Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Protein Variants

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 36 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49A117S/F277I/Q324H/M381I/V443I/S470I t1/2 for the mutant enzyme at 60°C is 95fold higher than the t1/2 value for the wild-type enzyme -, 760410
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49A117S/Q324H/M381I/V443I/S470I t1/2 for the mutant enzyme at 60°C is 75fold higher than the t1/2 value for the wild-type enzyme -, 760410
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49A117S/Q324H/V443I/S470I t1/2 for the mutant enzyme at 60°C is 13.5fold higher than the t1/2 value for the wild-type enzyme -, 760410
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49A44T asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T 686131
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49G163D mutant is markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values 689022
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49G163S mutant markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values 689022
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49G488S clinical mutant G6PDFukaya, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type 696447
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49G488V clinical mutant G6PDCampinas, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type 696447
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49K18A the mutant with reduced catalytic efficiency shows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold) 741254
Show all pathways known for 1.1.1.49Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.49K18A/R50A the mutant shows almost no activity 741254
Results 1 - 10 of 36 > >>