D127A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | binding of 5-phospho-alpha-D-ribose 1-diphosphate activates the enzyme by a structural change that lowers the Km for glutamine 100fold and couples glutamine hydrolysis to synthesis of 5-phospho-beta-D-ribosylamine | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + H2O | - |
Escherichia coli | L-glutamate + NH3 | - |
? |