EC Number   |
Protein Variants |
Reference |
|---|
    2.6.1.16 | S596F |
site-directed mutagenesis, the mutant shows slightly increased activity (7 U/l) compared to wild-type (5 U/l) |
-, 758961 |
| 2.6.1.16 | V597R |
site-directed mutagenesis, the mutant shows slightly increased activity (8 U/l) compared to wild-type (5 U/l) |
758961 |
| 2.6.1.16 | V605L |
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure |
673687 |
| 2.6.1.16 | V711F |
mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities |
671896 |
| 2.6.1.16 | V711F |
reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities |
671896 |
| 2.6.1.16 | W74A |
efficiency of ammonia transfer is close to zero. No use of ammonia as a substrate |
673687 |
| 2.6.1.16 | W74A |
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure |
673687 |
| 2.6.1.16 | W74F |
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure |
673687 |
| 2.6.1.16 | W74L |
decrease in ammonia transfer, 5-7fold increase in the affinity for glutamine in the presence of fructose 6-phosphate |
673687 |
| 2.6.1.16 | W74L |
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure |
673687 |
