EC Number |
Protein Variants |
Reference |
---|
2.6.1.16 | A38T |
mutant shows increased resistance against glucosamine-6-phosphate |
672444 |
2.6.1.16 | A594G |
site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l) |
-, 758961 |
2.6.1.16 | A602L |
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 | biotechnology |
the recombinant enzyme expressed in Saccharomyces cereviaise reveals some differences from the wild type enzyme, such as improved stability and less sensitivity to UDP-GlcNAc |
739575 |
2.6.1.16 | C1A |
C1A-GlmS does not reveal glutaminase activity at 37°C when tested in the presence of Gln only |
721419 |
2.6.1.16 | C1A |
the structure of the inactive C1A mutant, crystallized in the presence of D-fructose 6-phosphate and Gln is deterimined. The C1A-GlmS structure is organized as a hexamer. The enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer |
722779 |
2.6.1.16 | G40A |
mutant with exchanged guanine is inactive. The 2.7 A resolution crystal structure of the mutant shows that the RNA is in a conformation nearly identical to that of the wild-type glmS ribozyme. The experimental electron density maps indicate that GlcN6P binds to the G40A mutant in the same location as in the wild-type ribozyme. Raman pH titrations of GlcN6P using crystals of the G40A mutant glmS ribozyme show that the pKa of the amine of the ribozyme-bound GlcN6P differs substantially for the wild-type and G40A mutant ribozymes |
722453 |
2.6.1.16 | G471S |
mutant shows increased resistance against glucosamine-6-phosphate |
672444 |
2.6.1.16 | I271T |
mutant shows increased resistance against glucosamine-6-phosphate |
672444 |
2.6.1.16 | I3T |
mutant shows increased resistance against glucosamine-6-phosphate |
672444 |