Activating Compound | Comment | Organism | Structure |
---|---|---|---|
N-acetylglucosamine 6-phosphate | - |
Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
Y254F | the mutant is less active than wild-type enzyme, the replacement causes an uncoupling of the homotropic and heterotrophic effects | Escherichia coli |
Y254T | the mutation results in pure K-system with a similar catalytic activity to that of the wild-type enzyme, mutant displays kcat values similar to the wild-type enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type enzyme and two mutants | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-fructose 6-phosphate + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | enzyme is a dimer of trimers | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
11.4 | - |
D-glucosamine 6-phosphate | pH 7.7, 30°C, mutant enzyme Y254F | Escherichia coli | |
75 | - |
D-glucosamine 6-phosphate | pH 7.7, 30°C, mutant enzyme Y254F in presence of N-acetylglucosamine 6-phosphate | Escherichia coli | |
218 | - |
D-glucosamine 6-phosphate | pH 7.7, 30°C, mutant enzyme Y254T | Escherichia coli | |
248 | - |
D-glucosamine 6-phosphate | pH 7.7, 30°C, mutant enzyme Y254T in presence of N-acetylglucosamine 6-phosphate | Escherichia coli | |
292 | - |
D-glucosamine 6-phosphate | pH 7.7, 30°C, wild-type enzyme | Escherichia coli | |
320 | - |
D-glucosamine 6-phosphate | pH 7.7, 30°C, wild-type enzyme in presence of N-acetylglucosamine 6-phosphate | Escherichia coli |