Protein Variants | Comment | Organism |
---|---|---|
C228S | the kinetic and allosteric properties of the mutant enzyme in which Ser replaces Cys219 or Cys228 are the same as those described for the wild-type enzyme. The same result is obtained with the double mutation | Escherichia coli |
Y121T | while the wild-type enzyme behaves as a classical allosteric K-system which can be described by the allosteric concerted model, the mutant forms Y121T and Y121W present an asymmetric behaviour towards the allosteric activator, which can be described as two distinct half-of-the-sites allosteric activation steps occuring with different affinities for the N-acetyl-D-glucosamine 6-phosphate | Escherichia coli |
Y121W | while the wild-type enzyme behaves as a classical allosteric K-system which can be described by the allosteric concerted model, the mutant forms Y121T and Y121W present an asymmetric behaviour towards the allosteric activator, which can be described as two distinct half-of-the-sites allosteric activation steps occuring with different affinities for the N-acetyl-D-glucosamine 6-phosphate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.67 | - |
D-glucosamine 6-phosphate | pH 8.0, 30°C, mutant enzyme Tyr121Trp | Escherichia coli | |
2.01 | - |
D-glucosamine 6-phosphate | pH 8.0, 30°C, wild-type enzyme | Escherichia coli | |
2.6 | - |
D-glucosamine 6-phosphate | pH 8.0, 30°C, mutant enzyme Tyr121Thr | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-fructose 6-phosphate + NH3 | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia coli |