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Results 1 - 10 of 34 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16A38T mutant shows increased resistance against glucosamine-6-phosphate 672444
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16A594G site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l) -, 758961
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16A602L 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
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16biotechnology 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
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16C1A C1A-GlmS does not reveal glutaminase activity at 37°C when tested in the presence of Gln only 721419
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16C1A 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
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16G40A 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
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16G471S mutant shows increased resistance against glucosamine-6-phosphate 672444
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16I271T mutant shows increased resistance against glucosamine-6-phosphate 672444
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16I3T mutant shows increased resistance against glucosamine-6-phosphate 672444
Results 1 - 10 of 34 > >>